Monoclonal antibody directed to reticulocyte-binding protein homologue 5 (PFRH5)

Abstract

The present invention relates to antibodies for treatment or prevention of malaria.

Description

[0001]MONOCLONAL ANTIBODY This invenƟon was made with government support under Subcontracts No: P010223041 and 01706927 awarded by United States Agency for InternaƟonal Development (USAID). The government has certain rights in the invenƟon. FIELD OF THE INVENTION The present invenƟon relates to anƟbodies for treatment or prevenƟon of malaria. BACKGROUND OF THE INVENTION Malaria places the gravest public-health burden of all parasiƟc diseases, leading to ~215 million human clinical cases and ~620,000 deaths annually, with the majority of deaths in children. The infecƟon of red blood cells (RBCs) by the blood-stage form of the Plasmodium parasite is responsible for the clinical manifestaƟons of malaria. Examples of Plasmodium parasite include the species P. falciparum, P. vivax, P. ovale and P. malariae. The most virulent parasite species, P. falciparum, is endemic in large parts of sub-Saharan Africa and LaƟn America. It causes the majority of malaria deaths. It can infect RBCs of all ages and is not limited to immature RBCs. P. falciparum is therefore of parƟcular interest and is a major target for immuno-prophylaxis development (e.g., vaccines or anƟbody therapeuƟcs). The only malarial vaccine approved by the WHO for widespread use is RTS,S / AS01 (Mosquirix™), which is based on the RTS,S protein. The RTS,S protein acts by blocking infecƟon of P. falciparum in the liver. However, this vaccine has achieved only parƟal efficacy (~30-50% in phase II / III clinical trials). Previous studies have invesƟgated the potenƟal for anƟgens to induce anƟbodies which are effecƟve against blood-stage malaria parasites in vitro, using the standard growth inhibitory acƟvity (GIA) assay. One such anƟgen is apical membrane anƟgen 1 (PfAMA1). GIA assay invesƟgaƟons into other protein families involved in blood-stage Plasmodium parasite invasion of RBCs have found them to be ineffecƟve or less effecƟve than PfAMA1. PfAMA1 has therefore been a major focus of research on countering blood-stage malarial parasites, with numerous clinical trials. However, anƟbodies against PfAMA1 appear only to be effecƟve at an extremely high concentraƟon. In addiƟon, PfAMA1 induces strain-specific anƟbodies which are not effecƟve against geneƟcally diverse strains of the Plasmodium parasite (A. L. Goodman, S. J. Draper, Ann. Trop. Med. Parasitol. 104, 189 (2010)). In addiƟon, vaccine development has been hampered by the requirement for potenƟally reactogenic chemical adjuvants in addiƟon to the anƟgen to induce sufficient anƟbody responses in human subjects. Research has also been ongoing to idenƟfy other candidate malarial anƟgens for use as an anƟ-malarial immuno-prophylacƟc therapy. In parƟcular, the present inventors have previously idenƟfied ReƟculocyte-binding protein Homologue 5 (PfRH5) as a potenƟal anƟgen candidate for malarial vaccines (WO 2012 / 114125). The ReƟculocyte binding Homologue (PfRH) family comprises six members (PfRH1, PfRH2a, PfRH2b, PfRH3, PfRH4 and PfRH5), each of which is involved in the binding of the Plasmodium parasite to RBCs, with the possible excepƟon of PfRH3 which may be a non- expressed pseudogene. The PfRH family has been idenƟfied as adhesins on the surface of the merozoite form of the Plasmodium parasite, which bind to receptors on the surface of the erythrocyte and hence permit invasion of RBCs by the parasite in its blood-stage. The PfRH5 anƟgen has an approximate molecular weight of 63 KDa. In vitro cleaved fragments of approximately 45 KDa and 28 KDa have been reported. The present inventors have previously demonstrated that PfRH5 induces anƟbodies which are highly effecƟve in the GIA assay against the blood-stage Plasmodium falciparum parasite, and which neutralise parasites more effecƟvely than PfAMA1 and remain effecƟve at lower concentraƟons of immunoglobulin. In addiƟon, PfRH5 induces anƟbodies which are effecƟve against geneƟcally diverse strains of the Plasmodium parasite. Therefore, PfRH5 is a promising target anƟgen for an anƟ-malarial immuno-prophylacƟc. Earlier work by the present inventors has improved upon the full-length PfRH5 as a vaccine candidate by the development of raƟonally designed PfRH5 fragments, which contain regions or amino acid residues from within PfRH5 that give rise to protecƟve anƟbodies, whilst excluding other regions of the full-length PfRH5 sequence which may be associated with unwanted side effects. In addiƟon, raƟonally designed PfRH5 anƟgens have been developed with improved expression profiles and thermal stability without compromising immunological efficacy. However, currently, no monoclonal anƟbodies that target P. falciparum are licensed and no monoclonal anƟbodies that targeƟng a blood-stage malaria anƟgen are in clinical trials. There is therefore an urgent need for alternaƟve immuno-prophylacƟcs, such as a passively-transferred monoclonal anƟbody (mAb), which can protect against the disease-causing blood-stage Plasmodium parasite, potenƟally by emulaƟng natural immunity or by other immune mechanisms. In parƟcular, there is an ongoing need for the development of anƟbodies against PfRH5 with improved acƟvity. In parƟcular, there is a need for improved anƟbodies that are effecƟve at low concentraƟons. At the same Ɵme, it is necessary for said anƟbodies to be effecƟve against geneƟcally diverse strains of the Plasmodium parasite, with a view to future eliminaƟon campaigns, where they would be used alongside convenƟonal anƟmalarial drugs. The present invenƟon addresses one or more of the above needs by providing potent monoclonal anƟbodies against blood-stage P. falciparum. Each of the anƟbodies bind to PfRH5 which forms an essenƟal, non-redundant interacƟon with basigin on the erythrocyte cell surface. Directly interrupƟng this interacƟon or binding close to the interacƟon site prevents malaria invasion of the erythrocyte. SUMMARY OF THE INVENTION The present invenƟon provides an anƟ-PfRH5 anƟbody that specifically binds to a PfRH5 sequence (e.g., SEQ ID NO: 65 or 66), wherein the anƟbody binds to an epitope on PfRH5 but does not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely to the PfRH5 sequence; opƟonally wherein the anƟbody interacts with: one or more residues selected from the list consisƟng of: ILE 193, THR 199, GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, THR 216, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or one or more residues selected from the list consisƟng of: LYS 212, THR 216, LYS 219, VAL 220, LYS 327, ILE 328, and ASP 331 of SEQ ID NO: 65; and wherein said anƟbody does not interact with all the aforemenƟoned residues, and opƟonally wherein binding is determined by X-ray crystallography or cryo-electron microscopy (cryo-EM).. Also provided is: (a) an anƟ-PfRH5 anƟbody that specifically binds to a PfRH5 sequence comprising SEQ ID NO: 65, wherein the anƟbody binds to: one or more residues selected from the list consisƟng of: ILE 193, THR 199, GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, THR 216, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or one or more residues selected from the list consisƟng of: LYS 212, THR 216, LYS 219, VAL 220, LYS 327, ILE 328, and ASP 331 of SEQ ID NO: 65; and wherein said anƟbody does not interact with all the aforemenƟoned residues; (b) an anƟ-PfRH5 anƟbody that specifically binds to a disconƟnuous epitope consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338, LEU 339, GLU 341 and GLN 342 of SEQ ID NO: 65; (c) an anƟ-PfRH5 anƟbody that specifically binds to a disconƟnuous epitope consisƟng of: (a) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 85, SEQ ID NO: 86, SEQ ID NO: 81 and SEQ ID NO: 83; and (b) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 89 or SEQ ID NO: 90, SEQ ID NO: 82, SEQ ID NO: 84, SEQ ID NO: 87 and SEQ ID NO:88; and / or (d) an anƟ-PfRH5 anƟbody comprising a heavy chain or fragment thereof and a light chain or fragment thereof, wherein each of the heavy and light chains, or fragments thereof, comprise a variable region and said variable regions each comprise three CDR sequences; wherein: the heavy chain CDR sequences comprise SEQ ID NO: 1, 2 and 3, and the light chain CDR sequences comprise SEQ ID NO: 4, 5 and 6; the heavy chain CDR sequences comprise SEQ ID NO: 7, 8 and 9, and the light chain CDR sequences comprise SEQ ID NO: 10, 11 and 12; the heavy chain CDR sequences comprise SEQ ID NO: 13, 14 and 15, and the light chain CDR sequences comprise SEQ ID NO: 16, 17 and 18; the heavy chain CDR sequences comprise SEQ ID NO: 19, 20 and 21, and the light chain CDR sequences comprise SEQ ID NO: 22, 23 and 24; the heavy chain CDR sequences comprise SEQ ID NO: 25, 26 and 27 and the light chain CDR sequences comprise SEQ ID NO: 28, 29 and 30; or the heavy chain CDR sequences comprise SEQ ID NO: 31, 32 and 33, and the light chain CDR sequences comprise SEQ ID NO: 34, 35 and 36; (e) an anƟbody molecule or anƟgen-binding fragment thereof that competes for binding to PfRH5 with an anƟbody of the invenƟon or anƟgen-binding fragment thereof; (f) an anƟbody molecule or anƟgen-binding fragment thereof that binds to the same epitope as an anƟbody of the invenƟon or anƟgen-binding fragment thereof; (g) an isolated nucleic acid sequence, or pair of isolated nucleic acid sequences, encoding the heavy and / or the light chain(s) of an anƟbody of the invenƟon; opƟonally wherein the anƟbody comprises: a heavy chain comprising SEQ ID NO: 37 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 38 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 39 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 40 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 41 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 42 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 43 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 44 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 45 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 46 or a sequence having 80% sequence idenƟty thereto; or a heavy chain comprising SEQ ID NO: 47or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 48 or a sequence having 80% sequence idenƟty thereto; and / or (h) a vector or pair of vectors encoding the heavy and / or the light chain(s) of an anƟbody of the invenƟon; opƟonally wherein the anƟbody comprises: a heavy chain comprising SEQ ID NO: 37 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 38 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 39 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 40 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 41 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 42 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 43 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 44 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 45 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 46 or a sequence having 80% sequence idenƟty thereto; or a heavy chain comprising SEQ ID NO: 47or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 48 or a sequence having 80% sequence idenƟty thereto; (i) a vector or pair of vectors encoding the heavy and / or the light chain(s) of an anƟbody of the invenƟon; opƟonally wherein the anƟbody comprises: a heavy chain comprising SEQ ID NO: 37 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 38 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 39 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 40 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 41 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 42 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 43 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 44 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 45 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 46 or a sequence having 80% sequence idenƟty thereto; or a heavy chain comprising SEQ ID NO: 47 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 48 or a sequence having 80% sequence idenƟty thereto; (j) a host cell comprising an isolated nucleic acid sequence or pair of isolated nucleic acid sequences or a vector or pair of vectors of the invenƟon; (k) a composiƟon comprising one or more anƟbody or a vector or pair of vectors of the invenƟon and opƟonally comprising one or more of a pharmaceuƟcally acceptable excipient, diluent, or carrier; (l) an anƟbody, isolated DNA molecule, vector, or composiƟon of the invenƟon for use in therapy; (m) an anƟbody, isolated DNA molecule, vector, or composiƟon of the invenƟon for use in treaƟng and / or prevenƟng malaria; and (n) an anƟbody, isolated DNA molecule, vector, or composiƟon of the invenƟon for use as an immuno-prophylacƟc therapeuƟc, wherein the anƟbody has a growth inhibitory acƟvity (GIA) of at least 50% against the blood-stage Plasmodium parasite; wherein opƟonally: the growth inhibitory acƟvity (GIA) of at least 50% is against a plurality of geneƟc strains of the blood-stage Plasmodium parasite, preferably wherein the EC50 GIA value is less than 10 µg / mL; and / or the Plasmodium parasite is Plasmodium falciparum. DESCRIPTION OF FIGURES Figure 1. IsolaƟon of human monoclonal anƟbodies against RH5 240 human mAbs were isolated from vaccinees in a clinical trial and produced as recombinant IgG1 molecules. (A) Pictorial diagram showing the vaccinaƟon regimens and sampling of the Phase IIa clinical vaccine trial (ClinicalTrials.gov NCT02927145) from which monoclonal anƟbodies were isolated. (B) Pictorial diagram showing the IsolaƟon and expression of RH5-specific human monoclonal anƟbodies from peripheral blood mononuclear cells (PBMCs). Figure 2. Growth Inhibitory AcƟvity of R5.034-like mAbs All mAbs were screened for growth inhibiƟon acƟvity (GIA) against 3D7 clone Plasmodium falciparum. GIA has been shown to correlate with vaccine-induced protecƟon against P. falciparum blood-stage challenge in Aotus monkeys (2, 3) and a human challenge study (1). (A) EsƟmated concentraƟon for 50% growth inhibiƟon (EC50) of n=240 tested mAbs from the NCT02927145 clinical trial (1) and R5.016, the previous most potent anƟ-RH5 human mAb published (4). The six most potent mAbs (R5.034 and R5.034-like mAbs; R5.102, R5.159, R5.237, R5.268 and R5.270) are labelled, all have EC50values lower than 10 µg / mL. If a mAb EC50value could not be interpolated it was assigned a value of 10,000. (B) Four-parameter nonlinear regression model of mAb GIA tested in diluƟon series. Horizontal doƩed lines show the three GIA interpolaƟon values (30%, 50%, 80%). (C) Summary table of the interpolated EC values and their upper and lower 95% confidence limits. Figure 3. Epitope Binning of R5.034 and R5.034-like mAbs (A) AnƟbodies were compeƟƟon binned by HT-SPR on a Carterra LSA. mAbs were coupled as ligands onto a HC200M chip. A dendrogram is shown based on the compeƟƟon matrix. Branches are labelled with their epitope community number. Epitope bins are labelled under the corresponding bin, idenƟfied by a horizontal bar represenƟng idenƟcal compeƟƟon. Figure 4. Epitope CharacterisaƟon of R5.034 and R5.034-like mAbs. (A) Network plot based on mAb compeƟƟon values. Nodes represent mAbs. Square nodes represent mAbs that were excluded as ligands due to loss of acƟvity upon regeneraƟon. Solid lines indicate bidirecƟonal compeƟƟon between mAbs, doƩed lines represent unidirecƟonal compeƟƟon between mAbs. AnƟbodies are grouped by the epitope bin. A subset of anƟbodies in community 2, including epitope bin 2a which contains R5.016, compete with epitope bin 6 (R5.001). R5.034 and R5.034-like anƟbodies in epitope bin 2b do not compete with R5.001. (B) Network plot coloured by GIA EC50in µg / mL. Nodes coloured in red are potently neutralising. Epitope bin 2b is composed exclusively of potent clones. Figure 5. CharacterisaƟon of R5.034 and R5.034-like mAbs. (A) Summary table of the heavy and light chain variable region amino acid sequences of R5.034 and R5.034-like mAbs. (B) Summary table of the sequence characterisƟcs of R5.034 and R5.034-like mAbs, as well as R5.016 as a comparator. The amino acid sequences in A were annotated using the IMGT / V- QUEST program v3.5.31. (C) Isoaffinity plot of R5.034 and R5.034-like mAbs and other members of epitope community 2. Values were obtained by SPR. (D) KineƟc sensorgram of R5.034 determined by SPR, demonstraƟng its slow dissociaƟon constant. The black lines indicate the measured response while red lines indicate the curve fit. Graphs shows injecƟon of RH5.1 in a 3-fold diluƟon series with a top concentraƟon of 33.3 nM onto a captured R5.034 surface. Data fiƩed with a global Langmuir 1:1 interacƟon model. (E) CorrelaƟon of epitope 2 mAbs associaƟon constant and GIA EC50. The P value of a non-parametric two-tailed Spearman correlaƟon is shown. Figure 6: Assessment of intra-PfRH5 anƟbody synergy (A) Growth-inhibitory / neutralizing anƟbodies (nAbs) were tested at a final concentraƟon equivalent to their EC50 value, and non-nAbs were tested at a final concentraƟon of 0.3 mg / mL. The predicted Bliss addiƟvity % GIA was subtracted from the measured % GIA of the test anƟbody combinaƟon, and the difference is ploƩed as a percentage in the heatmap. Thresholds were used to categorize combinaƟons as synergisƟc (≥10%), addiƟve, or antagonisƟc (≥−10%). Test mAbs are annotated with their epitope bin assignment. (B) As for (A) except pairs of non-nAbs or mAbs with minimal GIA were combined. AnƟbodies were tested at a final concentraƟon of 0.2 mg / mL each. (C) GIA assay diluƟon curve of R5.028 (bin 3b) in combinaƟon with R5.246 (bin4b). AnƟbodies were combined in an equal raƟo and run in a 5-fold diluƟon curve starƟng from ∼1 mg / mL. Data were log transformed, and a four- parameter non-linear regression was ploƩed. The predicted Bliss addiƟvity % GIA of the mixture is shown as a dashed curve. A doƩed line is shown at 50% GIA for reference. (D) GIA assay diluƟon curves of the bin1a nAb R5.077 run in a 5-fold diluƟon starƟng from ∼0.5 mg / mL under various test condiƟons. Data were log transformed, and a four-parameter non-linear regression was ploƩed. For each curve, a non-nAb (R5.028 from bin 3b or R5.246 from bin 4b) or a combinaƟon of both non-nAbs was added at a fixed concentraƟon of 0.2 mg / mL each. Predicted Bliss addiƟvity GIA curves for each combinaƟon are shown as a dashed line. The black doƩed line indicates 80% GIA. The red doƩed line indicates the level of GIA measured alone for the fixed concentraƟon combinaƟon of the two non- nAbs (R5.028 + R5.246). (E) Same assay setup as in (D) except using R5.034 (bin 2b) in place of R5.077. (F) GIA assay diluƟon curves of total IgG purified from the sera of RH5.1 / AS01B vaccinees13 run in a 2- fold diluƟon starƟng from ∼14.4 mg / mL under various test condiƟons. PfRH5-specific IgG concentraƟon within the purified total IgG was determined by quanƟtaƟve ELISA13 and used to plot the data on the x axis. Data were also log transformed, and a four-parameter non-linear regression was ploƩed. For each curve, a non-nAb (R5.028 from bin 3b or R5.246 from bin 4b) or a combinaƟon of both non-nAbs was added at a fixed concentraƟon of 0.2 mg / mL each. Predicted Bliss addiƟvity GIA curves for each combinaƟon are shown as a dashed line. The black doƩed line indicates 80% GIA. The red doƩed line indicates the level of GIA measured alone for the fixed concentraƟon combinaƟon of the two non-nAbs (R5.028 + R5.246). Figure 7: Structure of R5.034 and efficacy against P. falciparum challenge (A) Crystal structure of PfRH5 using RH5ΔNL protein in complex with R5.034 Fv region. The image is of a top-down view, Ɵlted 10° along the x axis to view the binding interface on PfRH5 as predicted by PDBePISA. Common PfRH5 polymorphisms are annotated. CDR loops in the R5.034 structure are labeled with their IMGT idenƟfier. Residues in the IGHV and IGLV regions that are mutated from germ line are noted. (B) Structure of PfRH5 and R5.034 modelled Fab aligned with the epitope bin2 Fabs of 9AD4 (PDB: 4U0R)20 and R5.016 (PDB: 6RCU) and the basigin ectodomain with transmembrane helix (PDB: 7CKR). An AlphaFold predicƟve model of R5.034 Fab was aligned with the experimentally observed R5.034 Fv structure to hypothesize the spaƟal arrangement of the three anƟbodies. (C) Steady-state affinity, as assessed using SPR, of the R5.034 and R5.034LS mAb binding to human FcRn at pH 6.0. Sensorgrams are shown of a 9-step diluƟon curve beginning at the indicated concentraƟon of mAb. (D) TitraƟon of the R5.034 and R5.034LS mAbs in the assay of GIA against 3D7 clone P. falciparum parasites. Dots show the mean and error bars the range of n = 3 triplicate test wells per test mAb concentraƟon. Non-linear regression curve is shown. Figure 8: X-ray crystallography model of R5.034 Fv region bound to RH5 (PDB ID:8QKS) X-ray crystallography model of R5.034 Fv region bound to RH5 (PDB ID:8QKS) aligned with a model of R5.016 bound to RH5 (PDB ID:6RCV). (A-B) Unique interfacing residues on RH5 from the R5.016:RH5 structure are colored in red. (B) A plane intersecƟng the R5.016 or R5.034 heavy and light chains is shown to demonstrate the disƟnct angles of approach employed by the two anƟbodies. (C) The same structure is shown as in (A-B) but the R5.016 Fv has been omiƩed. RH5 residues predicted to form part of the RH5:R5.034 interface are shown. R5.034 heavy and light chain residues predicted to form part of the RH5:R5.034 interface are shown. CDR loops were idenƟfied through IMGT / V-QUEST and are labelled. Figure 9: Clustal sequence alignment of R5.034 and R5.034-like anƟbodies (A) Clustal sequence alignment of R5.034 and R5.034-like anƟbodies and the respecƟve germline heavy and light chain. Residues boxed in light grey are predicted to be part of the R5.034:RH5 interface. Residues coloured dark grey are mutated from the germline sequence. (B) Table of interfacing residues. DETAILED DESCRIPTION OF THE INVENTION DefiniƟons Unless defined otherwise, all technical and scienƟfic terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this disclosure belongs. Singleton, et al., DICTIONARY OF MICROBIOLOGY AND MOLECULAR BIOLOGY, 20 ED., John Wiley and Sons, New York (1994), and Hale & Marham, THE HARPER COLLINS DICTIONARY OF BIOLOGY, Harper Perennial, NY (1991) provide the skilled person with a general dicƟonary of many of the terms used in this disclosure. The meaning and scope of the terms should be clear; however, in the event of any latent ambiguity, definiƟons provided herein take precedent over any dicƟonary or extrinsic definiƟon. It should be understood that this invenƟon is not limited to the parƟcular methodology, protocols, and reagents, etc., described herein and as such can vary. The descripƟon of embodiments of the disclosure is not intended to be exhausƟve or to limit the disclosure to the precise form disclosed. While specific embodiments of, and examples for, the disclosure are described herein for illustraƟve purposes, various equivalent modificaƟons are possible within the scope of the disclosure, as those skilled in the relevant art will recognize. For example, while method steps or funcƟons are presented in a given order, alternaƟve embodiments may perform funcƟons in a different order, or funcƟons may be performed substanƟally concurrently. The teachings of the disclosure provided herein can be applied to other procedures or methods as appropriate. The various embodiments described herein can be combined to provide further embodiments. Aspects of the disclosure can be modified, if necessary, to employ the composiƟons, funcƟons and concepts described herein to provide yet further embodiments of the disclosure. Moreover, due to biological funcƟonal equivalency consideraƟons, some changes can be made in protein structure without affecƟng the biological or chemical acƟon in kind or amount. These and other changes can be made to the disclosure in light of the detailed descripƟon. All such modificaƟons are intended to be included within the scope of the appended claims. The headings provided herein are not limitaƟons of the various aspects or embodiments of this disclosure. As used herein, the term "capable of' when used with a verb, encompasses, or means the acƟon of the corresponding verb. For example, "capable of interacƟng" also means interacƟng, "capable of cleaving" also means cleaves, "capable of binding" also means binds and "capable of specifically targeƟng…" also means specifically targets. Numeric ranges are inclusive of the numbers defining the range. Where a range of values is provided, it is understood that each intervening value, to the tenth of the unit of the lower limit unless the context clearly dictates otherwise, between the upper and lower limits of that range is also specifically disclosed. Each smaller range between any stated value or intervening value in a stated range and any other stated or intervening value in that stated range is encompassed within this disclosure. The upper and lower limits of these smaller ranges may independently be included or excluded in the range, and each range where either, neither or both limits are included in the smaller ranges is also encompassed within this disclosure, subject to any specifically excluded limit in the stated range. Where the stated range includes one or both of the limits, ranges excluding either or both of those included limits are also included in this disclosure. As used herein, the arƟcles "a" and “an” may refer to one or to more than one (e.g. to at least one) of the grammaƟcal object of the arƟcle. Further, unless otherwise required by context, singular terms shall include pluraliƟes and plural terms shall include the singular. In this applicaƟon, the use of "or" means "and / or" unless stated otherwise. Furthermore, the use of the term "including", as well as other forms, such as "includes" and "included", is not limiƟng. “About” may generally mean an acceptable degree of error for the quanƟty measured given the nature or precision of the measurements. Exemplary degrees of error are within 20 percent (%), typically, within 10%, and more typically, within 5% of a given value or range of values. Preferably, the term “about” shall be understood herein as plus or minus (±) 5%, preferably ± 4%, ± 3%, ± 2%, ± 1%, ± 0.5%, ± 0.1%, of the numerical value of the number with which it is being used. The term "consisƟng of'' refers to composiƟons, methods, and respecƟve components thereof as described herein, which are exclusive of any element not recited in that descripƟon of the invenƟon. As used herein the term "consisƟng essenƟally of'' refers to those elements required for a given invenƟon. The term permits the presence of elements that do not materially affect the basic and novel or funcƟonal characterisƟc(s) of that invenƟon (i.e. inacƟve or non-immunogenic ingredients). Embodiments described herein as “comprising” one or more features may also be considered as disclosure of the corresponding embodiments “consisƟng of” and / or “consisƟng essenƟally of” such features. ConcentraƟons, amounts, volumes, percentages, and other numerical values may be presented herein in a range format. It is also to be understood that such range format is used merely for convenience and brevity and should be interpreted flexibly to include not only the numerical values explicitly recited as the limits of the range but also to include all the individual numerical values or sub- ranges encompassed within that range as if each numerical value and sub-range is explicitly recited. A "vector" or "construct" (someƟmes referred to as gene delivery or gene transfer "vehicle") refers to a macromolecule or complex of molecules comprising a polynucleoƟde to be delivered to a host cell, either in vitro or in vivo. A vector can be a linear or a circular molecule. A vector of the invenƟon may be viral or non-viral. All disclosure herein in relaƟon vectors of the invenƟon applies equally to viral and non-viral vectors unless otherwise stated. All disclosure in relaƟon to viral vectors of the invenƟon applies equally and without reservaƟon to adenovirus vectors or pox virus vectors. As used herein, the term "plasmid", refers to a common type of non-viral vector. A plasmid is an extra-chromosomal DNA molecule separate from the chromosomal DNA which is capable of replicaƟng independently of the chromosomal DNA. Preferably a plasmid is circular and may be double-stranded. The terms "nucleic acid casseƩe”, “nucleic acid construct", "expression casseƩe" and "nucleic acid expression casseƩe" are used interchangeably to mean a nucleic acid molecule that is capable of direcƟng transcripƟon. A nucleic acid casseƩe includes, at the least, a promoter, or a structure funcƟonally equivalent to a promoter and a nucleic acid sequence to be transcribed. Thus, a nucleic acid casseƩe includes, at the least, a promoter, or a structure funcƟonally equivalent to a promoter and a nucleic acid sequence encoding a protein of interest. In the present invenƟon, a nucleic acid casseƩe includes, at the least, a promoter, or a structure funcƟonally equivalent to a promoter, and a nucleic acid encoding a therapeuƟc protein. A nucleic acid casseƩe may include addiƟonal elements, such as an enhancer, and / or a transcripƟon terminaƟon signal. As used herein, the terms “transduced” and “modified” are used interchangeably to describe cells which have been modified to express a transgene of interest, parƟcularly an anƟgen as defined herein. Typically, the modificaƟon occurs through transducƟon of the cells. As used herein, the terms “Ɵtre” and “yield” are used interchangeably to mean the amount of viral vector produced by a method of the invenƟon. Amino acids are referred to herein using the name of the amino acid, the three-leƩer abbreviaƟon, or the single leƩer abbreviaƟon. Unless otherwise indicated, any nucleic acid sequences are wriƩen leŌ to right in 5' to 3' orientaƟon; amino acid sequences are wriƩen leŌ to right in amino to carboxy orientaƟon, respecƟvely. As used herein, the terms "protein" and "polypepƟde" are used interchangeably herein to designate a series of amino acid residues, connected to each other by pepƟde bonds between the alpha-amino and carboxyl groups of adjacent residues. The terms "protein", and "polypepƟde" refer to a polymer of amino acids, including modified amino acids (e.g., phosphorylated, glycated, glycosylated, etc.) and amino acid analogues, regardless of its size or funcƟon. "Protein" and "polypepƟde" are oŌen used in reference to relaƟvely large polypepƟdes, whereas the term "pepƟde" is oŌen used in reference to small polypepƟdes, but usage of these terms in the art overlaps. The terms "protein" and "polypepƟde" are used interchangeably herein when referring to a gene product and fragments thereof. Thus, exemplary polypepƟdes or proteins include gene products, naturally occurring proteins, homologs, orthologs, paralogs, fragments and other equivalents, variants, fragments, and analogues of the foregoing. As used herein, the terms “polynucleoƟdes”, "nucleic acid" and "nucleic acid sequence" refers to any molecule, preferably a polymeric molecule, incorporaƟng units of ribonucleic acid, deoxyribonucleic acid, or an analogue thereof. The nucleic acid can be either single-stranded or double-stranded. A single-stranded nucleic acid can be one nucleic acid strand of a denatured double- stranded DNA AlternaƟvely, it can be a single-stranded nucleic acid not derived from any double- stranded DNA. In one aspect, the nucleic acid can be DNA. In another aspect, the nucleic acid can be RNA Suitable nucleic acid molecules are DNA, including genomic DNA or cDNA. Other suitable nucleic acid molecules are RNA, including siRNA, shRNA, and anƟsense oligonucleoƟdes. The terms “transgene” and “gene” are also used interchangeably and both terms encompass fragments or variants thereof encoding the target protein, specifically an anƟgen of the invenƟon. Minor variaƟons in the amino acid sequences of the invenƟon are contemplated as being encompassed by the present invenƟon, providing that the variaƟons in the amino acid sequence(s) maintain at least 60%, at least 70%, more preferably at least 80%, at least 85%, at least 90%, at least 95%, and most preferably at least 97% or at least 99% sequence idenƟty to the amino acid sequence of the invenƟon or a fragment thereof as defined anywhere herein. The term homology is used herein to mean idenƟty. As such, the sequence of a variant or analogue sequence of an amino acid sequence of the invenƟon may differ on the basis of subsƟtuƟon (typically conservaƟve subsƟtuƟon) deleƟon or inserƟon. Proteins comprising such variaƟons are referred to herein as variants. Proteins of the invenƟon may include variants in which amino acid residues from one species are subsƟtuted for the corresponding residue in another species, either at the conserved or non- conserved posiƟons. Variants of protein molecules disclosed herein may be produced and used in the present invenƟon. Following the lead of computaƟonal chemistry in applying mulƟvariate data analysis techniques to the structure / property-acƟvity relaƟonships [see for example, Wold, et al. MulƟvariate data analysis in chemistry. Chemometrics-MathemaƟcs and StaƟsƟcs in Chemistry (Ed.: B. Kowalski); D. Reidel Publishing Company, Dordrecht, Holland, 1984 (ISBN 90-277-1846-6] quanƟtaƟve acƟvity- property relaƟonships of proteins can be derived using well-known mathemaƟcal techniques, such as staƟsƟcal regression, paƩern recogniƟon and classificaƟon [see for example Norman et al. Applied Regression Analysis. Wiley-lnterscience; 3rd ediƟon (April 1998) ISBN: 0471170828; Kandel, Abraham et al. Computer-Assisted Reasoning in Cluster Analysis. PrenƟce Hall PTR, (May 11, 1995), ISBN: 0133418847; Krzanowski, Wojtek. Principles of MulƟvariate Analysis: A User's PerspecƟve (Oxford StaƟsƟcal Science Series, No 22 (Paper)). Oxford University Press; (December 2000), ISBN: 0198507089; WiƩen, Ian H. et al Data Mining: PracƟcal Machine Learning Tools and Techniques with Java ImplementaƟons. Morgan Kaufmann; (October 11, 1999), ISBN:1558605525; Denison David G. T. (Editor) et al Bayesian Methods for Nonlinear ClassificaƟon and Regression (Wiley Series in Probability and StaƟsƟcs). John Wiley & Sons; (July 2002), ISBN: 0471490369; Ghose, Arup K. et al. Combinatorial Library Design and EvaluaƟon Principles, SoŌware, Tools, and ApplicaƟons in Drug Discovery. ISBN: 0- 8247-0487-8]. The properƟes of proteins can be derived from empirical and theoreƟcal models (for example, analysis of likely interfacing residues or calculated physicochemical property) of proteins sequence, funcƟonal and three-dimensional structures and these properƟes can be considered individually and in combinaƟon. Amino acids are referred to herein using the name of the amino acid, the three-leƩer abbreviaƟon, or the single leƩer abbreviaƟon. The term “protein", as used herein, includes proteins, polypepƟdes, and pepƟdes. As used herein, the term “amino acid sequence” is synonymous with the term “polypepƟde” and / or the term “protein”. In some instances, the term “amino acid sequence” is synonymous with the term “pepƟde”. The terms "protein" and "polypepƟde" are used interchangeably herein. In the present disclosure and claims, the convenƟonal one-leƩer and three-leƩer codes for amino acid residues may be used. The 3-leƩer code for amino acids as defined in conformity with the IUPACIUB Joint Commission on Biochemical Nomenclature (JCBN). It is also understood that a polypepƟde may be coded for by more than one nucleoƟde sequence due to the degeneracy of the geneƟc code. Amino acid residues at non-conserved posiƟons may be subsƟtuted with conservaƟve or non- conservaƟve residues. In parƟcular, conservaƟve amino acid replacements are contemplated. A “conservaƟve amino acid subsƟtuƟon” is one in which the amino acid residue is replaced with an amino acid residue having a similar side chain. Families of amino acid residues having similar side chains have been defined in the art, including basic side chains (e.g., lysine, arginine, or hisƟdine), acidic side chains (e.g., asparƟc acid or glutamic acid), uncharged polar side chains (e.g., glycine, asparagine, glutamine, serine, threonine, tyrosine, or cysteine), nonpolar side chains (e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, or tryptophan), beta-branched side chains (e.g., threonine, valine, isoleucine) and aromaƟc side chains (e.g., tyrosine, phenylalanine, tryptophan, or hisƟdine). Thus, if an amino acid in a polypepƟde is replaced with another amino acid from the same side chain family, the amino acid subsƟtuƟon is considered to be conservaƟve. The inclusion of conservaƟvely modified variants in a protein of the invenƟon does not exclude other forms of variant, for example polymorphic variants, interspecies homologs, and alleles. “Non-conservaƟve amino acid subsƟtuƟons” include those in which (i) a residue having an electroposiƟve side chain (e.g., Arg, His or Lys) is subsƟtuted for, or by, an electronegaƟve residue (e.g., Glu or Asp), (ii) a hydrophilic residue (e.g., Ser or Thr) is subsƟtuted for, or by, a hydrophobic residue (e.g., Ala, Leu, Ile, Phe or Val), (iii) a cysteine or proline is subsƟtuted for, or by, any other residue, or (iv) a residue having a bulky hydrophobic or aromaƟc side chain (e.g., Val, His, Ile or Trp) is subsƟtuted for, or by, one having a smaller side chain (e.g., Ala or Ser) or no side chain (e.g., Gly). “InserƟons” or “deleƟons” are typically in the range of about 1, 2, or 3 amino acids. The variaƟon allowed may be experimentally determined by systemaƟcally introducing inserƟons or deleƟons of amino acids in a protein using recombinant DNA techniques and assaying the resulƟng recombinant variants for acƟvity. This does not require more than rouƟne experiments for a skilled person. A “fragment” of a polypepƟde comprises at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 97% or more of the original polypepƟde. For example, a fragment may comprise at least 5, at least 10, at least 11, at least 12, at least 13, at least 14, at least 15, at least 16, at least 17, at least 18, at least 19, at least 20, at least 30, at least 40, at least 50, at least 60, at least 70, at least 80, at least 90, at least 100, at least 150, at least 200, at least 250, at least 300, at least 350, at least 400 or more amino acids of the protein from which it is derived. Preferably a fragment may comprise no more than 50, no more than 60, no more than 70, no more than 80, no more than 90, no more than 100, no more than 150, no more than 200, no more than 250, no more than 300, no more than 350, or no more than 400 amino acids of the protein from which it is derived. A fragment may be conƟnuous or disconƟnuous, preferably conƟnuous. The polynucleoƟdes of the present invenƟon may be prepared by any means known in the art. For example, large amounts of the polynucleoƟdes may be produced by replicaƟon in a suitable host cell. The natural or syntheƟc DNA fragments coding for a desired fragment will be incorporated into recombinant nucleic acid constructs, typically DNA constructs, capable of introducƟon into and replicaƟon in a prokaryoƟc or eukaryoƟc cell. Usually, the DNA constructs will be suitable for autonomous replicaƟon in a unicellular host, such as yeast or bacteria, but may also be intended for introducƟon to and integraƟon within the genome of a cultured insect, mammalian, plant or other eukaryoƟc cell lines. The polynucleoƟdes of the present invenƟon may also be produced by chemical synthesis, e.g., by the phosphoramidite method or the tri-ester method and may be performed on commercial automated oligonucleoƟde synthesizers. A double-stranded fragment may be obtained from the single stranded product of chemical synthesis either by synthesizing the complementary strand and annealing the strand together under appropriate condiƟons or by adding the complementary strand using DNA polymerase with an appropriate primer sequence. When applied to a nucleic acid sequence, the term “isolated” in the context of the present invenƟon denotes that the polynucleoƟde sequence has been removed from its natural geneƟc milieu and is thus free of other extraneous or unwanted coding sequences (but may include naturally occurring 5' and 3' untranslated regions such as promoters and terminators), and is in a form suitable for use within geneƟcally engineered protein producƟon systems. Such isolated molecules are those that are separated from their natural environment. In view of the degeneracy of the geneƟc code, considerable sequence variaƟon is possible among the polynucleoƟdes of the present invenƟon. Degenerate codons encompassing all possible codons for a given amino acid are set forth below: Amino Acid Codons Degenerate Codon Cys TGC TGT TGY Ser AGC AGT TCA TCC TCG TCT WSN Thr ACA ACC ACG ACT ACN Pro CCA CCC CCG CCT CCN Ala GCA GCC GCG GCT GCN Gly GGA GGC GGG GGT GGN Asn AAC AAT AAY Asp GAC GAT GAY Glu GAA GAG GAR Gln CAA CAG CAR His CAC CAT CAY Arg AGA AGG CGA CGC CGG CGT MGN Lys AAA AAG AAR Met ATG ATG Ile ATA ATC ATT ATH Leu CTA CTC CTG CTT TTA TTG YTN Val GTA GTC GTG GTT GTN Phe TTC TTT TTY Tyr TAC TAT TAY Trp TGG TGG Ter TAA TAG TGA TRR Asn / Asp RAY Glu / Gln SAR Any NNN One of ordinary skill in the art will appreciate that flexibility exists when determining a degenerate codon, representaƟve of all possible codons encoding each amino acid. For example, some polynucleoƟdes encompassed by the degenerate sequence may encode variant amino acid sequences, but one of ordinary skill in the art can easily idenƟfy such variant sequences by reference to the amino acid sequences of the present invenƟon. A “variant” nucleic acid sequence has substanƟal homology or substanƟal similarity to a reference nucleic acid sequence (or a fragment thereof). A nucleic acid sequence or fragment thereof is “substanƟally homologous” (or “substanƟally idenƟcal”) to a reference sequence if, when opƟmally aligned (with appropriate nucleoƟde inserƟons or deleƟons) with the other nucleic acid (or its complementary strand), there is nucleoƟde sequence idenƟty in at least about 70%, 75%, 80%, 85, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or more% of the nucleoƟde bases. Methods for homology determinaƟon of nucleic acid sequences are known in the art. AlternaƟvely, a “variant” nucleic acid sequence is substanƟally homologous with (or substanƟally idenƟcal to) a reference sequence (or a fragment thereof) if the “variant” and the reference sequence they are capable of hybridizing under stringent (e.g. highly stringent) hybridizaƟon condiƟons. Nucleic acid sequence hybridizaƟon will be affected by such condiƟons as salt concentraƟon (e.g. NaCl), temperature, or organic solvents, in addiƟon to the base composiƟon, length of the complementary strands, and the number of nucleoƟde base mismatches between the hybridizing nucleic acids, as will be readily appreciated by those skilled in the art. Stringent temperature condiƟons are preferably employed, and generally include temperatures in excess of 30°C, typically in excess of 37°C and preferably in excess of 45°C. Stringent salt condiƟons will ordinarily be less than 1000 mM, typically less than 500 mM, and preferably less than 200 mM. The pH is typically between 7.0 and 8.3. The combinaƟon of parameters is much more important than any single parameter. Methods of determining nucleic acid percentage sequence idenƟty are known in the art. By way of example, when assessing nucleic acid sequence idenƟty, a sequence having a defined number of conƟguous nucleoƟdes may be aligned with a nucleic acid sequence (having the same number of conƟguous nucleoƟdes) from the corresponding porƟon of a nucleic acid sequence of the present invenƟon. Tools known in the art for determining nucleic acid percentage sequence idenƟty include NucleoƟde BLAST (as described below). One of ordinary skill in the art appreciates that different species exhibit “preferenƟal codon usage”. As used herein, the term “preferenƟal codon usage” refers to codons that are most frequently used in cells of a certain species, thus favouring one or a few representaƟves of the possible codons encoding each amino acid. For example, the amino acid threonine (Thr) may be encoded by ACA, ACC, ACG, or ACT, but in mammalian host cells ACC is the most commonly used codon; in other species, different codons may be preferenƟal. PreferenƟal codons for a parƟcular host cell species can be introduced into the polynucleoƟdes of the present invenƟon by a variety of methods known in the art. IntroducƟon of preferenƟal codon sequences into recombinant DNA can, for example, enhance producƟon of the protein by making protein translaƟon more efficient within a parƟcular cell type or species. A “fragment” of a polynucleoƟde of interest comprises a series of consecuƟve nucleoƟdes from the sequence of said full-length polynucleoƟde. By way of example, a “fragment” of a polynucleoƟde of interest may comprise (or consist of) at least 600 consecuƟve nucleoƟdes from the sequence of said polynucleoƟde (e.g. at least 600, 650, 700, 750, 800850, 900, or 950 consecuƟve nucleic acid residues of said polynucleoƟde). Typically, a fragment as defined herein retains the same funcƟon as the full-length polynucleoƟde.The term "monoclonal anƟbody" (MAb) or "monoclonal anƟbody composiƟon", as used herein, refers to a populaƟon of anƟbody molecules that contain only one molecular species of anƟbody molecule consisƟng of a unique light chain gene product and a unique heavy chain gene product. In parƟcular, the complementarity determining regions (CDRs) of the monoclonal anƟbody are idenƟcal in all the molecules of the populaƟon. MAbs contain an anƟgen binding site capable of immunoreacƟng with a parƟcular epitope of the anƟgen characterized by a unique binding affinity for it. As used herein, the term "epitope" includes any protein determinant capable of specific binding to an immunoglobulin or fragment thereof, or a T-cell receptor. The term "epitope" includes any protein determinant capable of specific binding to an immunoglobulin or T-cell receptor. Epitopic determinants usually consist of chemically acƟve surface groupings of molecules such as amino acids or sugar side chains and usually have specific three-dimensional structural characterisƟcs, as well as specific charge characterisƟcs. The term "linear epitope" refers to an epitope with all of the points of interacƟon between the polypepƟde or protein and an anƟbody or anƟgen-binding fragment thereof occur linearly (conƟnuously) along the primary amino acid sequence of the protein or polypepƟde. Epitopes may be defined as structural or funcƟonal. FuncƟonal epitopes are generally a subset of the structural epitopes and have those residues that directly contribute to the affinity of the interacƟon. A "disconƟnuous epitope" (also referred to as a conformaƟonal epitope) refers to an epitope that comprises non-sequenƟal amino acids within a polypepƟde or protein, which come into proximity in the three-dimensional conformaƟon of the anƟgen. Unlike linear epitopes, which consist of conƟguous amino acids, disconƟnuous epitopes are formed by amino acids that are separated in the primary sequence but are brought together through the folding of the protein. In a conformaƟonal epitope, the points of interacƟon occur across amino acid residues that are separated from one another by at least one amino acid residue (disconƟnuous), i.e., the points of contact occur on disƟnct and separate regions of the anƟgen. Such epitopes are oŌen found on the surface of proteins and are recognized by anƟbodies that specifically interact with the conformaƟonal structure of the anƟgen rather than to a linear sequence. As described herein, the epitope(s) of RH5 bound by anƟbodies of the present invenƟon may be disconƟnuous epitopes. As used herein, the term “interfacing residues” refers to amino acid residues within an epitope or anƟgen-binding site of an anƟbody that interact when an anƟbody binds to its epitope. Thus, the “interfacing residues” of the epitope interact with the interfacing residues of the anƟgen-binding site of an anƟbody. Thus, interfacing residues form part of the anƟbody / anƟgen (anƟgen-binding site / epitope) interface. In other words, the interfacing residues of the epitope correspond to the structural epitope. Interfacing residues of an epitope may interact with those of the corresponding anƟgen-binding site of an anƟbody by contacƟng (e.g. forming part of the funcƟonal epitope), or may engage by some other means, e.g. by allowing the epitope to adopt the correct conformaƟon allowing binding by the anƟgen-binding site. Thus, the interfacing residues of an epitope (structural epitope) can comprise residues which contact residues within the anƟgen-binding site of an anƟbody (also referred to as contact residues). Contact residues may be idenƟfied / defined by a specific interacƟon distance and electron / EM density. As used herein, the term “interacƟng” refers to any form of molecular engagement between an anƟbody and its epitope. “InteracƟng” typically comprises the interacƟon of interfacing residues of the epitope and anƟgen-binding site, which can include contact between contact residues of the epitope and anƟgen-binding site. The term “binding” as used herein can be used to refer to the interacƟon of interfacing residues in an epitope and anƟgen-binding site (and hence to the interacƟon of a structural epitope with the anƟgen-binding site of an anƟbody), and / or to the interacƟon of contact residues in an epitope with an anƟgen-binding site. Thus, all disclosure herein of an anƟbody / anƟgen-binding site thereof interacƟng with one or more interfacing residues of an epitope could also be referred to as an anƟbody / anƟgen-binding site thereof binding to one or more interfacing residues of an epitope. Similarly, those disclosures apply equally and without reservaƟon to an anƟbody / anƟgen-binding site thereof interacƟng with / binding to one or more contact residues of an epitope. Methods of determining spaƟal conformaƟon of epitopes and well known in the art and may include, for example, X-ray crystallography, cryo-electron microscopy (cryo-EM), and nuclear magneƟc resonance (NMR) spectroscopy. Crystal structures can be determined at any appropriate resoluƟon, such as 3.2 Å and 4 Å. Suitable protocols for determining crystal structures at 3.2 Å and 4 Å are exemplified herein. See, e.g., X-ray crystallography protocols (BarreƩ, Jordan R et al. “Analysis of the diverse anƟgenic landscape of the malaria protein RH5 idenƟfies a potent vaccine-induced human public anƟbody clonotype.” Cell, S0092-8674(24)00655-X. 18 Jul. 2024, doi:10.1016 / j.cell.2024.06.015), NMR spectroscopy protocols (Valente, Ana P, and Mariana Manzano- Rendeiro. “Mapping conformaƟonal epitopes by NMR spectroscopy.” Current opinion in virology vol. 49 (2021): 1-6. doi:10.1016 / j.coviro.2021.04.001) and cryo-EM protocols (Turner et al. “Protocol for analyzing anƟbody responses to glycoprotein anƟgens using electron-microscopy-based polyclonal epitope mapping.” STAR protocols vol. 4,3 (2023): 102476. doi:10.1016 / j.xpro.2023.102476), which are herein incorporated by reference, and which provide exemplary X-ray crystallography protocols for determining whether an anƟbody binds to an epitope according to the invenƟon. Methods to determine whether an anƟbody "specifically interacts with one or more amino acids" within a parƟcular epitope (such as a disconƟnuous epitope) of a polypepƟde or protein are well known in the art. Determining whether an anƟbody specifically binds to an epitope, or one or more amino acids within an epitope, can be achieved using any method or combinaƟon of methods that are capable of analysing the interacƟon between the anƟbody and its anƟgen in a manner that takes into account the three-dimensional conformaƟon of the anƟgen. Such methods may include, but are not limited to, structural, biochemical, or computaƟonal techniques that assess the spaƟal arrangement of amino acids involved in the binding interacƟon. Methods for determining the three-dimensional structure of an anƟgen-anƟbody complex can be employed to show or determine that an anƟbody specifically binds to a disconƟnuous epitope and are well known in the art. These methods may include, but are not limited to, structural techniques such as X-ray crystallography, cryo-electron microscopy (cryo-EM), and nuclear magneƟc resonance (NMR) spectroscopy. Such structural analyses can be complemented by computaƟonal modelling or docking simulaƟons, which predict or confirm the anƟbody's binding conformaƟon. By way of a further non-limiƟng example, epitope mapping may be used for determining the specific regions of an anƟgen that are recognized by an anƟbody. These methods may include, but are not limited to, pepƟde scanning, hydrogen-deuterium exchange mass spectrometry (HDX-MS), site-directed mutagenesis, and structural analysis techniques such as X-ray crystallography or cryo-electron microscopy. By way of non-limiƟng example, as described in the Examples herein, epitope binning can be performed using high-throughput surface plasmon resonance (HT-SPR), such as on a Carterra LSA system or Biacore apparatus. AnƟbodies are coupled to a chip, and the anƟgen (such as RH5.1) is injected to assess the binding interacƟons with various anƟbodies. CompeƟƟon profiles can be generated, and heat maps or dendrograms may be used to idenƟfy disƟnct epitope communiƟes and bins, indicaƟng which anƟbodies share similar or disƟnct binding sites. This approach, which is well within the capabiliƟes of a skilled arƟsan, enables the precise definiƟon of the specific epitope or footprint on the anƟgen to which the anƟbodies bind. AlternaƟvely, or addiƟonally, by way of further non-limiƟng example according to the present disclosure, network plots based on observed compeƟƟon values may be generated to disƟnguish between different epitope bins, such as the disƟncƟon between R5.034-like mAbs in bin 2b and R5.016 in bin 2a. Such methods allow for the precise determinaƟon of how different anƟbodies bind to conformaƟonal epitopes. Binding of an anƟbody to PfRH5 can be quanƟfied by the dissociaƟon constant (KD) of the anƟbody for PfRH5. KDis a quanƟtaƟve measure used to describe the affinity between two molecules, typically a ligand and a receptor or an enzyme and a substrate. It represents the equilibrium constant for the dissociaƟon reacƟon, where a complex formed between the two molecules dissociates into its individual components. A lower dissociaƟon constant indicates a stronger binding affinity between the molecules, meaning that they are more likely to remain in complex form at equilibrium. Conversely, a higher dissociaƟon constant indicates weaker binding and a greater tendency for the complex to dissociate into its individual components. KDcan be measured accurately using known methods such as Surface Plasmon Resonance (SPR) or Bio-Layer Interferometry (BLI). The KDmeasurements (binding affinity) may be carried out by any suitable assay known in the art. Suitable assays include an affinity assay performable via a KinExA system (e.g., KinExA 3100, KinExA 3200, or KinExA 4000) (Sapidyne Instruments, Idaho), or ForteBio Octet system. The SPR technique is described in the Examples herein. In parƟcular, the binding affinity of anƟbodies to a disconƟnuous epitope can be assessed using SPR as illustrated in Example 5, where the dissociaƟon constants of R5.034 and R5.034-like mAbs were measured. Bio-layer interferometry (BLI) is a biophysical technique that operates on the principle of opƟcal interference between white light reflected from two surfaces: a layer of immobilized protein and an internal reference layer. In BLI, a ligand immobilized on the biosensor Ɵp surface binds with an analyte in soluƟon, causing an increase in opƟcal thickness at the biosensor Ɵp. This change leads to a shiŌ in the interference paƩern, which is measured in nanometers. The wavelength shiŌ (Δλ) directly correlates with the alteraƟon in opƟcal thickness of the biological layer. By tracking this shiŌ over Ɵme and ploƫng it against Ɵme, a classic associaƟon / dissociaƟon curve is generated. BLI enables real-Ɵme monitoring of binding specificity, associaƟon rate, dissociaƟon rate, and concentraƟon with excepƟonal precision and accuracy. Thus, the binding affinity of anƟbodies to a disconƟnuous epitope can be assessed using BLI as illustrated in Example 7. The correlaƟon between binding affinity and anƟbody potency can be further explored by ploƫng associaƟon rates against funcƟonal efficacy (e.g., GIA EC50), as demonstrated in the Examples. Moreover, in further non-limiƟng examples, techniques such as mutagenesis, wherein individual amino acids are systemaƟcally altered, can be used to confirm the involvement of non- adjacent residues in anƟbody binding. For example, site-directed mutagenesis may be performed to subsƟtute specific amino acids within the suspected epitope region, followed by assessing the anƟbody’s binding affinity. A significant reducƟon or loss of binding upon mutaƟon of non-conƟguous residues would indicate that the anƟbody is targeƟng an epitope (e.g a disconƟnuous epitope). AlternaƟvely, conformaƟonal sensiƟvity assays, where the anƟgen is denatured or structurally altered, can be conducted to determine if the anƟbody's binding capability is dependent on the naƟve three- dimensional structure of the anƟgen, further suggesƟng that the epitope is disconƟnuous. Preferably, X-ray crystallography or cry-EM are used to determine an epitope of the invenƟon. Suitable techniques are described in the examples herein. Crystal structures can be determined at any appropriate resoluƟon, such as 3.2 Å and 4 Å. Suitable protocols for determining crystal structures at 3.2 Å and 4 Å are exemplified herein. CompeƟƟon may be defined as the ability of an anƟbody or anƟgen-binding fragment thereof to compeƟƟvely inhibit the binding of an anƟbody or anƟgen-binding fragment thereof to PfRH5 in a staƟsƟcally significant manner. The ability of an anƟbody or anƟgen-binding fragment thereof to bind to the same epitope or compete for binding to PfRH5 with an anƟbody or anƟgen-binding fragment thereof of the disclosure can be readily determined by one of ordinary skill in the art without undue burden. Examples of suitable compeƟƟon assays are known in the art, including compeƟƟon binding ELISA, compeƟƟon binding assessed by BLI, compeƟƟon binding assed by SPR (e.g. with a Biacore) and high throughput SPR compeƟƟon binding analysis, e.g. with a Carterra-LSA .By way of further example, to determine if a test anƟbody competes with a reference anƟ-PfRH5 anƟbody of the disclosure, the reference anƟbody is allowed to bind to a PfRH5 protein or pepƟde under saturaƟng condiƟons. Next, the ability of a test anƟbody to bind to the PfRH5 protein molecule is assessed. If the test anƟbody is able to bind to PfRH5 following saturaƟon binding with the reference anƟ-PfRH5 anƟbody, it can be concluded that the test anƟbody binds to a different epitope than the reference anƟ-PfRH5 anƟbody. On the other hand, if the test anƟbody is not able to bind to the PfRH5 protein following saturaƟon binding with the reference anƟ-PfRH5 anƟbody, then the test anƟbody may bind to the same epitope as the epitope bound by the reference anƟ-PfRH5 anƟbody of the disclosure. As will be appreciated by a person of ordinary skill in the art, an anƟbody that competes for binding with a reference anƟbody may not necessarily bind to the idenƟcal epitope as the reference anƟbody but may sterically block binding of the reference anƟbody by binding an overlapping or adjacent epitope. CompeƟƟon between anƟbodies may be assayed easily in vitro, for example by tagging a specific reporter molecule to one anƟbody which can be detected in the presence of other untagged anƟbodies, to enable idenƟficaƟon of anƟbodies which bind the same epitope or an overlapping epitope. CompeƟƟon may be determined for example using ELISA in which PfRH5 is immobilized to a plate and a first tagged or labelled anƟbody along with one or more other untagged or unlabelled anƟbodies is added to the plate. Presence of an untagged anƟbody that competes with the tagged anƟbody is observed by a decrease in the signal emiƩed by the tagged anƟbody. CompeƟƟon assays can also be used in epitope mapping. In one instance epitope mapping may be used to idenƟfy the epitope bound by an anƟbody which opƟonally may have opƟmized neutralizing and / or modulaƟng characterisƟcs. Such an epitope can be linear or disconƟnuous. In tesƟng for compeƟƟon, a pepƟde fragment of the anƟgen may be employed, especially a pepƟde including or consisƟng essenƟally of an epitope of interest. A pepƟde having the epitope sequence plus one or more amino acids at either end may be used. AnƟbodies according to the present disclosure may be such that their binding for anƟgen is inhibited by a pepƟde with or including the sequence given. For example, two anƟbodies may be considered to bind to the same or overlapping epitopes if an excess of one anƟbody compeƟƟvely inhibits (blocks) the binding of the other by a measurable percentage, typically 50%, 75%, 90%, or higher, as determined by a compeƟƟve binding assay. AlternaƟvely, two anƟbodies may be determined to bind to the same epitope if mutaƟons in the anƟgen that diminish or abolish the binding of one anƟbody similarly affect the binding of the other anƟbody. Examples of suitable compeƟƟon assays are known in the art, including compeƟƟon binding ELISA, compeƟƟon binding assessed by BLI, compeƟƟon binding assed by SPR (e.g. with a Biacore) and high throughput SPR compeƟƟon binding analysis, e.g. with a Carterra-LSA, or any of those as described herein. AddiƟonally, compeƟƟon of two anƟbodies and / or binding of two anƟbodies to the same or overlapping epitopes may be determined using assays which measure a biologic readout, for example the ability to prevenƟon of malaria invasion of the erythrocyte. The terms "decrease", "reduced", "reducƟon", or "inhibit" are all used herein to mean a decrease by a staƟsƟcally significant amount. The terms "reduce," "reducƟon" or "decrease" or "inhibit" typically means a decrease by at least 10% as compared to a reference level (e.g. the absence of a given treatment) and can include, for example, a decrease by at least about 10%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 98%, at least about 99% , or more. As used herein, "reducƟon" or "inhibiƟon" encompasses a complete inhibiƟon or reducƟon as compared to a reference level. "Complete inhibiƟon" is a 100% inhibiƟon (i.e. abrogaƟon) as compared to a reference level. The terms "increased", "increase", "enhance", or "acƟvate" are all used herein to mean an increase by a staƟcally significant amount. The terms "increased", "increase", "enhance", or "acƟvate" can mean an increase of at least 25%, at least 50% as compared to a reference level, for example an increase of at least about 50%, or at least about 75%, or at least about 80%, or at least about 90%, at least about 95%, or at least about 98%, or at least about 99%, or at least about 100%, or at least about 250% or more compared with a reference level, or at least about a 1.5-fold, or at least about a 2-fold, or at least about a 2.5-fold, or at least about a 3-fold, or at least about a 4-fold, or at least about a 5- fold or at least about a 10-fold increase, or any increase between 1.5-fold and 10-fold or greater as compared to a reference level. In the context of a yield or Ɵtre, an "increase" is an observable or staƟsƟcally significant increase in such level. The terms "individual”, "subject”, and "paƟent”, are used interchangeably herein to refer to a mammalian subject for whom diagnosis, prognosis, disease monitoring, treatment, therapy, and / or therapy opƟmisaƟon is desired. The mammal can be (without limitaƟon) a human, non-human primate, mouse, rat, dog, cat, horse, or cow. Preferably, the individual, subject, or paƟent is a human. An “individual” may be an adult, juvenile or infant. An “individual” may be male or female. A "subject in need" of treatment for a parƟcular condiƟon can be an individual having that condiƟon, diagnosed as having that condiƟon, or at risk of developing that condiƟon. A subject can be one who has been previously diagnosed with or idenƟfied as suffering from or having a condiƟon in need of treatment or one or more complicaƟons or symptoms related to such a condiƟon, and opƟonally, have already undergone treatment for a condiƟon as defined herein or the one or more complicaƟons or symptoms related to said condiƟon. AlternaƟvely, a subject can also be one who has not been previously diagnosed as having a condiƟon as defined herein or one or more or symptoms or complicaƟons related to said condiƟon. For example, a subject can be one who exhibits one or more risk factors for a condiƟon, or one or more or symptoms or complicaƟons related to said condiƟon or a subject who does not exhibit risk factors. As used herein, the term “healthy individual” refers to an individual or group of individuals who are in a healthy state, e.g. individuals who have not shown any symptoms of the disease, have not been diagnosed with the disease and / or are not likely to develop the disease e.g. malaria. Preferably said healthy individual(s) is not on medicaƟon affecƟng malaria and has not been diagnosed with any other disease. The one or more healthy individuals may have a similar sex, age, and / or body mass index (BMI) as compared with the test individual. ApplicaƟon of standard staƟsƟcal methods used in medicine permits determinaƟon of normal levels of expression in healthy individuals, and significant deviaƟons from such normal levels. Herein the terms “control” and “reference populaƟon” are used interchangeably. The term “pharmaceuƟcally acceptable” as used herein means approved by a regulatory agency of the Federal or a state government, or listed in the U.S. Pharmacopeia, European Pharmacopeia, or other generally recognized pharmacopeia The publicaƟons discussed herein are provided solely for their disclosure prior to the filing date of the present applicaƟon. Nothing herein is to be construed as an admission that such publicaƟons consƟtute prior art to the claims appended hereto. Disclosure related to the various methods of the invenƟon are intended to be applied equally to other methods, therapeuƟc uses or methods, the data storage medium or device, the computer program product, and vice versa. PfRH5 AnƟbodies The following definiƟons are generally applicable to all anƟbodies of the invenƟon discussed below. Epitopes As demonstrated in the Examples herein, the anƟ-PfRH5 anƟbodies of the invenƟon bind to an epitope in the vicinity of a 3-helical bundle of the PfRH5-fold, with the CDRH3 loop projecƟng toward a cleŌ created by the outermost two α helices. The anƟ-PfRH5 anƟbodies of the invenƟon bind to an epitope centred on the α3b helix. Binding of the anƟbodies of the invenƟon to this epitope does not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely to PfRH5. In other words, an anƟbody of the invenƟon typically does not compete for binding with an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely. The lack of compeƟƟon / cross-blocking can be determined using any appropriate technique described herein, such as surface plasmon resonance (SPR). Exemplary SPR methods are described in the Examples herein, parƟcularly in relaƟon to Examples 3 and 4. This epitope is present within full-length PfRH5 (e.g. SEQ ID NO: 65 and 66, and versions thereof lacking the signal pepƟde, such as SEQ ID NO: 77), and also within the empirically designed PfRH5 fragments described herein. Thus, this epitope is situated at the N-terminus of both the PfRH5ΔN fragment (which lacks the signal pepƟde (corresponding to residues 1 to 23 of SEQ ID NO: 65 or 66) and the flexible / disordered N-terminal region (corresponding to residues 24 to 139 or 24 to 159 (preferably 24 to 139) of SEQ ID NO: 65 or 66) of PfRH5), as exemplified by SEQ ID NOs: 67 to 70; and the PfRH5ΔNL fragment (which lacks both the signal pepƟde and flexible / disordered N-terminal region idenƟfied above and the flexible loop region corresponding to amino acid residues 248 to 296 of SEQ ID NO: 65 or 66), as exemplified by SEQ ID NOs: 71 to 74 and 78. Accordingly,, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of amino acids ILE 193 to VAL 220 and LYS 327 to GLN 342 of PfRH5, i.e. amino acids ILE 193 to VAL 220 and LYS 327 to GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). In parƟcular, the invenƟon provides an epitope corresponding to (comprising or consisƟng of) residues ILE 193 to VAL 220 and LYS 327 to GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). More parƟcularly, the epitope may comprise or consist of amino acid residues ILE 193, THR 199, GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, THR 216, LYS 219, VAL 220, LYS 327, ILE 328, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339 and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). The epitope may comprise or consist of amino acid residues ILE 193, THR 199, GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, THR 216, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339 and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78); and / or the epitope may comprise or consist of amino acid residues LYS 212, THR 216, LYS 219, VAL 220, LYS 327, ILE 328 and ASP 331 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). Accordingly, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of amino acids LYS 202 to LYS 219 and LYS 327 to GLN 342 of PfRH5, i.e. amino acids LYS 202 to LYS 219 and LYS 327 to GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). In parƟcular, the invenƟon provides an epitope corresponding to (comprising or consisƟng of) residues LYS 202 to LYS 219 and LYS 327 to GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). More parƟcularly, the epitope may comprise or consist of amino acid residues corresponding LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, LYS 327, ILE 328, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339 and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). The epitope may comprise or consist of amino acid residues LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78); and / or the epitope may comprise or consist of amino acid residues PHE 209, ILE 213, LYS 327, ILE 328, ASP 331, ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). Accordingly, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of amino acids LYS 202 to LYS 219 and ASN 326 to GLN 342 of PfRH5, i.e. amino acids ILE 193 to VAL 220 and LYS 327 to GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). In parƟcular, the invenƟon provides an epitope corresponding to (comprising or consisƟng of) residues LYS 202 to LYS 219 and ASN 326 to GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). More parƟcularly, the epitope may comprise or consist of amino acid residues corresponding to LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339 and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). The epitope may comprise or consist of amino acid residues LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78); and / or the epitope may comprise or consist of amino acid residues PHE 209 , ILE 213, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, ASN 334, TYR 335, and ASN 338, of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). Accordingly, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of amino acids LYS 202 to LYS 219 and ASN 323 to GLN 342 of PfRH5, i.e. amino acids LYS 202 to LYS 219 and ASN 323 to GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). In parƟcular, the invenƟon provides an epitope corresponding to (comprising or consisƟng of) residues LYS 202 to LYS 219 and ASN 323 to GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). More parƟcularly, the epitope may comprise or consist of amino acid residues corresponding to LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338, LEU 339, GLU 341 and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). The epitope may comprise or consist of amino acid residues LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, PHE 325, ASP 331, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78); and / or the epitope may comprise or consist of amino acid residues PHE 209, ILE 213, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338 and GLU 341 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). The invenƟon provides a disconƟnuous epitope which comprises or consists of at least 1, 2, 3, 4, 5, 6, 7, 8, or 9 interfacing residues corresponding to (comprising or consisƟng of) LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASN 326, ILE 328, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). In parƟcular, the epitope may comprise or consist of interfacing residues corresponding to LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASN 326, ILE 328, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). More parƟcularly, the epitope may comprise or consist of interfacing residues corresponding to LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASN 326, ILE 328, TYR 335, LEU 339, and GLN 342 (as above) and one or more amino acid residues corresponding to ALA 208, PHE 209, LYS 212, LYS 219, LYS 327, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). By way of example, the epitope may comprise or consist of interfacing residues corresponding to LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASN 326, ILE 328, TYR 335, LEU 339, and GLN 342 (as above) and amino acid residues corresponding to ALA 208, PHE 209, LYS 212, LYS 219, LYS 327, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). The epitope may comprise or consist of interfacing residues corresponding to LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASN 326, ILE 328, TYR 335, LEU 339, and GLN 342 (as above) and one or more amino acid residues corresponding to ALA 208, PHE 209, LYS 212, LYS 219, LYS 327, MET 330, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). By way of example, the epitope may comprise or consist of interfacing residues corresponding to LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASN 326, ILE 328, TYR 335, LEU 339, and GLN 342 (as above) and amino acid residues corresponding to ALA 208, PHE 209, LYS 212, LYS 219, LYS 327, MET 330, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). The invenƟon provides a disconƟnuous epitope which comprises or consists of at least 1, 2, 3, 4, 5, 6, 7, 8, or 9 interfacing residues corresponding to (comprising or consisƟng of) LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASP 324, PHE 325, ASN 326, ILE 328, LYS 333, TYR 335, THR 337, LEU 339, GLU 341 and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). In parƟcular, the epitope may comprise or consist of interfacing residues corresponding to LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASP 324, PHE 325, ASN 326, ILE 328, LYS 333, TYR 335, THR 337, LEU 339, GLU 341 and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). More parƟcularly, the epitope may comprise or consist of interfacing residues corresponding to LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASP 324, PHE 325, ASN 326, ILE 328, LYS 333, TYR 335, THR 337, LEU 339, GLU 341 and GLN 342 (as above) and one or more amino acid residues corresponding to ALA 208, PHE 209, LYS 212, LYS 219, ASN 323, LYS 327, MET 330, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). By way of example, the epitope may comprise or consist of interfacing residues corresponding to LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASP 324, PHE 325, ASN 326, ILE 328, LYS 333, TYR 335, THR 337, LEU 339, GLU 341 and GLN 342 (as above) and amino acid residues corresponding to ALA 208, PHE 209, LYS 212, LYS 219, ASN 323, LYS 327, MET 330, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). With regards to PfRH5 fragments, the numbering of the amino acids of the epitope may differ from the residues indicated above (as these are defined by reference to the full-length sequence of PfRH5, typically SEQ ID NO: 65 or 66). However, the corresponding residues within a PfRH5 fragment may be readily idenƟfied using only rouƟne skill and methods (e.g. sequence alignment). Indeed, by way of example, these epitopes are idenƟfied in the fragments of SEQ ID NOs: 67 to 74 or 78 in the sequence informaƟon secƟon herein. Typically, the epitopes described above give rise to anƟbodies of the invenƟon, such as those exemplified herein. Accordingly, in some embodiments, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of: (a) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 81, SEQ ID NO: 83, SEQ ID NO: 85 or SEQ ID NO: 86; and (b) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 82, SEQ ID NO: 84, SEQ ID NO: 87, SEQ ID NO:88, SEQ ID NO: 89 and SEQ ID NO: 90. For example, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of: (a) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 81 and SEQ ID NO: 83; and (b) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 82 and SEQ ID NO: 84. For example, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of: (a) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 85 and SEQ ID NO: 86; and (b) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 82 and SEQ ID NO: 84. For example, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of: (a) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 85 and SEQ ID NO: 86; and (b) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 87 and SEQ ID NO: 88. For example, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of: (a) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 85 and SEQ ID NO: 86; and (b) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 89 and SEQ ID NO: 90. In preferable embodiments, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 81 and (b) the amino acid sequence of SEQ ID NO: 82. In preferable embodiments, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 83 and (b) the amino acid sequence of SEQ ID NO: 84. In preferable embodiments, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 85 and (b) the amino acid sequence of SEQ ID NO: 82. In preferable embodiments, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 86 and (b) the amino acid sequence of SEQ ID NO: 84. In preferable embodiments, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 85 and (b) the amino acid sequence of SEQ ID NO: 87. In preferable embodiments, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 86 and (b) the amino acid sequence of SEQ ID NO: 88. In preferable embodiments, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 85 and (b) the amino acid sequence of SEQ ID NO: 89. In preferable embodiments, the invenƟon provides a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 86 and (b) the amino acid sequence of SEQ ID NO: 90. It will be appreciated that an epitope may be determined using an appropriate technique, such as those described herein. In some embodiments an epitope of the invenƟon does not comprise or consist of one or more to ILE 193, THR 199, GLY 201, CYS 203, VAL 206, ASP 207, LYS 211, GLU 215 or VAL 220 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). In some embodiments an epitope of the invenƟon does not comprise or consist of any of ILE 193, THR 199, GLY 201, CYS 203, VAL 206, ASP 207, LYS 211, GLU 215 or VAL 220. of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). The invenƟon provides an epitope which may comprise or consist of ASN 323, ASP 324, PHE 325, ASN 326, MET 330, LYS 333, THR 337, and GLU 341 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). Any epitope herein may comprise these residues. A parƟcularly preferred epitope of the invenƟon may comprise or consist of LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338, LEU 339, GLU 341 and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). AnƟbodies The term "anƟbody", as used herein, broadly refers to any immunoglobulin (Ig) molecule comprised of four polypepƟde chains, two heavy (H) chains and two light (L) chains, or any funcƟonal fragment, mutant, variant, or derivaƟon thereof, which retains the essenƟal epitope binding features of an Ig molecule. Such mutant, variant, or derivaƟve anƟbody enƟƟes are known in the art, non- limiƟng embodiments of which are discussed below. In a full-length anƟbody, each heavy chain is comprised of a heavy chain variable region (abbreviated herein as VH) and a heavy chain constant region. The heavy chain constant region is comprised of three domains, CH1, CH2 and CH3. Each light chain is comprised of a light chain variable region (abbreviated herein as VL) and a light chain constant region. The light chain constant region is comprised of one domain, CL. The VH and VL regions can be further subdivided into regions of hypervariability, termed complementarity determining regions (CDR), interspersed with regions that are more conserved, termed framework regions (FR). Each VH and VL is composed of three CDRs and four FRs, arranged from amino-terminus to carboxy-terminus in the following order: FR1, CDR1, FR2, CDR2, FR3, CDR3, FR4. AnƟbodies may be polyclonal (pAb) or monoclonal (mAb). Typically, the anƟbodies of the invenƟon are mAbs. AnƟbodies of the invenƟon can be of any type (e.g., IgG, IgE, IgM, IgD, IgA and IgY), class (e.g., IgG1, IgG2, IgG3, IgG4, IgA1 and IgA2) or subclass and may be from any species (e.g., mouse, human, chicken, rat, rabbit, sheep, shark, and camelid). The term “anƟbody” may also encompass an "anƟgen-binding fragment" of an anƟbody (or simply "binding fragment"). An “anƟgen binding fragment” or “binding fragment” refers to one or more fragments of an anƟbody that retain the ability to specifically bind to an anƟgen. It has been shown that the anƟgen-binding funcƟon of an anƟbody can be performed by one or more fragments of a full-length anƟbody. Single chain anƟbodies are also encompassed. Such anƟgen-binding fragments may also be bispecific, dual specific, or mulƟ-specific, specifically binding to two or more different anƟgens. Thus, examples of binding fragments encompassed within the term "anƟgen- binding fragment" of an anƟbody include Fab, Fv, scFv, dAb, Fd, Fab’ or F(ab’)2, tandem scFv and diabodies. Also encompassed are anƟbody constructs, defined as a polypepƟde comprising one or more the anƟgen binding fragment of the invenƟon linked to a linker polypepƟde or an immunoglobulin constant domain. Linker polypepƟdes comprise two or more amino acid residues joined by pepƟde bonds and are used to link one or more anƟgen binding porƟons. An anƟbody of the invenƟon may be a "human anƟbody”; defined as an anƟbody having variable and constant regions derived from human germline immunoglobulin sequences, but which may include amino acid residues not encoded by human germline immunoglobulin sequences (e.g., mutaƟons introduced by random or site-specific mutagenesis in vitro or by somaƟc mutaƟon in vivo), for example in the CDRs and in parƟcular CDR3. Recombinant human anƟbodies are also encompassed by the present invenƟon. An anƟbody molecule having one or more CDRs, e.g. a set of CDRs, within an anƟbody framework. For example, one or more CDRs or a set of CDRs of an anƟbody may be graŌed into a framework (e.g. human framework) to provide an anƟbody molecule. The CDRs or set of CDR sequences may be those of any anƟbody as described herein, such as those of the R5.034 anƟbody. The framework regions may be of human germline gene segment sequences. Thus, the framework may be germlined, whereby one or more residues within the framework are changed to match the residues at the equivalent posiƟon in the most similar human germline framework. Such anƟbodies of the invenƟon may be referred to as “germlined anƟbodies”, in which the framework regions are of human germline gene segment sequences. A skilled individual can choose a germline segment that closely resembles the framework sequence of the anƟbody prior to germlining and assess the affinity or acƟvity of the anƟbodies to ensure that germlining does not significantly diminish anƟgen binding or potency in the assays described here. Human germline gene segment sequences are readily available to those with experƟse in the field and can be obtained, for instance, from resources such as the VBASE compilaƟon (VBASE, MRC Centre of Protein Engineering, UK, 1997, hƩp / / mrc- cpe.cam.ac.uk). An anƟbody of the invenƟon may be a "chimeric anƟbody"; defined as an anƟbody which comprises heavy and light chain variable region sequences from one species and constant region sequences from another species. The present invenƟon encompasses chimeric anƟbodies having, for example, murine heavy and light chain variable regions linked to human constant regions. An anƟbody of the invenƟon may be a "CDR-graŌed anƟbody"; defined as an anƟbody which comprise heavy and light chain variable region sequences from one species but in which the sequences of one or more of the CDR regions of VH and / or VL are replaced with CDR sequences of another species, such as anƟbodies having murine heavy and light chain variable regions in which one or more of the murine CDRs (e.g., CDR3 or all three CDRs) has been replaced with human CDR sequences. An anƟbody of the invenƟon may be a "humanized anƟbody"; defined as an anƟbody which comprise heavy and light chain variable region sequences from a non-human species (e.g., a mouse) but in which at least a porƟon of the VH and / or VL sequence has been altered to be more "human- like", i.e., more similar to human germline variable sequences. One type of humanized anƟbody is a CDR-graŌed anƟbody, in which human CDR sequences are introduced into non-human VH and VL sequences to replace the corresponding nonhuman CDR sequences. The terms "Kabat numbering", "Kabat definiƟons and "Kabat labeling" are used interchangeably herein. These terms, which are recognized in the art, refer to a system of numbering amino acid residues which are more variable (i.e. hypervariable) than other amino acid residues in the heavy and light chain variable regions of an anƟbody, or an anƟgen binding porƟon thereof (Kabat et al. (1971) Ann. NY Acad, Sci. 190:382-391 and Kabat, E.A., et al. (1991) Sequences of Proteins of Immunological Interest, FiŌh EdiƟon, U.S. Department of Health and Human Services, NIH PublicaƟon No.91-3242). AnƟbodies of the invenƟon are not limited to a parƟcular method of generaƟon or producƟon. Thus, the invenƟon provides anƟbodies which have been manufactured from a hybridoma that secretes the anƟbody, as well as anƟbodies produced from a recombinantly produced cell that has been transformed or transfected with a nucleic acid or nucleic acids encoding the anƟbody. Such hybridomas, recombinantly produced cells, and nucleic acids form part of the invenƟon. An anƟbody, or anƟgen-binding fragment thereof, of the invenƟon is selecƟve or specific for PfRH5, or a parƟcular epitope of PfRH5 as described herein. By specific, it will be understood that the anƟbody binds to the molecule of interest, in this case the PfRH5 fragment of the invenƟon, with no significant cross-reacƟvity to any other molecule, parƟcularly any other protein. For example, a binding compound or anƟbody of the invenƟon that is specific for a parƟcular PfRH5 epitope of the invenƟon will show no significant cross-reacƟvity with other PfRH5 epitopes. As another example, a binding compound or anƟbody of the invenƟon that is specific for PfRH5 will show no significant cross- reacƟvity with other malarial invasion proteins. Cross-reacƟvity may be assessed by any suitable method. Cross-reacƟvity of a binding compound (e.g. anƟbody) for a PfRH5 epitope with another PfRH5 epitope or non-PfRH5 protein may be considered significant if the binding compound (e.g. anƟbody) binds to the other molecule at least 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90% or 100% as strongly as it binds to the PfRH5 epitope. A binding compound (e.g. anƟbody) that is specific for the PfRH5 fragment may bind to another molecule such as PfAMA1 at less than 90%, 85%, 80%, 75%, 70%, 65%, 60%, 55%, 50%, 45%, 40%, 35%, 30%, 25% or 20% the strength that it binds to the PfRH5 epitope. Preferably, the binding compound (e.g. anƟbody) binds to the other molecule at less than 20%, less than 15%, less than 10% or less than 5%, less than 2% or less than 1% the strength that it binds to the PfRH5 epitope. Binding affinity may be quanƟfied in any suitable way, e.g. by KD. The binding affinity of a PfRH5 anƟbody of the invenƟon for PfRH5 may be quanƟfied in terms of dissociaƟon constant (KD). KDmay be determined using any appropriate technique, but SPR is generally preferred in the context of the present invenƟon. A PfRH5 anƟbody of the invenƟon may bind to PfRH5 with a KDof less than 1μM, less than 100nM, less than 50nM, less than 25nM, less than 10nM, less than 1nM, less than 900pM, less than 800pM, less than 700pM, less than 600pM, less than 500pM, less than 400pM, less than 300pM, less than 200pM, less than 100pM, less than 50pM, less than 40pM, less than 30pM, less than 25pM, less than 10pM, less than 5pM, or less. Preferably, a PfRH5 anƟbody of the invenƟon may bind to PfRH5 with a KDof less than 5 nM, less than 1nM, less than 900pM, less than 800pM, less than 700pM, less than 600pM, less than 500pM, less than 400pM, less than 300pM, less than 200pM, less than 100pM, less than 50pM, or less than 40 pM. AlternaƟvely, a PfRH5 anƟbody of the invenƟon may bind to PfRH5 with a KDof from 30pM to 50nM, from 30pM to 40nM, from 30pM to 30nM, from 30pM to 20nM, from 30pm to 10nM, from 30pM to 5nM or from 30pM to 3.5nM. Preferably, a PfRH5 anƟbody of the invenƟon may bind to PfRH5 with a KDof from 30pM to 3.5nM.All the novel anƟbodies idenƟfied by the present inventors bind to the PfRH5ΔNL fragment. As indicated above, this fragment lacks both the signal pepƟde (corresponding to residues 1 to 23 of SEQ ID NO: 65); the flexible / disordered N-terminal region (corresponding to residues 24 to 139 or 24 to 159 (preferably 24 to 139) of SEQ ID NO: 65) of PfRH5) and the flexible loop region corresponding to amino acid residues 248 to 296 of SEQ ID NO: 65). The PfRH5ΔNL fragment is exemplified by any of SEQ ID NOs: 71-74 and 78, parƟcularly SEQ ID NO: 78. Notably, the PfRH5ΔNL fragment of SEQ ID NO: 78 lacks resides K33 to K51 of the full-length PfRH5 protein, which have previously been reported as the minimal PfP113 binding region, and which was thought to be a potenƟal site for anƟbody-mediated neutralisaƟon. The invenƟon provides anƟbodies and anƟgen-binding fragments thereof that bind to a novel epitope as described herein. In some preferred embodiments, the invenƟon provides anƟbodies and anƟgen-binding fragments thereof that bind to an epitope which comprises or consists of LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338, LEU 339, GLU 341 and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). Said anƟbodies and anƟgen-binding fragments thereof may interact with each of these interfacing residues. Binding of an anƟbody or binding fragment thereof to said epitope may be determined using any appropriate technique, such as those described herein, parƟcularly X-ray crystallography and / or cryo- EM. The invenƟon provides anƟbodies that bind to a novel epitope within RH5ΔNL as exemplified by SEQ ID NOs: 67 or 68. Typically the epitopes described above give rise to (induce) neutralising / growth inhibitory anƟbodies of the invenƟon, such as those exemplified herein. In parƟcular, the inventors idenƟfied an epitope bin (i.e., epitope bin 2b) which contain potent neutralising anƟbodies. AnƟ-PfRH5 anƟbodies within epitope bin 2b specifically bind to a PfRH5 sequence, wherein said anƟbodies bind to an epitope on PfRH5 but do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001) to the PfRH5 sequence. In some embodiments, anƟ-PfRH5 anƟbodies within epitope bin 2b specifically bind to a PfRH5 sequence, wherein said anƟbodies bind to an epitope on PfRH5 and cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 55 and SEQ ID NO: 56 respecƟvely (e.g., R5.016) to the PfRH5 sequence. In some embodiments, anƟ-PfRH5 anƟbodies within epitope bin 2b specifically bind to a PfRH5 sequence, wherein said anƟbodies bind to an epitope on PfRH5 and: (i) cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 55 and SEQ ID NO: 56 respecƟvely (e.g., R5.016); and (ii) do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001); to the PfRH5 sequence. AnƟbodies of the invenƟon (i.e., anƟbodies within epitope bin 2b) were found not to cross block the binding of anƟbody R5.001 to PfRH5. In contrast, anƟbody R5.016 (which is part of epitope bin 2a) was found to cross block the binding of R5.016, R5.034, R5.034-like anƟbodies and R5.001. Thus, one of the disƟnguishing features of anƟbodies of the invenƟon (e.g., anƟbodies of epitope bin 2b) compared to anƟbodies of epitope bin 2a is the fact that anƟbodies of the invenƟon do not cross block the binding of R5.001 to PfRH5. Thus, the present inventors have idenƟfied a novel epitope on PfRH5 which elicits anƟbodies which possess significant neutralising (i.e. growth inhibitory) acƟvity. In some embodiments, anƟbodies of the invenƟon bind to an RH5 epitope that parƟally overlaps with the epitope bound by a reference anƟbody, such an anƟbody comprising SEQ ID NO: 55 and SEQ ID NO: 56 (e.g., R5.016). Interfacing residues between the anƟbody of the invenƟon and RH5 (e.g., SEQ ID NO: 65), and / or a reference anƟbody (such as an anƟbody comprising SEQ ID NO: 55 and SEQ ID NO: 56) and RH5 can be determined using tools such as PDBePISA (Proteins, Interfaces, Structures and Assemblies) (hƩps: / / www.ebi.ac.uk / pdbe / pisa / ). Specifically, in some invenƟon interact with one or more residues selected from the GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, THR 216, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or one or more residues selected from the list consisƟng of: LYS 212, THR 216, LYS 219, VAL 220, LYS 327, ILE 328, and ASP 331 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). In preferred embodiments, anƟbodies of the invenƟon do not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). Specifically, in some embodiments, anƟbodies of the invenƟon interact with one or more residues selected from the list consisƟng of: ILE 193, THR 199, GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, THR 216, LYS 219, ASP 331, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or one or more residues selected from the list consisƟng of: PHE 209, ILE 213, VAL 220, LYS 327, ILE 328, ASP 331, ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). In preferred embodiments, anƟbodies of the invenƟon do not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 or more residues selected from the list consisƟng of: ILE 193, THR 199, GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, THR 216, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or 1, 2, 3, 4, 5, 6 or 7 residues selected from the list consisƟng of: LYS 212, THR 216, LYS 219, VAL 220, LYS 327, ILE 328, and ASP 331 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). In preferred embodiments, anƟbodies of the invenƟon do not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 5 or more residues selected from the list consisƟng of: ILE 193, THR 199, GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, THR 216, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or 3 or more residues selected from the list consisƟng of: LYS 212, THR 216, LYS 219, VAL 220, LYS 327, ILE 328, and ASP 331 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). In preferred embodiments, anƟbodies of the invenƟon do not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). In some embodiments, anƟbodies of the invenƟon interact with one or more residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: ILE 193, THR 199, GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, THR 216, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or one or more residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: LYS 212, THR 216, LYS 219, VAL 220, LYS 327, ILE 328, and ASP 331 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). In preferred embodiments, anƟbodies of the invenƟon do not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). AnƟbodies of the invenƟon may interact with 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 or more residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: ILE 193, THR 199, GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, THR 216, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or 1, 2, 3, 4, 5, 6 or 7 residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: LYS 212, THR 216, LYS 219, VAL 220, LYS 327, ILE 328, and ASP 331 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). In preferred embodiments, anƟbodies of the invenƟon do not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 5 or more to residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: ILE 193, THR 199, GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, THR 216, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or 3 or more residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: LYS 212, THR 216, LYS 219, VAL 220, LYS 327, ILE 328, and ASP 331 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). In preferred embodiments, anƟbodies of the invenƟon do not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). Specifically, in some embodiments, anƟbodies of the invenƟon interact with one or more (interfacing) residues of a disconƟnuous epitope comprising or consisƟng of amino acids LYS 202 to LYS 219 and LYS 327 to GLN 342 of PfRH5, i.e. amino acids LYS 202 to LYS 219 and LYS 327 to GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78), as described herein. Accordingly, in some embodiments, anƟbodies of the invenƟon interact with one or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, LYS 327, ILE 328, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339 and GLN 342 of SEQ ID NO: 65. In parƟcular, anƟbodies of the invenƟon may interact with one or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or one or more (interfacing) residues selected from the list consisƟng of: PHE 209, ILE 213, LYS 327, ILE 328, ASP 331 ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or 1, 2, 3, 4, 5, 6, 7 or 8 (interfacing) residues selected from the list consisƟng of: PHE 209, ILE 213, LYS 327, ILE 328, ASP 331, ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 5 or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or 3 or more (interfacing) residues selected from the list consisƟng of: PHE 209, ILE 213, LYS 327, ILE 328, ASP 331, ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). In some embodiments, anƟbodies of the invenƟon interact with one or more (interfacing) residues in a PfRH5 sequence, wherein the (interfacing) residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or one or more (interfacing) residues in a PfRH5 sequence, wherein the (interfacing) residues correspond to posiƟons selected from the list consisƟng of: PHE 209, ILE 213, LYS 327, ILE 328, ASP 331, ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). AnƟbodies of the invenƟon may interact with 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 or more (interfacing) residues in a PfRH5 sequence, wherein the (interfacing) residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or 1, 2, 3, 4, 5, 6, 7 or 8 (interfacing) residues in a PfRH5 sequence, wherein the (interfacing) residues correspond to posiƟons selected from the list consisƟng of: PHE 209, ILE 213,, LYS 327, ILE 328, ASP 331, ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 5 or more (interfacing) residues in a PfRH5 sequence, wherein the (interfacing) residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or 3 or more (interfacing) residues in a PfRH5 sequence, wherein the (interfacing) residues correspond to posiƟons selected from the list consisƟng of: PHE 209, ILE 213, LYS 327, ILE 328, ASP 331, ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). Specifically, in some embodiments, anƟbodies of the invenƟon interact with one or more (interfacing) residues of a disconƟnuous epitope comprising or consisƟng of amino acids LYS 202 to LYS 219 and ASN 326 to GLN 342 of PfRH5, i.e. amino acids LYS 202 to LYS 219 and ASN 326 to GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78), as described herein. Accordingly, in some embodiments, anƟbodies of the invenƟon interact with one or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339 and GLN 342 of SEQ ID NO: 65. In parƟcular, anƟbodies of the invenƟon may interact with one or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or one or more (interfacing) residues selected from the list consisƟng of: PHE 209, ILE 213 ASN 326, LYS 327, ILE 328, MET 330, ASP 331, ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 (interfacing) residues selected from the list consisƟng of: PHE 209, ILE 213, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 5 or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or 3 or more (interfacing) residues selected from the list consisƟng of: PHE 209, ILE 213, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross- block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). In some embodiments, anƟbodies of the invenƟon interact with one or more (interfacing) residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or one or more (interfacing) residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: PHE 209, ILE 213, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). AnƟbodies of the invenƟon may interact with 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 or more (interfacing) residues in a PfRH5 sequence, wherein the (interfacing) residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 (interfacing) residues in a PfRH5 sequence, wherein the (interfacing) residues correspond to posiƟons selected from the list consisƟng of: PHE 209, ILE 213, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 5 or more (interfacing) residues in a PfRH5 sequence, wherein the (interfacing) residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASP 331, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or 3 or more (interfacing) residues in a PfRH5 sequence, wherein the (interfacing) residues correspond to posiƟons selected from the list consisƟng of: PHE 209, ILE 213, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, ASN 334, TYR 335, and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). Specifically, in some embodiments, anƟbodies of the invenƟon interact with one or more (interfacing) residues of a disconƟnuous epitope comprising or consisƟng of amino acids LYS 202 to LYS 219 and ASN 323 to GLN 342 of PfRH5, i.e. amino acids LYS 202 to LYS 219 and ASN 323 to GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78), as described herein. Accordingly, in some embodiments, anƟbodies of the invenƟon interact with one or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338, LEU 339, GLU 341 and GLN 342 of SEQ ID NO: 65. In parƟcular, anƟbodies of the invenƟon may interact with one or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, PHE 325, ASP 331, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or one or more residues selected from the list consisƟng of: PHE 209, ILE 213, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330 ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338 and GLU 341 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). In preferred embodiments, anƟbodies of the invenƟon do not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 or more residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, PHE 325, ASP 331, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or 1, 2, 3, 4, 5, 6 or 7 residues selected from the list consisƟng of: PHE 209, ILE 213, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330 ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338 and GLU 341 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). In preferred embodiments, anƟbodies of the invenƟon do not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 5 or more residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, PHE 325, ASP 331, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or 3 or more residues selected from the list consisƟng of: PHE 209, ILE 213, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330 ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338 and GLU 341 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). In preferred embodiments, anƟbodies of the invenƟon do not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). In some embodiments, anƟbodies of the invenƟon interact with one or more residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, PHE 325, ASP 331, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or one or more residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: PHE 209, ILE 213, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330 ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338 and GLU 341 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). In preferred embodiments, anƟbodies of the invenƟon do not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). AnƟbodies of the invenƟon may interact with 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 or more residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, PHE 325, ASP 331, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or 1, 2, 3, 4, 5, 6 or 7 residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: PHE 209, ILE 213, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330 ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338 and GLU 341 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). In preferred embodiments, anƟbodies of the invenƟon do not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 5 or more to residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, PHE 325, ASP 331, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or 3 or more residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: PHE 209, ILE 213, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330 ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338 and GLU 341 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). In preferred embodiments, anƟbodies of the invenƟon do not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). Specifically, in some embodiments, anƟbodies of the invenƟon interact with one or more (interfacing) residues selected from the group consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASN 326, ILE 328, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65. In parƟcular, anƟbodies of the invenƟon may interact with one or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or one or more (interfacing) residues selected from the list consisƟng of: ILE 213, THR 216, ASN 326 and ILE 328 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 1, 2, 3, 4, 5, 6, 7, or 8 interfacing residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or 1, 2, 3 or 4 interfacing residues selected from the list consisƟng of: ILE 213, THR 216, ASN 326 and ILE 328 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 5 or more interfacing residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or 1, 2, 3 or 4 interfacing residues selected from the list consisƟng of: ILE 213, THR 216, ASN 326 and ILE 328 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross- block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). In some embodiments, anƟbodies of the invenƟon interact with one or more (interfacing) residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or one or more (interfacing) residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: ILE 213, THR 216, ASN 326 and ILE 328 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). AnƟbodies of the invenƟon may interact with 1, 2, 3, 4, 5, 6, 7, or 8 interfacing residues in a PfRH5 sequence, wherein the interfacing residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or 1, 2, 3 or 4 interfacing residues in a PfRH5 sequence, wherein the interfacing residues correspond to posiƟons selected from the list consisƟng of: ILE 213, THR 216, ASN 326 and ILE 328 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). AnƟbodies of the invenƟon may interact with 5 or more interfacing residues in a PfRH5 sequence, wherein the interfacing residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or 1, 2,3 or 4 interfacing residues in a PfRH5 sequence, wherein the interfacing residues correspond to posiƟons selected from the list consisƟng of: ILE 213, THR 216, ASN 326 and ILE 328 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). Specifically, in some embodiments, anƟbodies of the invenƟon interact with: (a) one or more (interfacing) residues selected from the group consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASN 326, ILE 328, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and (b) one or more residues selected from the list consisƟng of ALA 208, PHE 209, LYS 212, LYS 219, LYS 327, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65. In parƟcular, anƟbodies of the invenƟon may interact with: (a) one or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or one or more (interfacing) residues selected from the list consisƟng of: ILE 213, ASN 326 and ILE 328 of SEQ ID NO: 65; and (b) one or more residues selected from the list consisƟng of ALA 208, PHE 209, LYS 212, LYS 219, and ASP 331, of SEQ ID NO: 65; and / or one or more residues selected from the list consisƟng of PHE 209, LYS 327, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65. For example, in some embodiments, anƟbodies of the invenƟon interact with: (a) 1, 2, 3, 4, 5, 6, 7, or 8 (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or 1, 2, 3 or 4 (interfacing) residues selected from the list consisƟng of: ILE 213, ASN 326 and ILE 328 of SEQ ID NO: 65; and (b) 1, 2, 3, 4, or 5 residues selected from the list consisƟng of ALA 208, PHE 209, LYS 212, LYS 219, and ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65; and / or 1, 2, 3, 4 or 5 residues selected from the list consisƟng of PHE 209, LYS 327, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65. For example, in some embodiments, anƟbodies of the invenƟon interact with: (a) 5 or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or 1, 2, 3 or 4 (interfacing) residues selected from the list consisƟng of: ILE 213, ASN 326 and ILE 328 of SEQ ID NO: 65; and (b) 4 or more residues selected from the list consisƟng of ALA 208, PHE 209, LYS 212, LYS 219, and ASP 331, of SEQ ID NO: 65; and / or 1, 2, 3, 4 or 5 residues selected from the list consisƟng of PHE 209, LYS 327, ASP 331 ASN 334 and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). The residues bound by an anƟbody of the invenƟon may be residues of another PfRH5 sequence which correspond to the above residues of SEQ ID NO: 65. Specifically, in some embodiments, anƟbodies of the invenƟon interact with: (a) one or more (interfacing) residues selected from the group consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASN 326, ILE 328, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and (b) one or more residues selected from the list consisƟng of ALA 208, PHE 209, LYS 212, LYS 219, LYS 327, MET 330, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65. In parƟcular, anƟbodies of the invenƟon may interact with: (a) one or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or one or more (interfacing) residues selected from the list consisƟng of: ILE 213, ASN 326 and ILE 328 of SEQ ID NO: 65; and (b) one or more residues selected from the list consisƟng of ALA 208, PHE 209, LYS 212, and LYS 219 of SEQ ID NO: 65; and / or one or more residues selected from the list consisƟng of PHE 209, LYS 327, MET 330, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65. For example, in some embodiments, anƟbodies of the invenƟon interact with: (a) 1, 2, 3, 4, 5, 6, 7, or 8 (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or 1, 2 or 3 (interfacing) residues selected from the list consisƟng of: ILE 213, ASN 326 and ILE 328 of SEQ ID NO: 65; and (b) 1, 2, 3, or 4 residues selected from the list consisƟng of ALA 208, PHE 209, LYS 212, and LYS 219 of SEQ ID NO: 65; and / or 1, 2, 3, 4, 5 or 6 residues selected from the list consisƟng of PHE 209, LYS 327, MET 330, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65. For example, in some embodiments, anƟbodies of the invenƟon interact with: (a) 5 or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or 1, 2 or 3 (interfacing) residues selected from the list consisƟng of: ILE 213, ASN 326 and ILE 328 of SEQ ID NO: 65; and (b) 3 or more residues selected from the list consisƟng of ALA 208, PHE 209, LYS 212, and LYS 219 of SEQ ID NO: 65; and / or 1, 2, 3, 4, 5 or 6 residues selected from the list consisƟng of PHE 209, LYS 327, MET 330, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). The residues bound by an anƟbody of the invenƟon may be residues of another PfRH5 sequence which correspond to the above residues of SEQ ID NO: 65. Specifically, in some embodiments, anƟbodies of the invenƟon interact with one or more (interfacing) residues selected from the group consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASP 324, PHE 325, ASN 326, ILE 328, LYS 333, TYR 335, THR 337, LEU 339, GLU 341 and GLN 342 of SEQ ID NO: 65. In parƟcular, anƟbodies of the invenƟon may interact with one or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, PHE 325, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or one or more (interfacing) residues selected from the list consisƟng of: ILE 213, ASP 324, PHE 325, ASN 326, ILE 328, THR 337, and GLU 341 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 1, 2, 3, 4, 5, 6, 7, 8 or 9 interfacing residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, PHE 325, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or 1, 2 , 3, 4, 5, 6 or 7 interfacing residues selected from the list consisƟng of: ILE 213, ASP 324, PHE 325, ASN 326, ILE 328, THR 337, and GLU 341 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). For example, in some embodiments, anƟbodies of the invenƟon interact with 5 or more interfacing residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, PHE 325, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or 1, 2, 3, 4, 5, 6or 7 interfacing residues selected from the list consisƟng of: ILE 213, ASP 324, PHE 325, ASN 326, ILE 328, THR 337, and GLU 341 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). In some embodiments, anƟbodies of the invenƟon interact with one or more (interfacing) residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, PHE 325, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or one or more (interfacing) residues in a PfRH5 sequence, wherein the residues correspond to posiƟons selected from the list consisƟng of: ILE 213, ASP 324, PHE 325, ASN 326, ILE 328, THR 337, and GLU 341 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). AnƟbodies of the invenƟon may interact with 1, 2, 3, 4, 5, 6, 7, 8, or 9 interfacing residues in a PfRH5 sequence, wherein the interfacing residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, PHE 325, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or 1, 2, 3, 4, 5, 6 or 7 interfacing residues in a PfRH5 sequence, wherein the interfacing residues correspond to posiƟons selected from the list consisƟng of: ILE 213, ASP 324, PHE 325, ASN 326, ILE 328, THR 337, and GLU 341 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). AnƟbodies of the invenƟon may interact with 5 or more interfacing residues in a PfRH5 sequence, wherein the interfacing residues correspond to posiƟons selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, PHE 325, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or 1, 2, 3 or more interfacing residues in a PfRH5 sequence, wherein the interfacing residues correspond to posiƟons selected from the list consisƟng of: ILE 213, ASP 324, PHE 325, ASN 326, ILE 328, THR 337, and GLU 341 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). Specifically, in some embodiments, anƟbodies of the invenƟon interact with: (a) one or more (interfacing) residues selected from the group consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, ASP 324, PHE 325, ASN 326, ILE 328, LYS 333, TYR 335, THR 337, LEU 339, GLU 341 and GLN 342 of SEQ ID NO: 65; and (b) one or more residues selected from the list consisƟng of ALA 208, PHE 209, LYS 212, LYS 219, ASN 323, LYS 327, MET 330, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65. In parƟcular, anƟbodies of the invenƟon may interact with: (a) one or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, PHE 325, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or one or more (interfacing) residues selected from the list consisƟng of: ILE 213, ASP 324, PHE 325, ASN 326, ILE 328, THR 337, and GLU 341 ; and (b) one or more residues selected from the list consisƟng of ALA 208, PHE 209, LYS 219 and LYS 212 of SEQ ID NO: 65; and / or one or more residues selected from the list consisƟng of PHE 209, ASN 323, LYS 327, MET 330, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65. For example, in some embodiments, anƟbodies of the invenƟon interact with: (a) 1, 2, 3, 4, 5, 6, 7, 8, or 9 (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, PHE 325, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or 1, 23, 4, 5, 6 or 7 (interfacing) residues selected from the list consisƟng of: ILE 213, ASP 324, PHE 325, ASN 326, ILE 328, THR 337, and GLU 341 of SEQ ID NO: 65; and (b) 1, 2, 3 or 4 residues selected from the list consisƟng of ALA 208, PHE 209, LYS 212, LYS 219 of SEQ ID NO: 65; and / or 1, 2, 3, 4, 5, 6 or 7 residues selected from the list consisƟng of PHE 209, ASN 323, LYS 327, MET 330, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65. For example, in some embodiments, anƟbodies of the invenƟon interact with: (a) 5 or more (interfacing) residues selected from the list consisƟng of: LYS 202, ILE 204, ALA 205, ILE 213, THR 216, PHE 325, TYR 335, LEU 339 and GLN 342 of SEQ ID NO: 65; and / or 1, 2, 3 or more (interfacing) residues selected from the list consisƟng of: ILE 213, ASP 324, PHE 325, ASN 326, ILE 328, THR 337, and GLU 341 of SEQ ID NO: 65; and (b) 2 or more residues selected from the list consisƟng of ALA 208, PHE 209, LYS 212, LYS 219 of SEQ ID NO: 65; and / or 1, 2, 3, 4 or more residues selected from the list consisƟng of PHE 209, ASN 323, LYS 327, MET 330, ASP 331, ASN 334 and ASN 338 of SEQ ID NO: 65. AnƟbodies may not interact with all of the aforemenƟoned interfacing residues. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). The residues bound by an anƟbody of the invenƟon may be residues of another PfRH5 sequence which correspond to the above residues of SEQ ID NO: 65. Specifically, in some embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of: (a) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 81, SEQ ID NO: 83, SEQ ID NO: 85 and SEQ ID NO: 86; and (b) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 82, SEQ ID NO: 84, SEQ ID NO: 87, SEQ ID NO:88, SEQ ID NO: 89 and SEQ ID NO: 90. For example, in some embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of: (a) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 81 and SEQ ID NO: 83; and (b) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 82 and SEQ ID NO: 84. For example, in some embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of: (a) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 85 and SEQ ID NO: 86; and (b) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 82 and SEQ ID NO: 84. For example, in some embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of : (a) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 85 and SEQ ID NO: 86; and (b) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 87 and SEQ ID NO: 88. For example, in some embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of : (a) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 85 and SEQ ID NO: 86; and (b) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 89 and SEQ ID NO: 90. In preferable embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 81 and (b) the amino acid sequence of SEQ ID NO: 82. In preferable embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 83 and (b) the amino acid sequence of SEQ ID NO: 84. In preferable embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 85 and (b) the amino acid sequence of SEQ ID NO: 82. In preferable embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 86 and (b) the amino acid sequence of SEQ ID NO: 84. In preferable embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 85 and (b) the amino acid sequence of SEQ ID NO: 87. In preferable embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 86 and (b) the amino acid sequence of SEQ ID NO: 88. In preferable embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 85 and (b) the amino acid sequence of SEQ ID NO: 89. In preferable embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of: (a) the amino acid sequence of SEQ ID NO: 86 and (b) the amino acid sequence of SEQ ID NO: 90. In some parƟcularly preferred embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of ASN 323, ASP 324, PHE 325, ASN 326, MET 330, LYS 333, THR 337 and GLU 341 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78), as described herein. For example, in some embodiments, anƟbodies of the invenƟon of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338, LEU 339, GLU 341 and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78), as described herein. For example, in some embodiments, anƟbodies of the invenƟon may bind to a disconƟnuous epitope comprising or consisƟng of LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, PHE 325, ASP 331, TYR 335, LEU 339, and GLN 342 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78), as described herein and PHE 209, ILE 213, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330 ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338 and GLU 341 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78), as described herein. Preferably, the interfacing residues are idenƟfied using PDBePISA. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). Binding of such anƟbodies of the invenƟon to an epitope may be determined by any appropriate technique, such as described herein. In preferred embodiments, binding of such anƟbodies of the invenƟon to an epitope may be determined by X-ray crystallography or cry-EM. Binding of an anƟbody of the invenƟon to any of the above epitopes may be determined using an appropriate technique, such as those described herein. AnƟbodies of the invenƟon may bind to a modified PfRH5 sequence. An exemplary modified PfRH5 sequence may have been modified to reduce or prevent N-glycosylaƟon (e.g., when being produced in mammalian or insect cell lines). In parƟcular, a PfRH5 sequence may have been modified to replace THR 216 of SEQ ID NO: 65 (or a corresponding residue) with ALA 216. In these instances, anƟbodies of the invenƟon may interact with ALA 216. By way of non-limiƟng example, anƟbodies of the invenƟon may interact with one or more residues in a (modified) PfRH5 sequence selected from: ILE 193, THR 199, GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, ALA 216, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339, and GLN 342 of SEQ ID NO: 65 (e.g., interfacing residues for the heavy chain of R5.016 and RH5); and / or one or more residues in a (modified) PfRH5 sequence selected from: LYS 212, ALA 216, LYS 219, VAL 220, LYS 327, ILE 328, and ASP 331 of SEQ ID NO: 65 (e.g., interfacing residues between the light chain of R5.016 and RH5). The THR residue corresponding to THR 216 of SEQ ID NO: 65 may be modified to an ALA in any of the PfRH5 sequences described herein. Therefore, any reference to THR 216 applies equally and without reservaƟon to ALA 216, or a corresponding THR / ALA subsƟtuƟon. Those skilled in the art are able to choose a suitable mode of determining binding of the anƟbody or anƟgen-binding fragment thereof to an anƟgen (or epitope thereof) according to their preference and general knowledge, in light of the methods and disclosure herein. By way of non- limiƟng example, binding of an anƟbody of the invenƟon to an epitope may be determined by X-ray crystallography or cry-EM. Suitable techniques are described in the examples herein. Crystal structures can be determined at any appropriate resoluƟon, such as 3.2 Å and 4 Å. Suitable protocols for determining crystal structures at 3.2 Å and 4 Å are exemplified herein. A neutralising anƟbody or binding fragment thereof of the invenƟon may addiƟonally or alternaƟvely comprise a heavy chain comprising: (a) a CDR1 sequence of SEQ ID NO: 1; a CDR2 sequence of SEQ ID NO: 2 and a CDR3 sequence of SEQ ID NO: 3 (e.g., the heavy chain CDR sequences of anƟbody R5.034); (b) a CDR1 sequence of SEQ ID NO: 7; a CDR2 sequence of SEQ ID NO: 8 and a CDR3 sequence of SEQ ID NO: 9 (e.g., the heavy chain CDR sequences of anƟbody R5.102); (c) a CDR1 sequence of SEQ ID NO: 13; a CDR2 sequence of SEQ ID NO: 14 and a CDR3 sequence of SEQ ID NO: 15 (e.g., the heavy chain CDR sequences of anƟbody R5.159); (d) a CDR1 sequence of SEQ ID NO: 19; a CDR2 sequence of SEQ ID NO: 20 and a CDR3 sequence of SEQ ID NO: 21 (e.g., the heavy chain CDR sequences of anƟbody R5.237); (e) a CDR1 sequence of SEQ ID NO: 25; a CDR2 sequence of SEQ ID NO: 26 and a CDR3 sequence of SEQ ID NO: 27 (e.g., the heavy chain CDR sequences of anƟbody R5.268); or (f) a CDR1 sequence of SEQ ID NO: 31; a CDR2 sequence of SEQ ID NO: 32 and a CDR3 sequence of SEQ ID NO: 33 (e.g., the heavy chain CDR sequences of anƟbody R5.270). An anƟbody or binding fragment thereof (e.g., a neutralising anƟbody or binding fragment thereof) of the invenƟon may comprise a light chain comprising: (a) a CDR1 sequence of SEQ ID NO: 4; a CDR2 sequence of SEQ ID NO: 5 and a CDR3 sequence of SEQ ID NO: 6 (e.g., the light chain CDR sequences of anƟbody R5.034); (b) a CDR1 sequence of SEQ ID NO: 10, a CDR2 sequence of SEQ ID NO: 11 and a CDR3 sequence of SEQ ID NO: 12 (e.g., the light chain CDR sequences of anƟbody R5.102); (c) a CDR1 sequence of SEQ ID NO: 16, a CDR2 sequence of SEQ ID NO: 17 and a CDR3 sequence of SEQ ID NO: 18 (e.g., the light chain CDR sequences of anƟbody R5.159); (d) a CDR1 sequence of SEQ ID NO: 22, a CDR2 sequence of SEQ ID NO: 23 and a CDR3 sequence of SEQ ID NO: 24 (e.g., the light chain CDR sequences of anƟbody R5.237); (e) a CDR1 sequence of SEQ ID NO: 28, a CDR2 sequence of SEQ ID NO: 29 and a CDR3 sequence of SEQ ID NO: 30 (e.g., the light chain CDR sequences of anƟbody R5.268); or (f) a CDR1 sequence of SEQ ID NO: 34, a CDR2 sequence of SEQ ID NO: 35 and a CDR3 sequence of SEQ ID NO: 36 (e.g., the light chain CDR sequences of anƟbody R5.270). Preferably, an anƟbody or binding fragment thereof (e.g., a neutralising anƟbody or binding fragment thereof) of the invenƟon may comprise: (a) a heavy chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 1, CDR2 has the sequence of SEQ ID NO: 2 and a CDR3 has the sequence of SEQ ID NO: 3, and a light chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 4, CDR2 has the sequence of SEQ ID NO: 5 and a CDR3 has the sequence of SEQ ID NO: 6 (e.g., the heavy and light chain CDR sequences of anƟbody R5.034); (b) a heavy chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 7, CDR2 has the sequence of SEQ ID NO: 8 and a CDR3 has the sequence of SEQ ID NO: 9, and a light chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 10, CDR2 has the sequence of SEQ ID NO: 11 and a CDR3 has the sequence of SEQ ID NO: 12 (e.g., the heavy and light chain CDR sequences of anƟbody R5.102); (c) a heavy chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 13, CDR2 has the sequence of SEQ ID NO: 14 and a CDR3 has the sequence of SEQ ID NO: 15, and a light chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 16, CDR2 has the sequence of SEQ ID NO: 17 and a CDR3 has the sequence of SEQ ID NO: 18 (e.g., the heavy and light chain CDR sequences of anƟbody R5.159); (d) a heavy chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 19, CDR2 has the sequence of SEQ ID NO: 20 and a CDR3 has the sequence of SEQ ID NO: 21, and a light chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 22, CDR2 has the sequence of SEQ ID NO: 23 and a CDR3 has the sequence of SEQ ID NO: 24 (e.g., the heavy and light chain CDR sequences of anƟbody R5.237); (e) a heavy chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 25, CDR2 has the sequence of SEQ ID NO: 26 and a CDR3 has the sequence of SEQ ID NO: 27, and a light chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 28, CDR2 has the sequence of SEQ ID NO: 29 and a CDR3 has the sequence of SEQ ID NO: 30 (e.g., the heavy and light chain CDR sequences of anƟbody R5.268); or (f) a heavy chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 31, CDR2 has the sequence of SEQ ID NO: 32 and a CDR3 has the sequence of SEQ ID NO: 33, and a light chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 34, CDR2 has the sequence of SEQ ID NO: 35 and a CDR3 has the sequence of SEQ ID NO: 36 (e.g., the heavy and light chain CDR sequences of anƟbody R5.270). In some embodiments, an anƟbody of the invenƟon, or binding fragment thereof, comprises: (a) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 37 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 38 (e.g., the heavy and light chain variable regions of anƟbody R5.034); (b) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 39 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 40 (e.g., the heavy and light chain variable regions of anƟbody R5.102); (c) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 41 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 42 (e.g., the heavy and light chain variable regions of anƟbody R5.159); (d) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 43 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 44 (e.g., the heavy and light chain variable regions of anƟbody R5.237); (e) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 45 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 46 (e.g., the heavy and light chain variable regions of anƟbody R5.268); or (f) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 47 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 48 (e.g., the heavy and light chain variable regions of anƟbody R5.270). Preferably, an anƟbody of the invenƟon, or binding fragment thereof, comprises a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 37 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 38. Further preferably, an anƟbody of the invenƟon, or binding fragment thereof, comprises a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 37 and a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 38. In some embodiments, an anƟbody of the invenƟon, or binding fragment thereof, comprises: (a) a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 37 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 38; (b) a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 39 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 40; (c) a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 41 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 42; (d) a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 43 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 44; (e) a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 45 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 46; or (f) a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 47 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 48. Preferably, an anƟbody of the invenƟon, or binding fragment thereof, comprises a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 37 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 38. Further preferably, an anƟbody of the invenƟon, or binding fragment thereof, comprises a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 37 and a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 38. In some embodiments, an anƟbody of the invenƟon, or binding fragment thereof, comprises: (a) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 37 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 1, a CDR2 sequence of SEQ ID NO: 2 and a CDR3 sequence of SEQ ID NO: 3 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 38 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 4, a CDR2 sequence of SEQ ID NO: 5 and a CDR3 sequence of SEQ ID NO: 6; (b) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 39 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 7, a CDR2 sequence of SEQ ID NO: 8 and a CDR3 sequence of SEQ ID NO: 9 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 40 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 10, a CDR2 sequence of SEQ ID NO: 11 and a CDR3 sequence of SEQ ID NO: 12; (c) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 41 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 13, a CDR2 sequence of SEQ ID NO: 14 and a CDR3 sequence of SEQ ID NO: 15 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 42 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 16, a CDR2 sequence of SEQ ID NO: 17 and a CDR3 sequence of SEQ ID NO: 18; (d) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 43 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 19, a CDR2 sequence of SEQ ID NO: 20 and a CDR3 sequence of SEQ ID NO: 21 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 44 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 22, a CDR2 sequence of SEQ ID NO: 23 and a CDR3 sequence of SEQ ID NO: 24; (e) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 45 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 25, a CDR2 sequence of SEQ ID NO: 26 and a CDR3 sequence of SEQ ID NO: 27 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 46 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 28, a CDR2 sequence of SEQ ID NO: 29 and a CDR3 sequence of SEQ ID NO: 30; or (f) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 47 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 31, a CDR2 sequence of SEQ ID NO: 32 and a CDR3 sequence of SEQ ID NO: 33 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 48 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 34, a CDR2 sequence of SEQ ID NO: 35 and a CDR3 sequence of SEQ ID NO: 36. Preferably, an anƟbody of the invenƟon, or binding fragment thereof, comprises a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 37 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 1, a CDR2 sequence of SEQ ID NO: 2 and a CDR3 sequence of SEQ ID NO: 3 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 38 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 4, a CDR2 sequence of SEQ ID NO: 5 and a CDR3 sequence of SEQ ID NO: 6. Further preferably, an anƟbody of the invenƟon, or binding fragment thereof, comprises a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 37 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 1, a CDR2 sequence of SEQ ID NO: 2 and a CDR3 sequence of SEQ ID NO: 3 and a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 38 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 4, a CDR2 sequence of SEQ ID NO: 5 and a CDR3 sequence of SEQ ID NO: 6. In some embodiments, an anƟbody of the invenƟon, or binding fragment thereof, comprises: (a) a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 37 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 1, a CDR2 sequence of SEQ ID NO: 2 and a CDR3 sequence of SEQ ID NO: 3 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 38 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 4, a CDR2 sequence of SEQ ID NO: 5 and a CDR3 sequence of SEQ ID NO: 6; (b) a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 39 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 7, a CDR2 sequence of SEQ ID NO: 8 and a CDR3 sequence of SEQ ID NO: 9 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 40 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 10, a CDR2 sequence of SEQ ID NO: 11 and a CDR3 sequence of SEQ ID NO: 12; (c) a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 41 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 13, a CDR2 sequence of SEQ ID NO: 14 and a CDR3 sequence of SEQ ID NO: 15 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 42 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 16, a CDR2 sequence of SEQ ID NO: 17 and a CDR3 sequence of SEQ ID NO: 18; (d) a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 43 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 19, a CDR2 sequence of SEQ ID NO: 20 and a CDR3 sequence of SEQ ID NO: 21 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 44 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 22, a CDR2 sequence of SEQ ID NO: 23 and a CDR3 sequence of SEQ ID NO: 24; (e) a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 45 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 25, a CDR2 sequence of SEQ ID NO: 26 and a CDR3 sequence of SEQ ID NO: 27 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 46 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 28, a CDR2 sequence of SEQ ID NO: 29 and a CDR3 sequence of SEQ ID NO: 30; or (f) a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 47 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 31, a CDR2 sequence of SEQ ID NO: 32 and a CDR3 sequence of SEQ ID NO: 33 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 48 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 34, a CDR2 sequence of SEQ ID NO: 35 and a CDR3 sequence of SEQ ID NO: 36. Preferably, an anƟbody of the invenƟon, or binding fragment thereof, comprises a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 37 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 1, a CDR2 sequence of SEQ ID NO: 2 and a CDR3 sequence of SEQ ID NO: 3 and / or a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 38 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 4, a CDR2 sequence of SEQ ID NO: 5 and a CDR3 sequence of SEQ ID NO: 6. Further preferably, an anƟbody of the invenƟon, or binding fragment thereof, comprises a heavy chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 37 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 1, a CDR2 sequence of SEQ ID NO: 2 and a CDR3 sequence of SEQ ID NO: 3 and a light chain variable region having at least 90% sequence idenƟty to the sequence of SEQ ID NO: 38 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 4, a CDR2 sequence of SEQ ID NO: 5 and a CDR3 sequence of SEQ ID NO: 6. In some embodiments, an anƟbody of the invenƟon, or binding fragment thereof, comprises: (a) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 37 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 38; (b) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 39 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 40; (c) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 41 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 42; (d) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 43 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 44; (e) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 45 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 46; or (f) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 47 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 48. In some embodiments, an anƟbody of the invenƟon, or binding fragment thereof, comprises: (a) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 37 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 1, a CDR2 sequence of SEQ ID NO: 2 and a CDR3 sequence of SEQ ID NO: 3 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 38 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 4, a CDR2 sequence of SEQ ID NO: 5 and a CDR3 sequence of SEQ ID NO: 6; (b) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 39 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 7, a CDR2 sequence of SEQ ID NO: 8 and a CDR3 sequence of SEQ ID NO: 9 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 40 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 10, a CDR2 sequence of SEQ ID NO: 11 and a CDR3 sequence of SEQ ID NO: 12; (c) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 41 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 13, a CDR2 sequence of SEQ ID NO: 14 and a CDR3 sequence of SEQ ID NO: 15 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 42 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 16, a CDR2 sequence of SEQ ID NO: 17 and a CDR3 sequence of SEQ ID NO: 18; (d) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 43 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 19, a CDR2 sequence of SEQ ID NO: 20 and a CDR3 sequence of SEQ ID NO: 21 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 44 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 22, a CDR2 sequence of SEQ ID NO: 23 and a CDR3 sequence of SEQ ID NO: 24; (e) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 45 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 25, a CDR2 sequence of SEQ ID NO: 26 and a CDR3 sequence of SEQ ID NO: 27 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 46 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 28, a CDR2 sequence of SEQ ID NO: 29 and a CDR3 sequence of SEQ ID NO: 30; or (f) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 47 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 31, a CDR2 sequence of SEQ ID NO: 32 and a CDR3 sequence of SEQ ID NO: 33 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 48 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 34, a CDR2 sequence of SEQ ID NO: 35 and a CDR3 sequence of SEQ ID NO: 36. Preferably, an anƟbody of the invenƟon, or binding fragment thereof, comprises: (a) a heavy chain variable region sequence of SEQ ID NO: 37 and / or a light chain variable region sequence of SEQ ID NO: 38; (b) a heavy chain variable region sequence of SEQ ID NO: 39 and / or a light chain variable region sequence of SEQ ID NO: 40; (c) a heavy chain variable region sequence of SEQ ID NO: 41 and / or a light chain variable region sequence of SEQ ID NO: 42; (d) a heavy chain variable region sequence of SEQ ID NO: 43 and / or a light chain variable region sequence of SEQ ID NO: 44; (e) a heavy chain variable region sequence of SEQ ID NO: 45 and / or a light chain variable region sequence of SEQ ID NO: 46; or (f) a heavy chain variable region sequence of SEQ ID NO: 47 and / or a light chain variable region sequence of SEQ ID NO: 48. Typically, an anƟbody of the invenƟon has both the heavy and light chain CDRs of the same anƟbody of the invenƟon (e.g. the heavy and light chain CDRs of R5.034) and the heavy and light chain FRs from this same anƟbody (e.g. the heavy and light chain FRs of R5.034). Preferably an anƟbody of the invenƟon comprises: (a) the heavy and light chain CDRs of the R5.034 anƟbody and the corresponding heavy and light chain FRs of the R5.034 anƟbody; (b) the heavy and light chain CDRs of the R5.102 anƟbody and the corresponding heavy and light chain FRs of the R5.102 anƟbody; (c) the heavy and light chain CDRs of the R5.159 anƟbody and the corresponding heavy and light chain FRs of the R5.159 anƟbody; (d) the heavy and light chain CDRs of the R5.237 anƟbody and the corresponding heavy and light chain FRs of the R5.237 anƟbody; (e) the heavy and light chain CDRs of the R5.268 anƟbody and the corresponding heavy and light chain FRs of the R5.268 anƟbody; or (f) the heavy and light chain CDRs of the R5.270 anƟbody and the corresponding heavy and light chain FRs of the R5.270 anƟbody as idenƟfied above. ParƟcularly preferred are neutralising anƟbodies with both the VH and VL sequences listed above. In a more preferred embodiment, a neutralising anƟbody or binding fragment thereof of the present invenƟon comprises the VH and VL sequences of R5.034, R5.102, R5.159, R5.237, R5.268 or R5.270. For example, in some embodiments, the anƟbody comprises a sequence corresponding to SEQ ID NO: 37 and a sequence corresponding to SEQ ID NO: 38. In some embodiments, the anƟbody comprises a sequence corresponding to SEQ ID NO: 39 and a sequence corresponding to SEQ ID NO: 40. In some embodiments, the anƟbody comprises a sequence corresponding to SEQ ID NO: 41 and a sequence corresponding to SEQ ID NO: 42. In some embodiments, the anƟbody comprises a sequence corresponding to SEQ ID NO: 43 and a sequence corresponding to SEQ ID NO: 44. In some embodiments, the anƟbody comprises a sequence corresponding to SEQ ID NO: 45 and a sequence corresponding to SEQ ID NO: 46. In some embodiments, the anƟbody comprises a sequence corresponding to SEQ ID NO: 47 and a sequence corresponding to SEQ ID NO: 48. In some embodiments, an anƟbody or binding fragment thereof of the present invenƟon comprises the full length heavy and light chain sequences of R5.034, R5.102, R5.159, R5.237, R5.268 or R5.270. As defined herein, anƟbodies of the invenƟon may include variant anƟbodies. Such variants may have CDRs sharing a high level of idenƟty with the CDRs of an anƟbody of the invenƟon, for example may have CDRs each of which independently may differ by one or two amino acids from the anƟbody of the invenƟon from which the variant anƟbody is derived, and wherein the variant retains the binding and funcƟonal properƟes of the anƟbody of the invenƟon. AddiƟonally, such anƟbodies may have one or more variaƟons (e.g. a conservaƟve amino acid subsƟtuƟon) in the framework regions. By way of a non-limiƟng example, variants of anƟbody R5.034 may have CDRs that differ by 1 or 2 amino acid residues in any one or more of the CDRs of anƟbody R5.034. ConservaƟve amino acid subsƟtuƟons are parƟcularly contemplated (see the disclosure herein in relaƟon to PfRH5 anƟgen variants, which applies equally to variants of anƟbodies of the invenƟon). The variaƟons in the amino acid sequences of the anƟbodies of the invenƟon should maintain at least 70%, 80%, 85%, 90%, 95%, 99%, or 99.9%. Variants having at least 90% sequence idenƟty with the anƟbodies of the invenƟon, parƟcularly the specific anƟbodies exemplified herein are specifically contemplated. VariaƟon may or may not be limited to the framework regions and not present in the CDRs. The term “neutralising anƟbody” is defined herein to mean an anƟbody which by itself (in the absence of any other PfRH5 anƟbody or other anƟbody against a malarial invasion protein) has the ability to (at least parƟally) inhibit the growth of Plasmodium falciparum parasites, and more preferably across a plurality of strains of blood-stage P. falciparum parasites. AnƟbody acƟvity may be quanƟfied using any appropriate technique and measured in any appropriate units. Typically, an anƟbody or binding fragment thereof (e.g., a neutralising anƟbody or binding fragment thereof) of the invenƟon have a GIA of at least at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90% or more against Plasmodium parasites. Preferably, the PfRH5 fragments of the invenƟon induce anƟbodies that have a growth inhibitory acƟvity (GIA) of at least 70%, at least 75%, at least 80%, at least 90% or more against Plasmodium parasites. The growth inhibitory acƟvity (GIA) may be measured at any appropriate concentraƟon of the anƟbodies. For example, the neutralising anƟbodies of the invenƟon may give a GIA of at least 30%, at least 50% and preferably at least 80% or more against the blood-stage Plasmodium parasite, at an IgG concentraƟon of 10 µg / ml IgG of the purified neutralising anƟbody. Preferably the neutralising PfRH5 anƟbodies of the invenƟon exert similarly high levels of GIA against both the vaccine-homologous clone, 3D7, and against a vaccine-heterologous strain, FVO. A neutralising PfRH5 anƟbody of the invenƟon has an EC50which is at least comparable to total IgG against full length PfRH5, and preferably significantly lower than the EC50against full-length PfRH5 of the EC50of known anƟ-PfRH5 anƟbodies. A neutralising anƟbody of the invenƟon preferably has an EC50significantly lower than that of the anƟ-PfAMA1 BG98 standard (Faber, B.W., et al., InfecƟon and immunity, 2013; incorporated herein by reference). Typically a neutralising PfRH5 anƟbody of the invenƟon has an EC50value of less than 50 µg / ml, less than 40 µg / ml, less than 30 µg / ml, less than 25 µg / ml, less than 20 µg / ml, less than 15 µg / ml, less than 10 µg / ml, less than 9 µg / ml, less than 8 µg / ml, less than 7 µg / ml, less than 6 µg / ml, less than 5 µg / ml, less than 4 µg / ml¸ less than 3 µg / ml¸ less than 2 µg / ml¸ less than 1 µg / ml, less than 100 ng / ml¸ or less. Typically, the neutralising anƟbodies of the invenƟon result in a GIA of at least 30%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90% or more against the blood-stage Plasmodium parasite. Preferably, the neutralising anƟbodies of the invenƟon will raise anƟbodies that result in a GIA of at least 70% against the blood-stage Plasmodium parasite measured at any appropriate concentraƟon as described herein. Typically, the anƟbody or binding fragment thereof (e.g., a neutralising anƟbody or binding fragment thereof) of the invenƟon are effecƟve against geneƟcally diverse strains of the Plasmodium parasite. This is likely to be of importance in achieving protecƟon against the variety of strains circulaƟng in the natural environment. Accordingly, preferably, the neutralising anƟbodies of the invenƟon will result in a GIA of at least at least 50%, at least 60%, at least 70%, at least 80%, at least 90% or more against a plurality of geneƟc strains of the blood-stage Plasmodium parasite. Preferably, the neutralising anƟbodies of the invenƟon will result in a GIA of at least 70% or more against a plurality of geneƟc strains of the blood-stage Plasmodium parasite. In some embodiments, the anƟbody blocks the binding of one or more of anƟbodies R5.034, R5.102, R5.159, R5.237, R5.268 or R5.270 to PfRH5. In some embodiments, the anƟbody blocks the binding of R5.034 to PfRH5. In some embodiments, the anƟbody blocks the binding of R5.102 to PfRH5. In some embodiments, the anƟbody blocks the binding of one or more of R5.159 to PfRH5. In some embodiments, the anƟbody blocks the binding of R5.237 to PfRH5. In some embodiments, the anƟbody blocks the binding of R5.268 to PfRH5. In some embodiments, the anƟbody blocks the binding of R5.270 to PfRH5. AlternaƟvely, or addiƟonally, in some embodiments, the anƟbody does not block the binding of anƟbody R5.001 to PfRH5. In some embodiments, the anƟbody does not block the binding of an anƟbody comprising a sequence corresponding to SEQ ID NO: 79 and a sequence corresponding to SEQ ID NO: 80 to PfRH5. In some embodiments the anƟbody further comprises a signal pepƟde; wherein opƟonally the signal pepƟdes direct secreƟon from human cells, and preferably said signal pepƟde is a mammalian signal pepƟde from Ɵssue plasminogen acƟvator. The present disclosure also provides for an anƟbody or anƟgen-binding fragment thereof that competes for binding to RH5 with an anƟ-PfRH5 anƟbody or anƟgen-binding fragment of the invenƟon. Typically, an anƟbody or anƟgen-binding fragment thereof competes for specific binding to PfRH5 with an anƟbody or anƟgen-binding fragment thereof of the invenƟon. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). In parƟcular, the disclosure provides for an anƟbody or anƟgen-binding fragment thereof that compete with the specific binding to PfRH5 with one or more of the R5.034, R5.102, R5.159, R5.237, R5.268 or R5.270 anƟbodies or anƟgen-binding fragments thereof, or a germlined version thereof. Preferably, the disclosure provides for an anƟbody or anƟgen-binding fragment thereof that compete with the specific binding to PfRH5 with R5.034 anƟbodies or anƟgen-binding fragments thereof, or a germlined version thereof. The disclosure provides for an anƟbody or anƟgen-binding fragment thereof that compete with the specific binding to PfRH5 with an anƟ-PfRH5 anƟbody or anƟgen-binding fragment thereof of the invenƟon having the set of HCDRs and LCDRs as described herein. In parƟcular, the disclosure provides for an anƟbody or anƟgen-binding fragment thereof that compete with the specific binding to PfRH5 with an anƟ-PfRH5 anƟbody or anƟgen-binding fragment thereof having the set of HCDRs and LCDRs of any one of R5.034, R5.102, R5.159, R5.237, R5.268 or R5.270 anƟbodies or anƟgen- binding fragments thereof, or a germlined version thereof. Preferably, the disclosure provides for an anƟbody or anƟgen-binding fragment thereof that compete with the specific binding to PfRH5 with an anƟ-PfRH5 anƟbody or anƟgen-binding fragment thereof having the set of HCDRs and LCDRs of R5.034 anƟbodies, or anƟgen-binding fragments thereof. The present disclosure also provides for an anƟbody or anƟgen-binding fragment thereof that bind to the same epitope as an anƟ-PfRH5 anƟbody or anƟgen-binding fragment thereof of the present invenƟon. As described herein, such anƟbodies of the present invenƟon do not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely (e.g., R5.001). In parƟcular, the disclosure provides for an anƟbody or anƟgen-binding fragment thereof that bind to the same epitope as any one or more of the R5.034, R5.102, R5.159, R5.237, R5.268 or R5.270 anƟbodies or anƟgen-binding fragments thereof, or a germlined version thereof. Preferably, the disclosure provides for an anƟbody or anƟgen-binding fragment thereof that bind to the same epitope as R5.034 anƟbodies or anƟgen-binding fragments thereof, or a germlined version thereof. The disclosure provides for an anƟbody or anƟgen-binding fragment thereof that bind to the same epitope as an anƟ-PfRH5 anƟbody or anƟgen-binding fragment thereof of the invenƟon having the set of HCDRs and LCDRs as described herewith. The disclosure provides for an anƟbody or anƟgen- binding fragment thereof that bind to the same epitope as an anƟ-PfRH5 anƟbody or anƟgen-binding fragment thereof of the invenƟon having the set of HCDRs and LCDRs of any one of R5.034, R5.102, R5.159, R5.237, R5.268 or R5.270 anƟbodies or anƟgen-binding fragments thereof, or a germlined version thereof. Preferably, the disclosure provides for an anƟbody or anƟgen-binding fragment thereof that bind to the same epitope as an anƟ-PfRH5 anƟbody or anƟgen-binding fragment thereof of the invenƟon having the set of HCDRs and LCDRs of R5.034 anƟbodies or anƟgen-binding fragments thereof, or a germlined version thereof. Two anƟbodies may be considered to bind to the same or overlapping epitope if each compeƟƟvely inhibits (blocks) binding of the other to the anƟgen. That is, a 1-, 5-, 10-, 20- or 100-fold excess of one anƟbody inhibits binding of the other by at least 50% but preferably 75%, 90% or even 99% as measured in a compeƟƟve binding assay. AlternaƟvely, two anƟbodies may be considered to have the same epitope if essenƟally all amino acid mutaƟons in the anƟgen that reduce or eliminate binding of one anƟbody reduce or eliminate binding of the other. Two anƟbodies may be considered to have overlapping epitopes if some amino acid mutaƟons that reduce or eliminate binding of one anƟbody reduce or eliminate binding of the other. AddiƟonal rouƟne experimentaƟon (e.g., pepƟde mutaƟon and binding analyses) can then be carried out to confirm whether the observed lack of binding of the test anƟbody is in fact due to binding to the same epitope as the reference anƟbody or if steric blocking (or another phenomenon) is responsible for the lack of observed binding. Experiments of this sort can be performed using ELISA, RIA, SPR, flow cytometry or any other quanƟtaƟve or qualitaƟve anƟbody-binding assay available in the art. Other suitable techniques to determine whether two anƟbodies bind to the same epitope include hydrogen / deuterium exchange (HDX) and X-ray crystallography. An anƟbody or anƟgen-binding fragment of the invenƟon may not interact with or bind to an epitope comprising or consisƟng of ILE 193, THR 199, GLY 201, CYS 203, VAL 206, ASP 207, LYS 211, GLU 215 or VAL 220 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). Thus, a disconƟnuous epitope of the invenƟon may not comprise one or more of ILE 193, THR 199, GLY 201, CYS 203, VAL 206, ASP 207, LYS 211, GLU 215 or VAL 220 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). An anƟbody or anƟgen-binding fragment of the invenƟon may not interact with one or more of ILE 193, THR 199, GLY 201, CYS 203, VAL 206, ASP 207, LYS 211, GLU 215 or VAL 220 of SEQ ID NO: 65, or the corresponding amino acid residues of another PfRH5 sequence (e.g. SEQ ID NO: 66) or fragment (such as any one of SEQ ID NOs: 67 to 74 or 78). Isolated nucleoƟde sequences In other aspects, the invenƟon provides an isolated nucleic acid sequence, or pair of isolated nucleic acid sequences, encoding the heavy and / or the light chain(s) of an anƟbody of the invenƟon. In some embodiments, the invenƟon provides an isolated nucleic acid sequence encoding a heavy chain comprising: (a) a CDR1 sequence of SEQ ID NO: 1; a CDR2 sequence of SEQ ID NO: 2 and a CDR3 sequence of SEQ ID NO: 3; (b) a CDR1 sequence of SEQ ID NO: 7; a CDR2 sequence of SEQ ID NO: 8 and a CDR3 sequence of SEQ ID NO: 9; (c) a CDR1 sequence of SEQ ID NO: 13; a CDR2 sequence of SEQ ID NO: 14 and a CDR3 sequence of SEQ ID NO: 15; (d) a CDR1 sequence of SEQ ID NO: 19; a CDR2 sequence of SEQ ID NO: 20 and a CDR3 sequence of SEQ ID NO: 21; (e) a CDR1 sequence of SEQ ID NO: 25; a CDR2 sequence of SEQ ID NO: 26 and a CDR3 sequence of SEQ ID NO: 27; or (f) a CDR1 sequence of SEQ ID NO: 31; a CDR2 sequence of SEQ ID NO: 32 and a CDR3 sequence of SEQ ID NO: 33. For example, in some embodiments, the invenƟon provides an isolated nucleic acid sequence encoding a light chain comprising: (a) a CDR1 sequence of SEQ ID NO: 4; a CDR2 sequence of SEQ ID NO: 5 and a CDR3 sequence of SEQ ID NO: 6; (b) a CDR1 sequence of SEQ ID NO: 10, a CDR2 sequence of SEQ ID NO: 11 and a CDR3 sequence of SEQ ID NO: 12; (c) a CDR1 sequence of SEQ ID NO: 16, a CDR2 sequence of SEQ ID NO: 17 and a CDR3 sequence of SEQ ID NO: 18; (d) a CDR1 sequence of SEQ ID NO: 22, a CDR2 sequence of SEQ ID NO: 23 and a CDR3 sequence of SEQ ID NO: 24; (e) a CDR1 sequence of SEQ ID NO: 28, a CDR2 sequence of SEQ ID NO: 29 and a CDR3 sequence of SEQ ID NO: 30; or (f) a CDR1 sequence of SEQ ID NO: 34, a CDR2 sequence of SEQ ID NO: 35 and a CDR3 sequence of SEQ ID NO: 36. For example, in some embodiments the invenƟon provides an isolated nucleic acid sequence, or pair of isolated nucleic acid sequences, encoding : (a) a heavy chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 1, CDR2 has the sequence of SEQ ID NO: 2 and a CDR3 has the sequence of SEQ ID NO: 3, and a light chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 4, CDR2 has the sequence of SEQ ID NO: 5 and a CDR3 has the sequence of SEQ ID NO: 6; (b) a heavy chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 7, CDR2 has the sequence of SEQ ID NO: 8 and a CDR3 has the sequence of SEQ ID NO: 9, and a light chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 10, CDR2 has the sequence of SEQ ID NO: 11 and a CDR3 has the sequence of SEQ ID NO: 12; (c) a heavy chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 13, CDR2 has the sequence of SEQ ID NO: 14 and a CDR3 has the sequence of SEQ ID NO: 15, and a light chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 16, CDR2 has the sequence of SEQ ID NO: 17 and a CDR3 has the sequence of SEQ ID NO: 18; (d) a heavy chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 19, CDR2 has the sequence of SEQ ID NO: 20 and a CDR3 has the sequence of SEQ ID NO: 21, and a light chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 22, CDR2 has the sequence of SEQ ID NO: 23 and a CDR3 has the sequence of SEQ ID NO: 24; (e) a heavy chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 25, CDR2 has the sequence of SEQ ID NO: 26 and a CDR3 has the sequence of SEQ ID NO: 27, and a light chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 28, CDR2 has the sequence of SEQ ID NO: 29 and a CDR3 has the sequence of SEQ ID NO: 30; or (f) a heavy chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 31, CDR2 has the sequence of SEQ ID NO: 32 and a CDR3 has the sequence of SEQ ID NO: 33, and a light chain comprising three CDR sequences wherein CDR1 has the sequence of SEQ ID NO: 34, CDR2 has the sequence of SEQ ID NO: 35 and a CDR3 has the sequence of SEQ ID NO: 36. For example, in some embodiments the invenƟon provides an isolated nucleic acid sequence, or pair of isolated nucleic acid sequences, encoding: (a) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 37 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 38; (b) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 39 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 40; (c) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 41 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 42; (d) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 43 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 44; (e) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 45 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 46; or (f) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 47 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 48. For example, in some embodiments the invenƟon provides an isolated nucleic acid sequence, or pair of isolated nucleic acid sequences, encoding: (a) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 37 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 1, a CDR2 sequence of SEQ ID NO: 2 and a CDR3 sequence of SEQ ID NO: 3 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 38 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 4, a CDR2 sequence of SEQ ID NO: 5 and a CDR3 sequence of SEQ ID NO: 6; (b) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 39 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 7, a CDR2 sequence of SEQ ID NO: 8 and a CDR3 sequence of SEQ ID NO: 9 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 40 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 10, a CDR2 sequence of SEQ ID NO: 11 and a CDR3 sequence of SEQ ID NO: 12; (c) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 41 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 13, a CDR2 sequence of SEQ ID NO: 14 and a CDR3 sequence of SEQ ID NO: 15 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 42 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 16, a CDR2 sequence of SEQ ID NO: 17 and a CDR3 sequence of SEQ ID NO: 18; (d) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 43 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 19, a CDR2 sequence of SEQ ID NO: 20 and a CDR3 sequence of SEQ ID NO: 21 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 44 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 22, a CDR2 sequence of SEQ ID NO: 23 and a CDR3 sequence of SEQ ID NO: 24; (e) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 45 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 25, a CDR2 sequence of SEQ ID NO: 26 and a CDR3 sequence of SEQ ID NO: 27 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 46 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 28, a CDR2 sequence of SEQ ID NO: 29 and a CDR3 sequence of SEQ ID NO: 30; or (f) a heavy chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 47 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 31, a CDR2 sequence of SEQ ID NO: 32 and a CDR3 sequence of SEQ ID NO: 33 and / or a light chain variable region having at least 80% sequence idenƟty to the sequence of SEQ ID NO: 48 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 34, a CDR2 sequence of SEQ ID NO: 35 and a CDR3 sequence of SEQ ID NO: 36. For example, in some embodiments the invenƟon provides an isolated nucleic acid sequence, or pair of isolated nucleic acid sequences, encoding: (a) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 37 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 38; (b) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 39 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 40; (c) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 41 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 42; (d) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 43 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 44; (e) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 45 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 46; or (f) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 47 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 48. For example, in some embodiments the invenƟon provides an isolated nucleic acid sequence, or pair of isolated nucleic acid sequences, encoding: (a) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 37 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 1, a CDR2 sequence of SEQ ID NO: 2 and a CDR3 sequence of SEQ ID NO: 3 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 38 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 4, a CDR2 sequence of SEQ ID NO: 5 and a CDR3 sequence of SEQ ID NO: 6; (b) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 39 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 7, a CDR2 sequence of SEQ ID NO: 8 and a CDR3 sequence of SEQ ID NO: 9 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 40 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 10, a CDR2 sequence of SEQ ID NO: 11 and a CDR3 sequence of SEQ ID NO: 12; (c) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 41 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 13, a CDR2 sequence of SEQ ID NO: 14 and a CDR3 sequence of SEQ ID NO: 15 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 42 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 16, a CDR2 sequence of SEQ ID NO: 17 and a CDR3 sequence of SEQ ID NO: 18; (d) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 43 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 19, a CDR2 sequence of SEQ ID NO: 20 and a CDR3 sequence of SEQ ID NO: 21 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 44 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 22, a CDR2 sequence of SEQ ID NO: 23 and a CDR3 sequence of SEQ ID NO: 24; (e) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 45 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 25, a CDR2 sequence of SEQ ID NO: 26 and a CDR3 sequence of SEQ ID NO: 27 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 46 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 28, a CDR2 sequence of SEQ ID NO: 29 and a CDR3 sequence of SEQ ID NO: 30; or (f) a heavy chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 47 wherein the heavy chain variable region comprises a CDR1 sequence of SEQ ID NO: 31, a CDR2 sequence of SEQ ID NO: 32 and a CDR3 sequence of SEQ ID NO: 33 and / or a light chain variable region having at least 80%, 85%, 90%, 95%, 99%, or 99.9% sequence idenƟty to the sequence of SEQ ID NO: 48 wherein the light chain variable region comprises a CDR1 sequence of SEQ ID NO: 34, a CDR2 sequence of SEQ ID NO: 35 and a CDR3 sequence of SEQ ID NO: 36. For example, in some embodiments the invenƟon provides an isolated nucleic acid sequence, or pair of isolated nucleic acid sequences, encoding: (a) a heavy chain variable region sequence of SEQ ID NO: 37 and / or a light chain variable region sequence of SEQ ID NO: 38; (b) a heavy chain variable region sequence of SEQ ID NO: 39 and / or a light chain variable region sequence of SEQ ID NO: 40; (c) a heavy chain variable region sequence of SEQ ID NO: 41 and / or a light chain variable region sequence of SEQ ID NO: 42; (d) a heavy chain variable region sequence of SEQ ID NO: 43 and / or a light chain variable region sequence of SEQ ID NO: 44; (e) a heavy chain variable region sequence of SEQ ID NO: 45 and / or a light chain variable region sequence of SEQ ID NO: 46; or (f) a heavy chain variable region sequence of SEQ ID NO: 47 and / or a light chain variable region sequence of SEQ ID NO: 48. Vectors and expression systems The present invenƟon provides a vector or pair of vectors encoding an anƟbody of the invenƟon. Typically, the vector (or pair of vectors) is present in the form of a formulaƟon or composiƟon. AnƟbodies of the invenƟon may be expressed by: (i) the same vector; or (ii) by two (or more) separate vectors. The vector(s) may be present in the form of a formulaƟon or composiƟon. The vector(s) may be a viral vector. Such a viral vector may be an adenovirus (of a human serotype such as AdHu5, a simian serotype such as ChAd63, ChAdOX1 or ChAdOX2, or another form), an adeno-associated virus (AAV), or poxvirus vector (such as a modified vaccinia Ankara (MVA)). ChAdOX1 and ChAdOX2 are disclosed in WO2012 / 172277 (herein incorporated by reference in its enƟrety). ChAdOX2 is a BAC-derived and E4 modified AdC68-based viral vector. Preferably said viral vector is an AAV vector. Viral vectors are usually non-replicaƟng or replicaƟon impaired vectors, which means that the viral vector cannot replicate to any significant extent in normal cells (e.g. normal human cells), as measured by convenƟonal means – e.g. via measuring DNA synthesis and / or viral Ɵtre. Non-replicaƟng or replicaƟon impaired vectors may have become so naturally (i.e. they have been isolated as such from nature) or arƟficially (e.g. by breeding in vitro or by geneƟc manipulaƟon). There will generally be at least one cell-type in which the replicaƟon-impaired viral vector can be grown – for example, modified vaccinia Ankara (MVA) can be grown in CEF cells. In one embodiment, the vector is selected from a human or simian adenovirus or a poxvirus vector. Typically, the viral vector is incapable of causing a significant infecƟon in an animal subject, typically in a mammalian subject such as a human or other primate. The vector(s) may be a DNA vector, such as a DNA plasmid. In one embodiment the DNA vector(s) is capable of expression in a mammalian cell expression system, such as an immunised cell. The vector may be suitable for expression in a bacterial and / or insect host cell or expression system, such as any of those exemplified herein. A non-limiƟng example of a suitable expression vector is a pET15b vector, which may be opƟonally modified to encode an N-terminal tag, such as a hexa-hisƟdine tag and / or a protease cleavage site, such as a TEV protease cleavage site. The vector(s) may be an RNA vector, such as a self-amplifying RNA vaccine (Geall, A.J. et al., Proc Natl Acad Sci USA 2012; 109(36) pp.14604-9; incorporated herein by reference). The present invenƟon may be a phage vector, such as an AAV / phage hybrid vector as described in Hajitou et al., Cell 2006; 125(2) pp.385-398; herein incorporated by reference. The anƟbodies of the invenƟon may include a leader sequence, for example to assist in recombinant producƟon and / or secreƟon. Any suitable leader sequence may be used, including convenƟonal leader sequences known in the art. Suitable leader sequences include Bip leader sequences, which are commonly used in the art to aid secreƟon from insect cells and human Ɵssue plasminogen acƟvator leader sequence (tPA), which is rouƟnely also used in viral, and DNA based vaccines and for protein vaccines to aid secreƟon from mammalian cell expression plaƞorms. By way of a non-limiƟng example, the anƟbodies of the invenƟon may include the secretory signal from bovine Ɵssue plasminogen acƟvator or may include another signal to direct the subcellular trafficking of the anƟbodies. AlternaƟvely, the anƟbodies of the invenƟon may be the mature form in which the N- terminal signal pepƟde has been removed. The anƟbodies of the invenƟon may addiƟonally comprise an N- or C-terminal tag, for example to assist in recombinant producƟon and / or purificaƟon. Any N- or C-terminal tag may be used, including convenƟonal tags known in the art. Suitable tags sequences include C-terminal hexa- hisƟdine tags and the “C-tag” (the four amino acids EPEA at the C-terminus), which are commonly used in the art to aid purificaƟon from heterologous expression systems, e.g. insect cells, mammalian cells, bacteria, or yeast. Other examples of suitable tags include GST and MBP tags, or any other convenƟonal tag which may be used to facilitate increased expression. In other embodiments, the anƟbodies of the invenƟon are purified from heterologous expression systems without the need to use a purificaƟon tag. An anƟbody of the invenƟon may be expressed using any suitable systems. For example, anƟbodies of the invenƟon can be generated using such methods as mouse hybridomas, phage display or ribosome display. Other methods known to the person skilled in the art may also be used. The resultant funcƟonal anƟbodies from a mouse immunisaƟon or a phage display screen can then have their sequences (e.g., CDR sequences and / or heavy and light chain variable sequences) confirmed by DNA sequencing or their binding confirmed by epitope mapping. Accordingly, the invenƟon provides a hybridoma expressing any anƟbody (e.g., a neutralising anƟbody or binding fragment thereof) of the invenƟon. AnƟbodies of the invenƟon may be expressed using convenƟonal systems. Such a system may be a prokaryoƟc or a eukaryoƟc system. Examples of such systems are well-known in the art. Non- limiƟng examples of suitable host systems include Escherichia coli, Saccharomyces cerevisiae, Pichia pastoris, non-lyƟc insect cell expression systems such as Schneider 2 (S2) and Schneider 3 (S3) cells from Drosophila melanogaster and Sf9 and Sf21 cells from Spodoptera frugiperda, and mammalian expression systems such as CHO cells and human embryonic kidney (HEK / HEK293) cells (preferably CHO cells). Accordingly, the invenƟon provides a host cell containing a recombinant expression vector which encodes an anƟbody of the invenƟon. Suitable host cells include bacteria, mammalian cells, plant cells, filamentous fungi, yeast and baculovirus systems and transgenic plants and animals. The expression of anƟbodies and anƟbody fragments in prokaryoƟc cells is well established in the art. For a review, see for example PIückthun [PIückthun, A. Bio / Technology 9: 545-551 (1991 )]. A common bacterial host is E. coli. Expression in eukaryoƟc cells in culture is also available to those skilled in the art as an opƟon for producƟon of a binding member [Chadd HE and Chamow SM (2001) Current Opinion in Biotechnology 12: 188-194; Andersen DC and Krumm en L (2002) Current Opinion in Biotechnology 13: 117; Larrick JW and Thomas OW (2001) Current Opinion in Biotechnology 12:411-418]. Mammalian cell lines available in the art for expression of a heterologous polypepƟde include Chinese hamster ovary (CHO) cells, HeLa cells, baby hamster kidney cells, NS0 mouse melanoma cells, YB2 / 0 rat myeloma cells, human embryonic kidney cells, human embryonic reƟna cells and many others. In some preferred embodiments the host cell is a CHO cell. TherapeuƟc IndicaƟons In some aspects, the invenƟon provides an anƟbody, isolated DNA molecule, vector, or composiƟon for use in therapy. For example, in some embodiments, the invenƟon provides an anƟbody, isolated DNA molecule, vector or composiƟon for use in treaƟng and / or prevenƟng malaria. Preferably, the invenƟon provides an anƟbody or composiƟon (e.g., comprising an anƟbody) for use in treaƟng and / or prevenƟng malaria. The present invenƟon also provides a method of sƟmulaƟng or inducing an immune response in a subject comprising administering to the subject an anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon (as described above). Thus, the invenƟon provides a composiƟon comprising an anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon. In one embodiment, the method of sƟmulaƟng or inducing an immune response in a subject comprises administering an anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon (as described above) to a subject. In the context of the therapeuƟc uses and methods, a “subject” is any animal subject that would benefit from sƟmulaƟon or inducƟon of an immune response against a Plasmodium parasite. Typical animal subjects are mammals, such as primates, for example, humans. Thus, the present invenƟon provides a method for treaƟng or prevenƟng malaria. The present invenƟon also provides an anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon for use in the prevenƟon or treatment of malaria. The present invenƟon also provides the use of an anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon in the manufacture of a medicament for the prevenƟon and / or treatment of malaria. The present invenƟon provides the use of an anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon for use either alone or in combinaƟon in the prevenƟon or treatment of malaria. In one embodiment, the method for treaƟng or prevenƟng malaria comprises administering a therapeuƟcally effecƟve amount of an anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon, either alone or in combinaƟon, to a subject. As used herein, the term “treatment” or “treaƟng” embraces therapeuƟc or preventaƟve / prophylacƟc measures and includes post-infecƟon therapy and amelioraƟon of malaria. As used herein, the term “prevenƟng” includes prevenƟng the iniƟaƟon of malaria and / or reducing the severity or intensity of malaria. The term “prevenƟng” includes inducing or providing protecƟve immunity against malaria. Immunity to malaria may be quanƟfied using any appropriate technique, examples of which are known in the art. An anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon may be administered to a subject (typically a mammalian subject such as a human or other primate) already having malaria, a condiƟon or symptoms associated with malaria, to treat or prevent malaria. For example, the subject may be suspected of having come in interfacing with Plasmodium parasite, or has had known interfacing with Plasmodium parasite, but is not yet showing symptoms of exposure. When administered to a subject (e.g. a mammal such as a human or other primate) that already has malaria, or is showing symptoms associated with Plasmodium parasite infecƟon, an anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon (as described above) can cure, delay, reduce the severity of, or ameliorate one or more symptoms, and / or prolong the survival of a subject beyond that expected in the absence of such treatment. AlternaƟvely, an anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon (as described above) may be administered to a subject (e.g. a mammal such as a human or other primate) who ulƟmately may be infected with Plasmodium parasite, in order to prevent, cure, delay, reduce the severity of, or ameliorate one or more symptoms of malaria, or in order to prolong the survival of a subject beyond that expected in the absence of such treatment, or to help prevent that subject from transmiƫng malaria. The treatments and preventaƟve therapies of the present invenƟon are applicable to a variety of different subjects of different ages. In the context of humans, the therapies are applicable to children (e.g. infants, children under 5 years old, older children or teenagers) and adults. In the context of other animal subjects (e.g. mammals such as primates), the therapies are applicable to immature subjects and mature / adult subjects. The present invenƟon provides an anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon (described herein). Said composiƟons may further comprise one or more further components as described herein. The lack of polymorphism at the PfRH5 locus (five non-synonymous SNP across its enƟre length in circulaƟng P. falciparum parasites) suggest either a lack of substanƟal immune pressure, or a high degree of funcƟonal constraint that prevents mutaƟons from freely occurring. This property makes it highly likely that the anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon (described herein) preferably have broadly neutralising acƟvity. Thus, the anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon (described herein) typically provide a highly effecƟve cross-strain GIA against the Plasmodium parasite. Thus, in one embodiment, the invenƟon provides protecƟon (such as long-term protecƟon) against disease caused by Plasmodium parasites. Typically, an anƟbody of the invenƟon, composiƟon of the invenƟon, or one or more vectors of the invenƟon provides an anƟbody response (e.g. a neutralising anƟbody response) to Plasmodium parasiƟc infecƟon. The treatment and / or prevenƟon of malaria according to the present invenƟon may further comprise boosƟng a subject. Such “boosƟng” may comprise the administraƟon of a pox virus, such as MVA. AnƟbody combinaƟons In some embodiments, the present invenƟon provides an anƟbody for use in a method for prevenƟng or treaƟng malaria, the method comprising administering the anƟbody of the invenƟon and one or more addiƟonal (e.g., a second) anƟ-malarial anƟbody to a subject, wherein the anƟbody of the invenƟon and the one or more addiƟonal anƟ-malarial anƟbody are administered simultaneously or sequenƟally; opƟonally wherein the second anƟ-malarial anƟbody is selected from the list consisƟng of monoclonal anƟbody CIS43LS (see, NCT04206332 and Gaudinski et al., A Monoclonal AnƟbody for Malaria PrevenƟon. N Engl J Med.2021 Aug 26;385(9):803-814, Kayentao et al., Safety and Efficacy of a Monoclonal AnƟbody against Malaria in Mali. N Engl J Med. 2022 Nov 17;387(20):1833-1842 and Lyke et al., Low-dose intravenous and subcutaneous CIS43LS monoclonal anƟbody for protecƟon against malaria (VRC 612 Part C): a phase 1, adapƟve trial. Lancet Infect Dis. 2023 May;23(5):578-588 which are incorporated herein by reference), monoclonal anƟbody L9LS (see, NCT05019729 and Wu et al., Low-Dose Subcutaneous or Intravenous Monoclonal AnƟbody to Prevent Malaria. N Engl J Med. 2022 Aug 4;387(5):397-407, which is incorporated herein by reference) and monoclonal anƟbody TB31F (see, NCT04238689 and van der Boor et al., Safety, tolerability, and Plasmodium falciparum transmission-reducing acƟvity of monoclonal anƟbody TB31F: a single-centre, open-label, first-in-human, dose-escalaƟon, phase 1 trial in healthy malaria-naive adults. Lancet Infect Dis.2022 Nov;22(11):1596-1605, which is incorporated herein by reference). The present invenƟon also provides an anƟbody for use in a method for prevenƟng or treaƟng malaria, the method comprising administering an anƟbody of the invenƟon to a subject that has been administered, is being administered, or will be administered a second anƟ-malarial anƟbody; opƟonally wherein the second anƟ-malarial anƟbody is selected from the list consisƟng of monoclonal anƟbody CIS43LS (see, NCT04206332), monoclonal anƟbody L9LS (see, NCT05019729) and monoclonal anƟbody TB31F (see, NCT04238689). The present invenƟon also provides an anƟbody for use in a method for prevenƟng or treaƟng malaria, the method comprising administering an anƟ-malarial anƟbody selected from the list consisƟng of monoclonal anƟbody CIS43LS (see, NCT04206332), monoclonal anƟbody L9LS (see, NCT05019729) and monoclonal anƟbody TB31F (see, NCT04238689) to a subject that has been administered, is being administered, or will be administered an anƟbody of the invenƟon. As used herein, the term “simultaneously” is used to describe the administraƟon of an anƟbody of the invenƟon and a second anƟ-malarial anƟbody at the same Ɵme. In one embodiment, simultaneous administraƟon refers to the administraƟon of an anƟbody of the invenƟon and a second anƟ-malarial anƟbody at the same administraƟon site. In another embodiment, simultaneous administraƟon refers to the administraƟon of an anƟbody of the invenƟon and a second anƟ-malarial anƟbody at different administraƟon sites. As used herein, the term “sequenƟally” is used to describe the administraƟon of the anƟbody of the invenƟon and second anƟ-malarial anƟbody at different Ɵmes. When administered sequenƟally, the anƟbody of the invenƟon and the second anƟ-malarial anƟbody may be administered in any order. In one embodiment, the anƟbody of the invenƟon is administered before the second anƟ-malarial anƟbody. In another embodiment, the second anƟ-malarial anƟbody is administered before the anƟbody of the invenƟon. In some embodiments, the one or more addiƟonal anƟbody is a non-neutralising anƟbody, or binding fragment thereof, that specifically binds a non-neutralising anƟbody epitope (e.g., an epitope corresponding to residues Ser153 to Ile163 and Asp305 to Lys319 of PfRH5). The one or more non-neutralising anƟbody may be any non-neutralising anƟbody as described herein. In specific embodiments, the non-neutralising anƟbody is a non-neutralising anƟbody as disclosed in WO 2020 / 074908, which is incorporated herein by reference. The combinaƟon of a non-neutralising anƟbody of the invenƟon and a neutralising anƟbody of the invenƟon may be in the form of two separate anƟbody molecules or binding fragments thereof. In which case, the anƟbodies may be used or administered (or in the case of a therapeuƟc indicaƟon) sequenƟally or simultaneously, with simultaneous use or administraƟon being preferred. If the use / administraƟon is sequenƟal, preferably the non-neutralising anƟbody is used / administered first. AlternaƟvely, the non-neutralising anƟbody or binding fragment thereof and the neutralising anƟbody or binding fragment thereof may be in the form of a single molecule. Thus, the invenƟon provides bispecific molecules comprising both a non-neutralising anƟbody or binding fragment thereof and a neutralising anƟbody or binding fragment thereof. Such bispecific molecules include fusion proteins, trifuncƟonal anƟbodies, F(ab’)2, bispecific T-cell engager molecules, dual-variable-domain immunoglobulins (DVD-Ig™, in which the anƟgen-binding variable domains of two monoclonal anƟbodies are combined via linkers (typically naturally occurring linkers) to create a tetravalent, dual- targeƟng single agent). Examples of bispecific anƟbody structures are well known in the art, as are methods for their producƟon, including the so-called “Knobs-into-Holes” (KiH) approach, the controlled Fab arm exchange method (cFAE) and using scFvs. As well as use or administraƟon of the non-neutralising anƟbodies and neutralising anƟbodies of the invenƟon in protein (i.e. anƟbody) form as discussed above, the non-neutralising and neutralising anƟbodies of the invenƟon may be used or administered in any other appropriate form. In some embodiments, one or more non-neutralising anƟbody is generated in vivo. In vivo generaƟon of said anƟbodies may be via the administraƟon of one or more vector (e.g. a viral vector, RNA vaccine or DNA plasmid) which encodes, and expresses said one or more non-neutralising anƟbody. AlternaƟvely, in vivo generaƟon of said anƟbodies may be by the administraƟon of a vector or vaccine which (i) delivers an anƟgen which will induce the immune system to make said one or more non-neutralising anƟbody, or (ii) encodes or expresses an anƟgen which will then induce the immune system to make said one or more non-neutralising anƟbody; or (iii) natural exposure to malaria. The combinaƟon of a non-neutralising anƟbody of the invenƟon and a malarial vaccine may be used or administered (or in the case of a therapeuƟc indicaƟon) sequenƟally or simultaneously. If the use / administraƟon is sequenƟal, preferably the malarial vaccine is used / administered first. The non-neutralising anƟbodies may be used or administered as a vector encoding said non- neutralising anƟbody. Any combinaƟon of delivery method may be used for the non-neutralising anƟbodies and neutralising anƟbodies of the invenƟon. In parƟcular, the non-neutralising anƟbody may be delivered by a means selected from vaccine inducƟon, in vivo vector generaƟon or direct anƟbody protein delivery as described herein, or a combinaƟon thereof, and independently the neutralising anƟbody may be delivered by direct anƟbody protein delivery. In some preferred embodiments both the neutralising and non-neutralising anƟbodies are given directly as protein anƟbodies. Regardless of how the non-neutralising anƟbody is delivered (e.g. as a protein anƟbody, expressed in vivo by a vector or plasmid of the invenƟon or generated in vivo by the administraƟon of a malarial vaccine (protein, virus-like parƟcle or any other type of vaccine, examples of which are described herein)), or how the neutralising anƟbody is delivered (e.g. as a protein anƟbody), a non- neutralising anƟbody of the invenƟon can synergise the acƟvity of the neutralising anƟbodies as described herein. The non-neutralising anƟbodies of the invenƟon are able to potenƟate or synergise the acƟvity of the neutralising anƟbodies. The terms potenƟate and synergise (or variants thereof) are used interchangeably herein. By potenƟaƟon, it is meant that the non-neutralising anƟbody increases the effect of the neutralising anƟbody beyond the effect obtained using the non-neutralising anƟbody alone. This can be quanƟfied in any suitable way and measured using convenƟonal means, as exemplified in the Examples herein. Typically, a non-neutralising anƟbody of the invenƟon or binding fragment thereof reduces the amount or concentraƟon of neutralising anƟbody required to obtain the desired inhibitory effect on the Plasmodium parasite. As a non-limiƟng example, a non-neutralising anƟbody or binding fragment thereof of the invenƟon may decrease the EC80value of a neutralising anƟbody or binding fragment thereof by at least two-fold, at least three-fold, at least four-fold, at least five-fold, at least six-fold, at least seven-fold, at least eight-fold, at least nine-fold, at least ten-fold or more compared with the EC80value of the neutralising anƟbody or binding fragment thereof alone. In some preferred embodiments, the non-neutralising anƟbody or binding fragment thereof decreases the EC80value of the neutralising anƟbody or binding fragment thereof by at least five-fold, more preferably at least seven-fold, even more preferably at least nine-fold or more compared with the EC80value of the neutralising anƟbody or binding fragment thereof alone. Typically, the maximum synergisƟc effect of a non-neutralising anƟbody of the invenƟon or binding fragment thereof is achieved using a concentraƟon of greater than 1 µg / ml, greater than 10 µg / ml, greater than 50 µg / ml, greater than 100 µg / ml, greater than 150 µg / ml, greater than 200 µg / ml, greater than 250 µg / ml, greater than 300 µg / ml, or more of the non-neutralising anƟbody or binding fragment thereof. In some preferred embodiments, the maximum synergisƟc effect of a non- neutralising anƟbody of the invenƟon or binding fragment thereof is achieved using a concentraƟon of greater than 150 µg / ml, even more preferably greater than 200 µg / ml of the non-neutralising anƟbody or binding fragment thereof. The raƟo of a neutralising anƟbody or binding fragment thereof to non-neutralising anƟbody or binding fragment thereof (nAb:non-nAb) may be about 2:1, about 2.5:1, about 3:1, about 3.5:1, about 4:1 or about 4.5:1. Typically the nAb:non-nAb raƟo is about 4:1. The lower the concentraƟon of neutralising anƟbody or binding fragment thereof, the greater the effect of nAb-biased raƟos. Thus, for concentraƟons of neutralising anƟbody (or binding fragment thereof) below 100 µg / ml, a nAb:non- nAb raƟo of 4:1 is preferred. However, at neutralising anƟbody (or binding fragment thereof) concentraƟons above 100 µg / ml, the nAb:non-nAb has less effect, with nAb:non-nAb raƟos in the range of 1:4 to 4:1 being roughly equivalent. PharmaceuƟcal ComposiƟons and FormulaƟons The anƟbody of the invenƟon (as defined above) can be combined or administered in addiƟon to a pharmaceuƟcally acceptable carrier. AlternaƟvely, or in addiƟon the anƟbody of the invenƟon can further be combined with one or more of a salt, excipient, diluent, adjuvant, immunoregulatory agent and / or anƟmicrobial compound. The term “anƟbody” is herein used interchangeably with the terms “therapeuƟc / prophylacƟc composiƟon”, “formulaƟon” or “medicament”. PharmaceuƟcally acceptable salts include acid addiƟon salts formed with inorganic acids such as, for example, hydrochloric or phosphoric acids, or with organic acids such as aceƟc, oxalic, tartaric, maleic, and the like. Salts formed with the free carboxyl groups may also be derived from inorganic bases such as, for example, sodium, potassium, ammonium, calcium, or ferric hydroxides, and such organic bases as isopropylamine, trimethylamine, 2-ethylamino ethanol, hisƟdine, procaine, and the like. AdministraƟon of immunogenic composiƟons, therapeuƟc formulaƟons, medicaments, and prophylacƟc formulaƟons (e.g. anƟbodies) is generally by convenƟonal routes e.g. intravenous, subcutaneous, intraperitoneal, or mucosal routes. The administraƟon may be by parenteral injecƟon, for example, a subcutaneous, intradermal, or intramuscular injecƟon. FormulaƟons comprising neutralizing anƟbodies may be parƟcularly suited to administraƟon intravenously, intramuscularly, intradermally, or subcutaneously. Accordingly, immunogenic composiƟons, therapeuƟc formulaƟons, medicaments, and prophylacƟc formulaƟons (e.g. anƟbodies) of the invenƟon are typically prepared as injectables, either as liquid soluƟons or suspensions. Solid forms suitable for soluƟon in, or suspension in, liquid prior to injecƟon may alternaƟvely be prepared. The preparaƟon may also be emulsified, or the pepƟde encapsulated in liposomes or microcapsules. The acƟve immunogenic ingredients are oŌen mixed with excipients which are pharmaceuƟcally acceptable and compaƟble with the acƟve ingredient. Suitable excipients are, for example, water, saline, dextrose, glycerol, ethanol, or the like and combinaƟons thereof. In addiƟon, if desired, the composiƟon may contain minor amounts of auxiliary substances such as weƫng or emulsifying agents, pH buffering agents, and / or adjuvants which enhance the effecƟveness of the vaccine. Generally, the carrier is a pharmaceuƟcally-acceptable carrier. Non-limiƟng examples of pharmaceuƟcally acceptable carriers include water, saline, and phosphate-buffered saline. In some embodiments, however, the composiƟon is in lyophilized form, in which case it may include a stabilizer, such as BSA. In some embodiments, it may be desirable to formulate the composiƟon with a preservaƟve, such as thiomersal or sodium azide, to facilitate long term storage. Examples of addiƟonal adjuvants which may be effecƟve include but are not limited to: complete Freund’s adjuvant (CFA), Incomplete Freund’s adjuvant (IFA), Saponin, a purified extract fracƟon of Saponin such as Quil A, a derivaƟve of Saponin such as QS-21, lipid parƟcles based on Saponin such as ISCOM / ISCOMATRIX, E. coli heat labile toxin (LT) mutants such as LTK63 and / or LTK72, aluminium hydroxide, N-acetyl-muramyl-L-threonyl-D-isoglutamine (thr-MDP), N-acetyl-nor-muramyl- L-alanyl-D-isoglutamine (CGP 11637, referred to as nor-MDP), N-acetylmuramyl-L-alanyl-D- isoglutaminyl-L-alanine-2-(1’-2’-dipalmitoyl-sn-glycero-3-hydroxyphosphoryl oxy)-ethylamine (CGP 19835A, referred to as MTP-PE), and RIBI, which contains three components extracted from bacteria, monophosphoryl lipid A, trehalose dimycolate and cell wall skeleton (MPL+TDM+CWS) in a 2 % squalene / Tween 80 emulsion, the MF59 formulaƟon developed by NovarƟs, and the AS02, AS01, AS03 and AS04 adjuvant formulaƟons developed by GSK Biologicals (Rixensart, Belgium). Examples of buffering agents include, but are not limited to, sodium succinate (pH 6.5), and phosphate buffered saline (PBS; pH 6.5 and 7.5). AddiƟonal formulaƟons which are suitable for other modes of administraƟon include suppositories and, in some cases, oral formulaƟons or formulaƟons suitable for distribuƟon as aerosols. For suppositories, tradiƟonal binders and carriers may include, for example, polyalkylene glycols or triglycerides; such suppositories may be formed from mixtures containing the acƟve ingredient in the range of 0.5% to 10%, preferably 1%-2%. Oral formulaƟons include such normally employed excipients as, for example, pharmaceuƟcal grades of mannitol, lactose, starch, magnesium stearate, sodium saccharine, cellulose, magnesium carbonate, and the like. These composiƟons take the form of soluƟons, suspensions, tablets, pills, capsules, sustained release formulaƟons or powders. It is within the rouƟne pracƟce of a clinician to determine an effecƟve amount of an anƟbody or vaccine composiƟon (preferably an anƟbody composiƟon) of the invenƟon. An effecƟve amount is an amount sufficient to elicit a protecƟve immune response against malaria. A clinician will also be able to determine appropriate dosage interval using rouƟne skill. Kits A kit comprising an anƟbody or anƟgen-binding fragment thereof as described herein is also provided as an aspect of the present disclosure. In certain embodiments, the anƟbody or anƟgen- binding fragment thereof is an isolated anƟbody molecule of the disclosure, or anƟgen-binding fragment thereof. In certain embodiments, the anƟbody comprises the set of HCDRs and LCDRs of any anƟbody, as described herein, with the anƟbody R5.034, or an anƟgen-binding fragment thereof, being parƟcularly preferred. In the kit, the anƟbody or anƟgen-binding fragment thereof may be labelled to allow its reacƟvity in a sample to be determined, e.g., as described further below. Further, the binding member may or may not be aƩached to a solid support. Components of a kit are generally sterile and in sealed vials or other containers. Kits may be employed in diagnosƟc analysis or other methods for which binding members are useful. A kit may be for use in a method described above. A kit may contain instrucƟons for use of the components in a method, e.g., a method in accordance with the present disclosure. Ancillary materials to assist in or to enable performing such a method may be included within a kit of the disclosure. The ancillary materials include a second, different anƟbody or anƟgen- binding fragment thereof which binds to the first anƟbody or anƟgen-binding fragment thereof and is conjugated to a detectable label (e.g., a fluorescent label, radioacƟve isotope, or enzyme). AnƟbody- based kits may also comprise beads for conducƟng an immunoprecipitaƟon. Each component of the kits is generally in its own suitable container. Thus, these kits generally comprise disƟnct containers suitable for each anƟbody or anƟgen-binding fragment thereof. Further, the kits may comprise instrucƟons for performing the assay and methods for interpreƟng and analysing the data resulƟng from the performance of the assay. The present disclosure also provides the use of an anƟbody or anƟgen-binding fragment thereof as above for measuring anƟgen levels in a compeƟƟon assay, that is to say a method of measuring the level of anƟgen in a sample by employing a anƟbody or anƟgen-binding fragment thereof as provided by the present disclosure in a compeƟƟon assay. This may be where the physical separaƟon of bound from unbound anƟgen is not required. Linking a reporter molecule to the binding member so that a physical or opƟcal change occurs on binding is one possibility. The reporter molecule may directly or indirectly generate detectable signals, which may be quanƟfiable. The linkage of reporter molecules may be directly or indirectly, covalently, e.g., via a pepƟde bond or non-covalently. Linkage via a pepƟde bond may be as a result of recombinant expression of a gene fusion encoding anƟbody and reporter molecule. CompeƟƟon between anƟbodies may be assayed easily in vitro, for example using ELISA and / or by a biochemical compeƟƟon assay such as one tagging a specific reporter molecule to one anƟbody or anƟgen-binding fragment thereof which can be detected in the presence of one or more other untagged anƟbodies or anƟgen-binding fragments thereof, to enable idenƟficaƟon of anƟbodies or anƟgen-binding fragments thereof which bind the same epitope or an overlapping epitope. Such methods are readily known to one of ordinary skill in the art, and are described in more detail herein. Labels AnƟbodies or binding fragments thereof may be labelled with a detectable or funcƟonal label. Thus, an anƟbody can be present in the form of an immunoconjugate so as to obtain a detectable and / or quanƟfiable signal. An immunoconjugate may comprise an anƟbody molecule of the disclosure conjugated with detectable or funcƟonal label. A detectable label as referred to herein may be any label which produces or can be induced to produce a signal, including but not limited to fluorescers, chemiluminescers (e.g., horseradish peroxidase), coloured labels (e.g. latex [blue] or colloidal gold [red]), radiolabels, enzymes, photosensiƟsers, and magneƟc labels. The amount of label bound at a surface, e.g., a surface of a capillary bore, may therefore be detected and / or measured by detecƟng fluorescence or luminescence, colour, radioacƟvity, enzyme acƟvity, light absorbance, or changes in magneƟc field. Detectable labels may be aƩached to anƟbodies using convenƟonal chemistry. Preferably, a detectable label is a label detectable by opƟcal interrogaƟon, e.g., with a digital camera or flatbed scanner. Labels that can be detected by opƟcal interrogaƟon include fluorescers, chemiluminescers and coloured labels. The mechanism by which a signal can be generated for opƟcal detecƟon includes (but is not necessarily limited to): light absorpƟon, light scaƩering, light diffracƟon, light reflecƟon, fluorescence, or luminescence. Suitable labels include, by way of illustraƟon and not limitaƟon, - enzymes, such as alkaline phosphatase, glucose-6-phosphate dehydrogenase ("G6PDH"), alpha-D-galactosidase, glucose oxydase, glucose amylase, carbonic anhydrase, acetylcholinesterase, lysozyme, malate dehydrogenase and peroxidase, e.g., horseradish peroxidase; - dyes; - fluorescent labels or fluorescers, such as fluorescein and its derivaƟves, fluorochrome, rhodamine compounds and derivaƟves, GFP (GFP for "Green Fluorescent Protein"), dansyl, umbelliferone, phycoerythrin, phycocyanin, allophycocyanin, o-phthaldehyde, and fluorescamine; fluorophores such as lanthanide cryptates and chelates, e.g., Europium etc (Perkin Elmer and Cis BiointernaƟonal), - chemoluminescent labels or chemiluminescers, such as isoluminol, luminol and the dioxetanes; - bio-luminescent labels, such as luciferase and luciferin; - sensiƟzers; - coenzymes; - enzyme substrates; - radiolabels, including but not limited to, bromine77, carbon14, cobalt57, fluorine8, gallium67, gallium68, hydrogen3(triƟum) indium111, indium113m, iodine123m, iodine125, iodine126, iodine131, iodine133, mercury107, mercury203, phosphorous32, rhenium99m, rhenium101, rhenium105, ruthenium95, ruthenium97, ruthenium103, ruthenium105, scandium47, selenium75, sulphur35, techneƟum99, techneƟum99m, tellurium121m, tellurium122m, tellurium125m, thulium165, thulium167, thulium168, yƩrium199and other radio labels menƟoned herein; - parƟcles, such as latex or carbon parƟcles; metal sol; crystallite; liposomes; cells, etc., which may be further labelled with a dye, catalyst, or other detectable group; - molecules such as bioƟn, digoxygenin or 5-bromodeoxyuridine; - toxin moieƟes, such as for example a toxin moiety selected from a group of Pseudomonas exotoxin (PE or a cytotoxic fragment or mutant thereof), Diptheria toxin or a cytotoxic fragment or mutant thereof, a Botulinum toxin A, B, C, D, E or F, ricin, or a cytotoxic fragment thereof e.g. ricin A, abrin or a cytotoxic fragment thereof, saporin or a cytotoxic fragment thereof, pokeweed anƟviral toxin or a cytotoxic fragment thereof and bryodin 1 or a cytotoxic fragment thereof. SEQUENCE INFORMATION SEQ ID NO: 1: R5.034 heavy chain CDR1 GFTFNTYW SEQ ID NO: 2: R5.034 heavy chain CDR2 IQQDGSEK SEQ ID NO: 3: R5.034 heavy chain CDR3 ARDNPASAVAFDV SEQ ID NO: 4: R5.034 light chain CDR1 SSNIGNNA SEQ ID NO: 5: R5.034 light chain CDR2 FDD SEQ ID NO: 6: R5.034 light chain CDR3 AAWDDRLNGVV SEQ ID NO: 7: R5.102 heavy chain CDR1 GFTFSSYW SEQ ID NO: 8: R5.102 heavy chain CDR2 INQDGSEK SEQ ID NO: 9: R5.102 heavy chain CDR3 ARVVVVTASAFDS SEQ ID NO: 10: R5.102 light chain CDR1 SSNIGNNA SEQ ID NO: 11: R5.102 light chain CDR2 YDD SEQ ID NO: 12: R5.102 light chain CDR3 AAWDDSLNGLV SEQ ID NO: 13: R5.159 heavy chain CDR1 GFTFDDYV SEQ ID NO: 14: R5.159 heavy chain CDR2 ISWNSDNI SEQ ID NO: 15: R5.159 heavy chain CDR3 VKDTLSTVSTYVFHS SEQ ID NO: 16: R5.159 light chain CDR1 NIGSKS SEQ ID NO: 17: R5.159 light chain CDR2 DDS SEQ ID NO: 18: R5.159 light chain CDR3 QVWDTTSDHPV SEQ ID NO: 19: R5.237 heavy chain CDR1 GFTFSSYW SEQ ID NO: 20: R5.237 heavy chain CDR2 IKHDGTEK SEQ ID NO: 21: R5.237 heavy chain CDR3 ARTGYISSWTLDY SEQ ID NO: 22: R5.237 light chain CDR1 SSNIGNNA SEQ ID NO: 23: R5.237 light chain CDR2 YDD SEQ ID NO: 24: R5.237 light chain CDR3 AAWDDSLNGGV SEQ ID NO: 25: R5.268 heavy chain CDR1 GFTFSRYE SEQ ID NO: 26: R5.268 heavy chain CDR2 ISSSGSMI SEQ ID NO: 27: R5.268 heavy chain CDR3 ARATGSSGHFDY SEQ ID NO: 28: R5.268 light chain CDR1 NIGSKS SEQ ID NO: 29: R5.268 light chain CDR2 DDS SEQ ID NO: 30: R5.268 light chain CDR3 QVWDISSDHRV SEQ ID NO: 31: R5.270 heavy chain CDR1 GFTFSSYW SEQ ID NO: 32: R5.270 heavy chain CDR2 IKQDGSEK SEQ ID NO: 33: R5.270 heavy chain CDR3 ARVGVVVAATLDY SEQ ID NO: 34: R5.270 light chain CDR1 SSNIGNNA SEQ ID NO: 35: R5.270 light chain CDR2 FDD SEQ ID NO: 36: R5.270 light chain CDR3 AAWDDSLNGLV SEQ ID NO: 37: R5.034 heavy chain variable region EVQLVESGGGLVQPGGSLRLSCAASGFTFNTYWMSWVRQAPGKGLEWVANIQQDGSEKDYLNSVRGRFTISRDN AKKSLYLQMNSLRAEDTAVYYCARDNPASAVAFDVWGQGAMVTVSS SEQ ID NO: 38: R5.034 light chain variable region QSALTQPPSVSEAPRRRVTIYCSGSSSNIGNNAVSWYQQLPGKSPKLLIYFDDLVTSGVSDRFSGSKSGTSASLAISGL QSEDEADYYCAAWDDRLNGVVFGGGTKLTVL SEQ ID NO: 39: R5.102 heavy chain variable region EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYWMTWVRQAPGKGLEWVANINQDGSEKYYVDSVKGRFTISRDN AKKSLYLQMNSLRAEDTAVYYCARVVVVTASAFDSWGQGTMVTVSS SEQ ID NO: 40: R5.102 light chain variable region QSVLTQPPSVSEAPRQRVTISCSGSSSNIGNNAVNWYQQLPGKAPQLLIYYDDLLPSGVSDRFSGSKSGTSASLAISG LQSEDEADYYCAAWDDSLNGLVFGGGTKLTVL SEQ ID NO: 41: R5.159 heavy chain variable region EVQLVESGGGLVQPGRSLRLSCAASGFTFDDYVMHWVRQTPGKGLEWVSSISWNSDNIDYADSVKGRFTISRDNA KNSLYLQMNSLRSEDTAFYYCVKDTLSTVSTYVFHSWGQGTLVTVSS SEQ ID NO: 42: R5.159 light chain variable region SSELTQPPSVSVAPGQTARITCGGNNIGSKSVHWYQQKPGQAPVMVVHDDSDRPSGIPERLSGSNSGNTATLTISR VEAGDEADYYCQVWDTTSDHPVFGGGTKLTVL SEQ ID NO: 43: R5.237 heavy chain variable region EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYWMTWVRQAPGKGLEWVANIKHDGTEKYYVDSVKGRFTISRDNA RNSLYLQMNSLRAEDTAVYYCARTGYISSWTLDYWGQGTLVTVSS SEQ ID NO: 44: R5.237 light chain variable region QSVLTQPPSVSEAPRQRVTISCSGSSSNIGNNAVNWYQQLPGKAPKLLIYYDDLLPSGVSDRFSGSKSGTSASLAISGL QSEDEADYYCAAWDDSLNGGVFGGGTKLTVL SEQ ID NO: 45: R5.268 heavy chain variable region EVQLVESGGGLVQPGGSLRLSCAASGFTFSRYEMNWVRQAPGKGLVWISYISSSGSMIYYADSVKGRFTVSRDNAK KSLYLQMNSLRAEDTAVYYCARATGSSGHFDYWGQGTLVTVSS SEQ ID NO: 46: R5.268 light chain variable region NFMLTQPPSVSVAPGQTARITCGGNNIGSKSVHWYQQKPGQAPVLVVYDDSDRPSGIPERFSGSNSGNTATLTISRV EAGDEADYYCQVWDISSDHRVFGGGTKLTVL SEQ ID NO: 47: R5.270 heavy chain variable region EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVANIKQDGSEKYYVDSVKGRFTISRDNA KNSLHLQMNSLRPEDTAVYFCARVGVVVAATLDYWGQGTLVTVSS SEQ ID NO: 48: R5.270 light chain variable region QSVLTQPPSVSEAPRQRVTISCSGSSSNIGNNAVNWYQQLPRKAPKLLIYFDDLLPSGVSDRFSGSKSGTSASLAISGL QSEDEADYYCAAWDDSLNGLVFGGGTKLTVL SEQ ID NO: 49: R5.016 heavy chain CDR1 GYTFTSYG SEQ ID NO: 50: R5.016 heavy chain CDR2 ISGYDGNT SEQ ID NO: 51: R5.016 heavy chain CDR3 ARDGPQVGDFDWQVYYYYGMDV SEQ ID NO: 52: R5.016 light chain CDR1 QSINTW SEQ ID NO: 53: R5.016 light chain CDR2 KAS SEQ ID NO: 54: R5.016 light chain CDR3 QQYNSYLYT SEQ ID NO: 55: R5.016 VH QVQLVQSGAEVKKPGASVRVSCKASGYTFTSYGISWVRQAPGQGLEWMGWISGYDGNTNYAQKLQGRVTMTTD TSTSTAYMELRSLRSDDTAVYYCARDGPQVGDFDWQVYYYYGMDVWGQGTTVTVSS SEQ ID NO: 56: R5.016 VL AIRMTQSPSTLSASVGDRVTITCRASQSINTWLAWYQQKPGKAPNLLISKASSLESGVPSRFSGSGSGTEFTLTISSLQ PDDFATYFCQQYNSYLYTFGQGTKVEIR SEQ ID NO: 57: R5.016 heavy chain framework region (FR) 1 QVQLVQSGAEVKKPGASVRVSCKASGYTFT SEQ ID NO: 58: R5.016 heavy chain framework region (FR) 2 WVRQAPGQGLEWMG SEQ ID NO: 59: R5.016 heavy chain framework region (FR) 3 RVTMTTDTSTSTAYMELRSLRSDDTAVYYCAR SEQ ID NO: 60: R5.016 heavy chain framework region (FR) 4 WGQGTTVTVSS SEQ ID NO: 61: R5.016 heavy chain framework region (FR) 1 AIRMTQSPSTLSASVGDRVTITC SEQ ID NO: 62: R5.016 heavy chain framework region (FR) 2 WYQQKPGKAPNLLIS SEQ ID NO: 63: R5.016 heavy chain framework region (FR) 3 GVPSRFSGSGSGTEFTLTISSLQPDDFATYFC SEQ ID NO: 64: R5.016 heavy chain framework region (FR) 4 FGQGTKVEIRRTV SEQ ID NO: 65: Full length PfRH5 amino acid sequence (3D7) including signal sequence 1 MIRIKKKLIL TIIYIHLFIL NRLSFENAIK KTKNQENNLT LLPIKSTEEE KDDIKNGKDI 61 KKEIDNDKEN IKTNNAKDHS TYIKSYLNTN VNDGLKYLFI PSHNSFIKKY SVFNQINDGM 121 LLNEKNDVKN NEDYKNVDYK NVNFLQYHFK ELSNYNIANS IDILQEKEGH LDFVIIPHYT 181 FLDYYKHLSY NSIYHKSSTY GKCIAVDAFI KKINETYDKV KSKCNDIKND LIATIKKLEH 241 PYDINNKNDD SYRYDISEEI DDKSEETDDE TEEVEDSIQD TDSNHTPSNK KKNDLMNRTF 301 KKMMDEYNTK KKKLIKCIKN HENDFNKICM DMKNYGTNLF EQLSCYNNNF CNTNGIRYHY 361 DEYIHKLILS VKSKNLNKDL SDMTNILQQS ELLLTNLNKK MGSYIYIDTI KFIHKEMKHI 421 FNRIEYHTKI INDKTKIIQD KIKLNIWRTF QKDELLKRIL DMSNEYSLFI TSDHLRQMLY 481 NTFYSKEKHL NNIFHHLIYV LQMKFNDVPI KMEYFQTYKK NKPLTQ • Signal sequence (amino acids 1 to 23) is in bold italics, flexible N-terminal (amino acids 1 to 139) and flexible loop (amino acids 248 to 296) regions are underlined. • The (disconƟnuous) epitope for the non-neutralising anƟbodies of the invenƟon is shown in broken underline. • The (disconƟnuous) epitope for the neutralising mAb4 anƟbody of the invenƟon is shown in double underline. • The (disconƟnuous) epitope for the neutralising mAb16 anƟbody of the invenƟon is shown in wavy underline. SEQ ID NO: 66: Full length PfRH5 amino acid sequence (7G8) including signal sequence 1 MIRIKKKLIL TIIYIHLFIL NRLSFENAIK KTKNQENNLT LLPIKSTEEE KDDIKNGKDI 61 KKEIDNDKEN IKTNNAKDHS TYIKSYLNTN VNDGLKYLFI PSHNSFIKKY SVFNQINDGM 121 LLNEKNDVKN NEDYKNVDYK NVNFLQYHFK ELSNYNIANS IDILQEKEGH LDFVIIPHYT 181 FLDYYKHLSY NSIYHKSSTY GKYIAVDAFI KKINETYDKV KSKCNDIKND LIATIKKLEH 241 PYDINNKNDD SYRYDISEEI DDKSEETDDE TEEVEDSIQD TDSNHTPSNK KKNDLMNRTF 301 KKMMDEYNTK KKKLIKCIKN HENDFNKICM DMKNYGTNLF EQLSCYNNNF CNTNGIRYHY 361 DEYIHKLILS VKSKNLNKDL SDMTNILQQS ELLLTNLNKK MGSYIYIDTI KFIHKEMKHI 421 FNRIEYHTKI INDKTKIIQD KIKLNIWRTF QKDELLKRIL DMSNEYSLFI TSDHLRQMLY 481 NTFYSKEKHL NNIFHHLIYV LQMKFNDVPI KMEYFQTYKK NKPLTQ • Signal sequence (amino acids 1 to 23) is in bold italics, flexible N-terminal (amino acids 1 to 139) and flexible loop (amino acids 248 to 296) regions are underlined. • The (disconƟnuous) epitope for the non-neutralising anƟbodies of the invenƟon is shown in broken underline. • The (disconƟnuous) epitope for the neutralising mAb4 anƟbody of the invenƟon is shown in double underline. • The (disconƟnuous) epitope for the neutralising mAb16 anƟbody of the invenƟon is shown in wavy underline. SEQ ID NO: 67: PfRH5 amino acid sequence (3D7) excluding signal sequence and flexible N-terminal region (amino acids 1 to 139) (3D7 RH5ΔN) 1 KNVNFLQYHF KELSNYNIAN SIDILQEKEG HLDFVIIPHY TFLDYYKHLS YNSIYHKSST 61 YGKCIAVDAF IKKINETYDK VKSKCNDIKN DLIATIKKLE HPYDINNKND DSYRYDISEE 121 IDDKSEETDD ETEEVEDSIQ DTDSNHTPSN KKKNDLMNRT FKKMMDEYNT KKKKLIKCIK 181 NHENDFNKIC MDMKNYGTNL FEQLSCYNNN FCNTNGIRYH YDEYIHKLIL SVKSKNLNKD 241 LSDMTNILQQ SELLLTNLNK KMGSYIYIDT IKFIHKEMKH IFNRIEYHTK IINDKTKIIQ 301 DKIKLNIWRT FQKDELLKRI LDMSNEYSLF ITSDHLRQML YNTFYSKEKH LNNIFHHLIY 361 VLQMKFNDVP IKMEYFQTYK KNKPLTQ SEQ ID NO: 68: PfRH5 amino acid sequence (7G8) excluding signal sequence and flexible N-terminal region (amino acids 1 to 139): (7G8 RH5ΔN) 1 KNVNFLQYHF KELSNYNIAN SIDILQEKEG HLDFVIIPHY TFLDYYKHLS YNSIYHKSST 61 YGKYIAVDAF IKKINETYDK VKSKCNDIKN DLIATIKKLE HPYDINNKND DSYRYDISEE 121 IDDKSEETDD ETEEVEDSIQ DTDSNHTPSN KKKNDLMNRT FKKMMDEYNT KKKKLIKCIK 181 NHENDFNKIC MDMKNYGTNL FEQLSCYNNN FCNTNGIRYH YDEYIHKLIL SVKSKNLNKD 241 LSDMTNILQQ SELLLTNLNK KMGSYIYIDT IKFIHKEMKH IFNRIEYHTK IINDKTKIIQ 301 DKIKLNIWRT FQKDELLKRI LDMSNEYSLF ITSDHLRQML YNTFYSKEKH LNNIFHHLIY 361 VLQMKFNDVP IKMEYFQTYK KNKPLTQ SEQ ID NO: 69: PfRH5 amino acid sequence (3D7) excluding signal sequence and flexible N-terminal region (amino acids 1 to 159) 1 SIDILQEKEG HLDFVIIPHY TFLDYYKHLS YNSIYHKSST YGKCIAVDAF IKKINETYDK 61 VKSKCNDIKN DLIATIKKLE HPYDINNKND DSYRYDISEE IDDKSEETDD ETEEVEDSIQ 121 DTDSNHTPSN KKKNDLMNRT FKKMMDEYNT KKKKLIKCIK NHENDFNKIC MDMKNYGTNL 181 FEQLSCYNNN FCNTNGIRYH YDEYIHKLIL SVKSKNLNKD LSDMTNILQQ SELLLTNLNK 241 KMGSYIYIDT IKFIHKEMKH IFNRIEYHTK IINDKTKIIQ DKIKLNIWRT FQKDELLKRI 301 LDMSNEYSLF ITSDHLRQML YNTFYSKEKH LNNIFHHLIY VLQMKFNDVP IKMEYFQTYK 361 KNKPLTQ SEQ ID NO: 70: PfRH5 amino acid sequence (7G8) excluding signal sequence and flexible N-terminal region (amino acids 1 to 159) 1 SIDILQEKEG HLDFVIIPHY TFLDYYKHLS YNSIYHKSST YGKYIAVDAF IKKINETYDK 61 VKSKCNDIKN DLIATIKKLE HPYDINNKND DSYRYDISEE IDDKSEETDD ETEEVEDSIQ 121 DTDSNHTPSN KKKNDLMNRT FKKMMDEYNT KKKKLIKCIK NHENDFNKIC MDMKNYGTNL 181 FEQLSCYNNN FCNTNGIRYH YDEYIHKLIL SVKSKNLNKD LSDMTNILQQ SELLLTNLNK 241 KMGSYIYIDT IKFIHKEMKH IFNRIEYHTK IINDKTKIIQ DKIKLNIWRT FQKDELLKRI 301 LDMSNEYSLF ITSDHLRQML YNTFYSKEKH LNNIFHHLIY VLQMKFNDVP IKMEYFQTYK 361 KNKPLTQ SEQ ID NO: 71: PfRH5 amino acid sequence (3D7) excluding signal sequence, flexible N-terminal (amino acids 1 to 139) and flexible loop (amino acids 248 to 296) regions (3D7 RH5ΔNL) 1 KNVNFLQYHF KELSNYNIAN SIDILQEKEG HLDFVIIPHY TFLDYYKHLS YNSIYHKSST 61 YGKCIAVDAF IKKINETYDK VKSKCNDIKN DLIATIKKLE HPYDINNKNR TFKKMMDEYN 121 TKKKKLIKCI KNHENDFNKI CMDMKNYGTN LFEQLSCYNN NFCNTNGIRY HYDEYIHKLI 181 LSVKSKNLNK DLSDMTNILQ QSELLLTNLN KKMGSYIYID TIKFIHKEMK HIFNRIEYHT 241 KIINDKTKII QDKIKLNIWR TFQKDELLKR ILDMSNEYSL FITSDHLRQM LYNTFYSKEK 301 HLNNIFHHLI YVLQMKFNDV PIKMEYFQTY KKNKPLTQ SEQ ID NO: 72: PfRH5 amino acid sequence (7G8) excluding signal sequence, flexible N-terminal (amino acids 1 to 139) and flexible loop (amino acids 248 to 296) regions: (7G8 RH5ΔNL) 1 KNVNFLQYHF KELSNYNIAN SIDILQEKEG HLDFVIIPHY TFLDYYKHLS YNSIYHKSST 61 YGKYIAVDAF IKKINETYDK VKSKCNDIKN DLIATIKKLE HPYDINNKNR TFKKMMDEYN 121 TKKKKLIKCI KNHENDFNKI CMDMKNYGTN LFEQLSCYNN NFCNTNGIRY HYDEYIHKLI 181 LSVKSKNLNK DLSDMTNILQ QSELLLTNLN KKMGSYIYID TIKFIHKEMK HIFNRIEYHT 241 KIINDKTKII QDKIKLNIWR TFQKDELLKR ILDMSNEYSL FITSDHLRQM LYNTFYSKEK 301 HLNNIFHHLI YVLQMKFNDV PIKMEYFQTY KKNKPLTQ SEQ ID NO: 73: PfRH5 amino acid sequence (3D7) excluding signal sequence, flexible N-terminal (amino acids 1 to 159) and flexible loop (amino acids 248 to 296) regions 1 SIDILQEKEG HLDFVIIPHY TFLDYYKHLS YNSIYHKSST YGKCIAVDAF IKKINETYDK 61 VKSKCNDIKN DLIATIKKLE HPYDINNKNR TFKKMMDEYN TKKKKLIKCI KNHENDFNKI 121 CMDMKNYGTN LFEQLSCYNN NFCNTNGIRY HYDEYIHKLI LSVKSKNLNK DLSDMTNILQ 181 QSELLLTNLN KKMGSYIYID TIKFIHKEMK HIFNRIEYHT KIINDKTKII QDKIKLNIWR 241 TFQKDELLKR ILDMSNEYSL FITSDHLRQM LYNTFYSKEK HLNNIFHHLI YVLQMKFNDV 301 PIKMEYFQTY KKNKPLTQ SEQ ID NO: 74: PfRH5 amino acid sequence (7G8) excluding signal sequence, flexible N-terminal (amino acids 1 to 159) and flexible loop (amino acids 248 to 296) regions 1 SIDILQEKEG HLDFVIIPHY TFLDYYKHLS YNSIYHKSST YGKYIAVDAF IKKINETYDK 61 VKSKCNDIKN DLIATIKKLE HPYDINNKNR TFKKMMDEYN TKKKKLIKCI KNHENDFNKI 121 CMDMKNYGTN LFEQLSCYNN NFCNTNGIRY HYDEYIHKLI LSVKSKNLNK DLSDMTNILQ 181 QSELLLTNLN KKMGSYIYID TIKFIHKEMK HIFNRIEYHT KIINDKTKII QDKIKLNIWR 241 TFQKDELLKR ILDMSNEYSL FITSDHLRQM LYNTFYSKEK HLNNIFHHLI YVLQMKFNDV 301 PIKMEYFQTY KKNKPLTQ SEQ ID NO: 75: RH5.1 ENAIKKTKNQENNLALLPIKSTEEEKDDIKNGKDIKKEIDNDKENIKTNNAKDHSTYIKSYLNTNVNDGLKYLFIPSHN SFIKKYSVFNQINDGMLLNEKNDVKNNEDYKNVDYKNVNFLQYHFKELSNYNIANSIDILQEKEGHLDFVIIPHYTFL DYYKHLSYNSIYHKSSTYGKCIAVDAFIKKINEAYDKVKSKCNDIKNDLIATIKKLEHPYDINNKNDDSYRYDISEEIDDK SEETDDETEEVEDSIQDTDSNHAPSNKKKNDLMNRAFKKMMDEYNTKKKKLIKCIKNHENDFNKICMDMKNYGT NLFEQLSCYNNNFCNTNGIRYHYDEYIHKLILSVKSKNLNKDLSDMTNILQQSELLLTNLNKKMGSYIYIDTIKFIHKE MKHIFNRIEYHTKIINDKTKIIQDKIKLNIWRTFQKDELLKRILDMSNEYSLFITSDHLRQMLYNTFYSKEKHLNNIFHH LIYVLQMKFNDVPIKMEYFQTYKKNKPLTQ SEQ ID NO: 76: Full length RH5.1, Bold = BiP Secretion Signal Peptide for Expression in Insect Cells, Underlined = C-Tag for affinity purification MKLCILLAVVAFVGLSLGENAIKKTKNQENNLALLPIKSTEEEKDDIKNGKDIKKEIDNDKENIKTNNAKDHSTYIKSY LNTNVNDGLKYLFIPSHNSFIKKYSVFNQINDGMLLNEKNDVKNNEDYKNVDYKNVNFLQYHFKELSNYNIANSIDI LQEKEGHLDFVIIPHYTFLDYYKHLSYNSIYHKSSTYGKCIAVDAFIKKINEAYDKVKSKCNDIKNDLIATIKKLEHPYDIN NKNDDSYRYDISEEIDDKSEETDDETEEVEDSIQDTDSNHAPSNKKKNDLMNRAFKKMMDEYNTKKKKLIKCIKNH ENDFNKICMDMKNYGTNLFEQLSCYNNNFCNTNGIRYHYDEYIHKLILSVKSKNLNKDLSDMTNILQQSELLLTNLN KKMGSYIYIDTIKFIHKEMKHIFNRIEYHTKIINDKTKIIQDKIKLNIWRTFQKDELLKRILDMSNEYSLFITSDHLRQML YNTFYSKEKHLNNIFHHLIYVLQMKFNDVPIKMEYFQTYKKNKPLTQEPEA SEQ ID NO: 77: PfRH5 (PfRH5FL) sequence of amino acids E26-Q526 of the 3D7 clone P. falciparum reference sequence, with mutations to delete N-linked glycosylation (N38Q and N214Q) and with an additional C-terminal AviTag™ and Strep-II® tag in tandem ENAIKKTKNQ ENQLTLLPIK STEEEKDDIK NGKDIKKEID NDKENIKTNN AKDHSTYIKS 60 YLNTNVNDGL KYLFIPSHNS FIKKYSVFNQ INDGMLLNEK NDVKNNEDYK NVDYKNVNFL 120 QYHFKELSNY NIANSIDILQ EKEGHLDFVI IPHYTFLDYY KHLSYNSIYH KSSTYGKCIA 180 VDAFIKKIQE TYDKVKSKCN DIKNDLIATI KKLEHPYDIN NKNDDSYRYD ISEEIDDKSE 240 ETDDETEEVE DSIQDTDSNH TPSNKKKNDL MNRTFKKMMD EYNTKKKKLI KCIKNHENDF 300 NKICMDMKNY GTNLFEQLSC YNNNFCNTNG IRYHYDEYIH KLILSVKSKN LNKDLSDMTN 360 ILQQSELLLT NLNKKMGSYI YIDTIKFIHK EMKHIFNRIE YHTKIINDKT KIIQDKIKLN 420 IWRTFQKDEL LKRILDMSNE YSLFITSDHL RQMLYNTFYS KEKHLNNIFH HLIYVLQMKF 480 NDVPIKMEYF QTYKKNKPLT QGSASGLNDI FEAQKIEWHE WSHPQFEK 528 SEQ ID NO: 78: PfRH5ΔNL KNVNFLQYHF KELSNYNIAN SIDILQEKEG HLDFVIIPHY TFLDYYKHLS YNSIYHKSST 60 YGKCIAVDAF IKKINEAYDK VKSKCNDIKN DLIATIKKLE HPYDINNKNR AFKKMMDEYN 120 TKKKKLIKCI KNHENDFNKI CMDMKNYGTN LFEQLSCYNN NFCNTNGIRY HYDEYIHKLI 180 LSVKSKNLNK DLSDMTNILQ QSELLLTNLN KKMGSYIYID TIKFIHKEMK HIFNRIEYHT 240 KIINDKTKII QDKIKLNIWR TFQKDELLKR ILDMSNEYSL FITSDHLRQM LYNTFYSKEK 300 HLNNIFHHLI YVLQMKFNDV PIKMEYFQTY KKNKPLTQEP EA 342 SEQ ID NO: 79: R5.001 heavy chain variable region QVQLVQSGAEMKKPGASVKVSCKASGYTFTSYGISWVRQAPGQGLEWMGWISAYNGNTNYARKLQGRVTMTT DTSTSTAYMELRSLRSDDTAVYYCARDMATYGDPNYFDPWGQGTLVTVSS SEQ ID NO: 80: R5.001 light chain variable region DIVMTQSPSSLSASVGDRVTITCRASQGISRWLAWYQQKPEKAPKSLIYAASSLQSGVPSRFSGSGSGTDFTLTISSLQ PEDFATYYCQQYNTYPLTFGGGTKVEIR SEQ ID NO: 81: Exemplary residues 193-220 of the (disconƟnuous) epitope for the non-neutralising anƟbodies of the invenƟon IYHKSSTYGKCIAVDAFIKKINETYDKV SEQ ID NO: 82: Exemplary residues 327-342 of the (disconƟnuous) epitope for the non-neutralising anƟbodies of the invenƟon KICMDMKNYGTNLFEQ SEQ ID NO: 83: Exemplary residues 193-220 of the (disconƟnuous) epitope for the non-neutralising anƟbodies of the invenƟon IXXXXXTXGKCIAVDAFXKKIXETXXKV SEQ ID NO: 84: Exemplary residues 327-342 of the (disconƟnuous) epitope for the non-neutralising anƟbodies of the invenƟon KIXXDXXNYXXNLXXQ SEQ ID NO: 85: Exemplary residues 202-219 of the (disconƟnuous) epitope for the non-neutralising anƟbodies of the invenƟon KCIAVDAFIKKINETYDK SEQ ID NO: 86: Exemplary residues 202-219 of the (disconƟnuous) epitope for the non-neutralising anƟbodies of the invenƟon KXIAXXAFXXKIXXTXXK SEQ ID NO: 87: Exemplary residues 326-342 of the (disconƟnuous) epitope for the non-neutralising anƟbodies of the invenƟon NKICMDMKNYGTNLFEQ SEQ ID NO: 88: Exemplary residues 326-342 of the (disconƟnuous) epitope for the non-neutralising anƟbodies of the invenƟon NKIXMDXXNYXXNLXXQ SEQ ID NO: 89: Exemplary residues 323-342 of the (disconƟnuous) epitope for the non-neutralising anƟbodies of the invenƟon NDFNKICMDMKNYGTNLFEQ SEQ ID NO: 90: Exemplary residues 323-342 of the (disconƟnuous) epitope for the non-neutralising anƟbodies of the invenƟon NDFNKIXMDXKNYXTNLXEQ SEQ ID NO: 91: Amino acid sequence of gene segment HV3-7_GL EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVANIKQDGSEKYYVDSVKGRFTISRDNA KNSLYLQMNSLRAEDTAVYYCAR SEQ ID NO: 92: Amino acid sequence of gene segment LV1-36_GL QSVLTQPPSVSEAPRQRVTISCSGSSSNIGNNAVNWYQQLPGKAPKLLIYYDDLLPSGVSDRFSGSKSGTSASLA ISGLQSEDEADYYCAAWDDSLNG EXAMPLES The invenƟon is now described with reference to the Examples below. These are not limiƟng on the scope of the invenƟon, and a person skilled in the art would be appreciate that suitable equivalents could be used within the scope of the present invenƟon. Thus, the Examples may be considered component parts of the invenƟon, and the individual aspects described therein may be considered as disclosed independently, or in any combinaƟon. Materials and methods Human Blood Sample CollecƟon All mAbs were obtained from samples of adult volunteers immunized with the RH5.1 / AS01B vaccine as part of the VAC063 clinical trial. VAC063 was an open-label, mulƟ-center, dose-finding Phase I / IIa trial, including a controlled human malaria infecƟon (CHMI) component, to assess the safety, immunogenicity, and efficacy of the candidate P. falciparum blood-stage malaria vaccine RH5.1 / AS01B. Volunteers were healthy, malaria-naïve UK adults ranging from 18–45 years of age. The study was conducted in the UK at the Centre for Clinical Vaccinology and Tropical Medicine, University of Oxford, Oxford, Guys and St Thomas' NIHR CRF, London and the NIHR Wellcome Trust Clinical Research Facility in Southampton. The study received ethical approval from the UK NHS Research Ethics Service (Oxfordshire Research Ethics CommiƩee A, Ref 16 / SC / 0345), and was approved by the UK Medicines and Healthcare products Regulatory Agency (Ref 21584 / 0362 / 001-0011). Volunteers signed wriƩen consent forms and consent was verified before each vaccinaƟon. The trial was registered on ClinicalTrials.gov (NCT02927145) and was conducted according to the principles of the current revision of the DeclaraƟon of Helsinki 2008 and in full conformity with the ICH guidelines for Good Clinical PracƟce (GCP). DonaƟons of human RBC from healthy adult volunteers for use in assays received ethical approval from the UK NHS Research Ethics Service (London – City & East Research Ethics CommiƩee, Ref 18 / LO / 0415). The RH5.1 vaccine was based on the full-length PfRH5 anƟgen (amino acids E26 - Q526) with 3D7 clone P. falciparum sequence, as reported in detail elsewhere. In brief, the vaccine was manufactured as a secreted soluble product from a stable Drosophila melanogaster Schneider 2 (S2) cell line and affinity purified via a C-terminal four amino acid (E-P-E-A) “C-tag.” All four putaƟve N- linked glycosylaƟon sequons (N-X-S / T) were mutated Thr to Ala. Volunteer samples from VAC063 Groups 1, 2, 3, 5 and 7 were used in this study. ParƟcipants in Groups 1, 2 and 5 received three “monthly” vaccinaƟons of RH5.1 / AS01B at days 0, 28 and 56, with a dose escalaƟon of RH5.1 from 2 μg (Group 1), to 10 μg (Groups 2 and 5). Volunteers in Group 3 received two 50 μg doses of RH5.1 followed by a final dose of 10 μg RH5.1 given at day 182 (a “delayed fracƟonal dosing” (DFx) regimen). All vaccines were formulated in in 0.5 mL AS01B adjuvant (GSK) regardless of RH5.1 protein dose. Group 5 underwent blood-stage CHMI with 3D7 clone P. falciparum 14 days aŌer their third vaccinaƟon. Group 7 was composed of a subset of Group 5 vaccinees who went on to receive a final, delayed and fourth booster vaccinaƟon (D4thB) with 10 μg RH5.1 / AS01B approximately four months aŌer their third vaccinaƟon followed by a second round of CHMI. Peripheral blood mononuclear cell (PBMC) samples were isolated and cryopreserved at approximately 2-4 weeks post-final vaccinaƟon for each group. Human blood samples were collected into lithium heparin-treated vacutainer blood collecƟon systems (Becton Dickinson). PBMC were isolated and used within 6 h in fresh assays, otherwise excess cells were frozen in fetal calf serum (FCS) containing 10% dimethyl sulfoxide and stored in liquid nitrogen. Plasma samples were stored at −80 °C. For serum preparaƟon, untreated blood samples were stored at room temperature (RT) and then the cloƩed blood was centrifuged for 5 min at 1800 rpm. Serum was stored at −80°C. Experimental Animal Models The study using liver-humanized mice was carried out at the Oregon Health and Sciences University (OHSU) which is accredited by the AssociaƟon for Assessment and AccreditaƟon of Laboratory Animal Care InternaƟonal (AAALACi) and is a Category I facility with an approved Assurance (#A3304-01) on file with the Office for Laboratory Animal Welfare (OLAW), NIH, USA. The protocol was approved by the OHSU InsƟtuƟonal Animal Care and Use CommiƩee (IACUC) under protocol IP00002077. Fah- / - Rag2- / - Il2rγ- / - (FRG) huHep mice on the NOD background were purchased from Yecuris, Inc. (Beaverton, OR, USA). Cell Lines Expi293F HEK cells were cultured in suspension in Expi293 expression medium (Thermo Fisher ScienƟfic) at 37°C, 8% CO2, on an orbital shaker set at 125 RPM. Drosophila S2 cells were cultured in suspension in EX-CELL 420 medium (Sigma-Aldrich) supplemented with 100 U / mL penicillin, 0.1 mg / mL streptomycin and 10% foetal bovine serum (FBS) at 25 °C. Stable S2 cell lines expressing PfRH5 proteins were generated using the ExpreS2 plaƞorm (ExpreS2ion Biotechnologies) as previously described. IsolaƟon of PfRH5-specific B cells PfRH5-specific B cells were single cell sorted from the majority of cryopreserved PBMC samples as previously described but with minor modificaƟon as follows. In brief, samples were thawed into R10 media (RPMI [R0883, MilliporeSigma] supplemented with 10% heat-inacƟvated FCS [60923, Biosera], 100 U / mL penicillin / 0.1 mg / mL streptomycin [P0781, MilliporeSigma], 2 mM L-glutamine [G7513, Millipore Sigma]) and were then washed and rested in R10 for 1 h. B cells were enriched (Human Pan-B cell Enrichment Kit [19554, StemCell Technologies]) and then stained with viability dye FVS780 (565388, BD Biosciences). Next, B cells were stained with anƟ-human CD19-BV786 (Clone: SJ25C1, 563325, BD Biosciences) and anƟ-human IgG-BB515 (Clone: G18-145, 564581, BD Biosciences), as well as two fluorophore-conjugated PfRH5 probes. To prepare the probes, monobioƟnylated PfRH5 was produced by transient co-transfecƟon of HEK293F cells with a plasmid encoding BirA bioƟn ligase and a plasmid encoding a modified PfRH5. The PfRH5 plasmid was based on ‘RH5-bio’ (a giŌ from Gavin Wright; University of York, York, United Kingdom; Addgene plasmid #47780). RH5-bio was modified prior to transfecƟon to incorporate a C-terminal C-tag for subsequent protein purificaƟon, as well as a 15 amino acid deleƟon to remove the disordered C-terminus of PfRH5 and a 115 amino acid deleƟon from the linear N-terminus to produce a protein known as “RH5ΔNC.” Probes were freshly prepared for each experiment by incubaƟon of mono-bioƟnylated RH5ΔNC with streptavidin-phycoerythrin (PE) (S866, Invitrogen) or streptavidin-allophycocyanin (APC) (405207, eBioscience) at an approximately 4:1 molar raƟo to facilitate tetramer generaƟon and subsequent centrifugaƟon to remove aggregates (13,000–14,000 rpm [max microcentrifuge speed] at RT for 10 min). Following surface staining, cells were washed and kept on ice unƟl acquisiƟon on the MoFlo (Dako cytomaƟon). RH5ΔNC-specific B cells were idenƟfied as live CD19+ IgG+ RH5ΔNC-APC+ RH5ΔNC- PE+ cells and single cell sorted into 96-well plates containing 10μL / well lysis buffer (10mM Tris [T3038, Sigma], 1 unit / mL RNasin Ribonuclease Inhibitor [N2515, Promega]) and frozen at -80 °C. A subset of eight mAbs (R5.242, R5.243, R5.244, R5.246, R5.247, R5.248, R5.249 and R5.250) were derived from a cell sort that included an addiƟonal cell hashing step (TotalSeq- C0251 / C0252 / C0253 / C0254 / C0255 anƟ-human Hashtag 1 / 2 / 3 / 4 / 5 anƟbodies, cat # 394661 / 394663 / 394665 / 394667 / 394669, Biolegend) prior to B cell enrichment and staining. These hashed samples were then either single-cell sorted into 96-well plates (as above) or pooled for B cell receptor (BCR) sequencing analysis using the 10X chromium plaƞorm; performed at the Oxford Genomics Center, University of Oxford, UK. Monoclonal AnƟbody Cloning Reverse transcripƟon and nested PCR of anƟbody heavy (VH) and light (VL) chains was carried out as previously described and using previously reported primers. PCR products were purified using a PCR purificaƟon kit (Qiagen, 28006) and then cloned into the AbVec expression plasmids to produce recombinant human IgG1 mAbs (a giŌ from Patrick C. Wilson, University of Chicago, USA). In brief, plasmids and PCR products were 5′ digested using BshTI and 3′digested using SalI (AbVec-HCIgG1), XhoI (AbVec-LLC) and Pfl23II (AbVec-KLC) before ligaƟon using QuickLigase (NEB). LigaƟon products were then used to transform MulƟShot™ StripWell TOP10 chemically competent Escherichia coli (Thermo Fisher ScienƟfic) following the manufacturer’s instrucƟons. Transformed cells were plated on LB agar 8-well Petri plates (Teknova) containing 100 μg / mL carbenicillin and grown at 37 °C overnight in a staƟc incubator. Colonies were picked and sent to Source BioScience for sequencing, and those with producƟve anƟbody VH and VL sequences (analysed with Geneious® soŌware) were inoculated and plasmids extracted using a QIAgen MINIprep kit. Sequence analysis was carried out using Geneious Prime®. Germline idenƟty and gene usage parameters were determined using IMGT / V-QUEST. Heavy chain CDR3 (CDRH3) lengths were idenƟfied using IMGT numbering. SomaƟc hypermutaƟon (SHM) % was calculated from the outpuƩed idenƟty % for each V, D and J region from IMGT, by subtracƟng the value from 100%. To clone R5.034LS, the R5.034 IgG1 heavy chain constant region was replaced with a gene string encoding the same human IgG1 constant heavy region containing the two LS mutaƟons (M451L / N457S) via the SalI and HindIII restricƟon sites. Recombinant R5.034 was then produced as previously described. Expression and PurificaƟon of AnƟbodies TransfecƟons of HEK293F cells using a 1:1 raƟo of HC and light chain (LC) plasmids were set up in 10 mL culture volumes in 50 mL vented cap reacƟon tubes using Expifectamine™ transfecƟon kit (Thermo Fisher ScienƟfic) as per the manufacturer’s instrucƟons. IgG purificaƟon was carried out using Econo-PAC® chromatography columns (Bio-Rad) and Protein A Sepharose (Sigma-Aldrich), and purified mAbs were buffer-exchanged into phosphate buffered saline (PBS). Expression and PurificaƟon of Proteins Unless stated otherwise, all PfRH5 and PfCyRPA soluble proteins and reagents were designed based on the 3D7 clone P. falciparum reference sequence with all the N-glycan sequons (N-X-S / T) mutated from a serine or threonine to alanine. RH5.1 and RH5ΔNL The design, producƟon, and purificaƟon of RH5.1 and RH5ΔNL have previously been described. In brief, stable Drosophila S2 polyclonal cell lines expressing full-length RH5.1 (residues E26- Q526) or RH5ΔNL (residues K140-K247 and N297-Q526 of PfRH5 with 3D7 or 7G8 P. falciparum sequence, differing only by the C203Y polymorphism) were cultured in EX-CELL 420 media and expanded in shake flasks to the desired scale. Cell supernatant was harvested and loaded onto a 10 mL column packed with CaptureSelect affinity C-Tag XL resin, washed in 10 column volumes of TBS pH 7.4 and eluted in 2M MgCl2. FracƟons were then pooled, concentrated using a 10 kDa Amicon ultra centrifugal filter and run on an HiLoad 16 / 600 Superdex 200 pg size exclusion chromatography (SEC) column into TBS pH 7.4 (20 mM Tris-HCl, 150 mM NaCl). RH5ΔNC-BioƟn The producƟon of the RH5ΔNC-BioƟn has been described. Mono-bioƟnylated RH5ΔNC-BioƟn, previously referred to as ‘RH5-Bio’, was generated through co-transfecƟon of Expi293 cells with a plasmid encoding RH5ΔNC-BioƟn and another plasmid encoding BirA bioƟn ligase. RH5ΔNC-BioƟn was then purified from the supernatant by C-tag affinity chromatography follow by SEC into TBS pH 7.4 (20 mM Tris-HCl, 150 mM NaCl). PfCyRPA Full-length PfCyRPA (residues 29-362) was expressed in Expi293 cells and purified through C- tag affinity chromatography follow by SEC into TBS pH 7.4 as previously described. Basigin NaƟve human basigin sequence, encoding residues M1-L206, followed by rat CD4 domains 3 and 4 and a C-terminal hexa-hisƟdine tag was expressed through transient transfecƟon of Expi293 cells. Protein was then purified from the supernatant by immobilized metal affinity chromatography (IMAC) using a Ni2+ resin followed by SEC into TBS pH 7.4 (20 mM Tris-HCl, 150 mM NaCl) as previously described. ELISA For assessment of anƟbody binding by ELISA, Nunc Maxisorp plates were coated overnight (>16 h) with either RH5.1, heat-denatured RH5.1 (held at 90 °C for 10 min), or RH5ΔNL at 2 μg / mL. Plates were washed in wash buffer (PBS with 0.05% Tween 20 [PBST]) and blocked with 100 μL / well of Blocker00E4 Casein (Thermo Fisher ScienƟfic) for 1 h. Plates were washed and anƟbodies at 10 μg / mL diluted in casein were added. Following a 2 h incubaƟon, plates were washed and a 1:1000 diluƟon of goat anƟ-human IgG (γ-chain specific) alkaline phosphate conjugate anƟbody (A3187, Thermo Fisher) was added and incubated for 1 h. Plates were washed in washing buffer and 100 μL development buffer (p-nitrophenyl phosphate substrate diluted in diethanolamine buffer) was added per well and developed according to internal controls. All mAbs were tested in duplicate against each coaƟng anƟgen. Unless otherwise stated, 50 μL was added per well and all steps were carried out at RT. A given mAb was tested against all anƟgens within the same plate. For the pepƟde array ELISAs, steps were idenƟcal to the above except streptavidin-coated plates (Pierce) were used and were coated with an array of 62 x 20-mer PfRH5 pepƟdes overlapping by 12 amino acids as previously reported. AnƟbody KineƟcs High-throughput SPR binding experiments in Figures 2 and S2 were performed on a Carterra LSA instrument equipped with a 2D planar carboxymethyldextran surface (CMDP) chip type (Carterra) using a 384-ligand array format. The CMDP chip was first condiƟoned with 60 s injecƟons of 50 mM NaOH, 1 M NaCl and 10 mM glycine (pH 2.0) before acƟvaƟon with a freshly prepared 1:1:1 mixture of 100 mM MES (pH 5.5), 100 mM sulfo-N-hydroxysuccinimide, and 400 mM 1-ethyl-3-(3- dimethylaminopropyl) carbodiimide hydrochloride. A coupled lawn of goat anƟ-human IgG Fc (hFc; 50 μg / mL in 10 mM sodium acetate, pH 4.5) (Jackson ImmunoResearch) was then prepared before quenching with 0.5 M ethanolamine (pH 8.5) and washing with 10 mM glycine (pH 2.0). mAbs prepared at 100 ng / mL in Tris-buffered saline with 0.01% Tween-20 (TBST) were then captured onto the surface in a 384-array format via a mulƟ-channel device, capturing 96 ligands at a Ɵme. For binding kineƟcs and affinity measurements, a six-point threefold diluƟon series of RH5.1 protein (33.3 nM – 46.7 pM) in TBST was sequenƟally injected onto the chip from lowest to highest concentraƟon. For each concentraƟon, the anƟgen was injected for 5 min (associaƟon phase), followed by TBST injecƟon for 15 min (dissociaƟon phase). Two regeneraƟon cycles of 30 s were performed between each diluƟon series by injecƟng 10 mM glycine (pH 2.0) on the chip surface. The SPR results were exported to KineƟcs SoŌware (Carterra) and analyzed as nonregeneraƟve kineƟcs data to calculate associaƟon rate constant (Kon), dissociaƟon rate constant (Koff) and equilibrium dissociaƟon constant (KD) values via fiƫng to the Langmuir 1:1 model. Prior to fiƫng, the data were referenced to the anƟ-hFc surface then double referenced using the final stabilizing blank injecƟon. Epitope Binning by Surface Plasmon Resonance High-throughput epitope binning experiments were performed in a classical sandwich assay format using the Carterra LSA and an HC30M chip. The chip was condiƟoned as described above before anƟbodies prepared at 10 μg / mL in 10 mM sodium acetate (pH 4.5) with 0.05% Tween were coupled to the surface: the chip surface was first acƟvated with a freshly prepared 1:1:1 acƟvaƟon mix of 100 mM MES (pH 5.5), 100 mM sulfo-N-hydroxysuccinimide, and 400 mM 1-ethyl-3-(3- dimethylaminopropyl) carbodiimide hydrochloride, and anƟbodies were injected and immobilized onto the chip surface by direct coupling. The chip surface was then quenched with 1 M ethanolamine (pH 8.5), followed by washing with 10 mM glycine (pH 2.0). SequenƟal injecƟons of 50 nM RH5.1 protein (5 min) followed immediately by the 10 μg / mL sandwiching anƟbody (5 min), both diluted in HEPES-buffered saline Tween-EDTA (HBSTE) with 0.5 mg / mL bovine serum albumin (BSA), were added to the coupled array and the surfaces regenerated with 10 mM glycine (pH 2.0) using two 30 s regeneraƟon cycles. Data were analysed using the Carterra Epitope soŌware. The epitope binning experiment for mouse mAbs QA1 and 9AD4 was performed as above but using a HC200M chip and TBST as the running buffer and diluent. DeterminaƟon of Protein Blockade by Bio-layer Interferometry (BLI) All BLI was carried out on an OctetRED384 (ForteBio) using anƟ-human Fc-capture sensors (Sartorius, 18-5060) to immobilize anƟ-PfRH5 mAbs. Assays were carried out in a 384-well format in black plates (Greiner). For assaying the ability of each mAb to block RH5.1 binding to basigin and PfCyRPA, the experiment followed a sequenƟal assay: mAb immobilizaƟon (15 μg / mL, 300 s), RH5.1 binding (1 μM, 300 s), protein ligand binding (3 μM PfCyRPA or basigin, 300 s) with a 30 s dissociaƟon phase in TBST between each step. Finally, a 120 s dissociaƟon step was carried out in TBST before a 10 s pulsed regeneraƟon of biosensors with 10 mM glycine (pH 2). Within each plate, PfCyRPA blocking was first assessed for a set of mAbs immediately followed by regeneraƟon and then basigin blocking acƟvity assessed for the same set of mAbs. As internal or “senƟnel mAb” controls, each plate included a PfCyRPA-blocking mAb (R5.015), a basigin blocking mAb (R5.004) and a non-blocking mAb (R5.011). In addiƟon, in each assay, a reference baseline set of biosensors was run in parallel using the same format but replacing the protein ligand binding step with a TBST step. Data were analysed in the Octet Data Analysis HT soŌware (Fortebio). The reference biosensors were assigned as references in the soŌware and subtracted from the test biosensors. Steps were aligned to the start of each associaƟon step and the associaƟon and dissociaƟon was fiƩed. Response value report points were set at 20 s (start of associaƟon) and 290 s (end of associaƟon) and exported. For the majority of mAbs, the 290 s report point was used. For a subset of mAbs with very fast dissociaƟon, the 20 s Ɵmepoint was used (because report points at 290 s could be erroneously reported as blocking due to dissociaƟon of the underlying RH5.1 surface from the captured mAb). For the RH5.1 report points, the data were unreferenced. For each mAb, the basigin and PfCyRPA responses were normalized by dividing by the RH5.1 response. Any mAb with a normalized response value of <0.04 nm for basigin or PfCyRPA was categorized as “blocking” for that protein ligand. Data were discarded if R5.015 had a response >0.04 nm for PfCyRPA; R5.004 had a response >0.04 nm for basigin; or if R5.011 had a response <0.04 nm for either protein ligand. Assay of Growth InhibiƟon AcƟvity (GIA) Single concentraƟon in vitro GIA assays were carried as previously described according to the methods of the GIA InternaƟonal Reference Centre at NIAID / NIH, USA. All assays used 3D7 clone P. falciparum parasites cultured in human RBC from in-house volunteer donaƟons or supplied by the UK NHS Blood and Transplant service for non-clinical issue. Briefly, mAbs were buffer exchanged into incomplete parasite growth media (ICM = RPMI, 2 mM L-glutamine, 0.05 g / L hypoxanthine, 5.94 g / L HEPES) before performing the GIA assay and allowing parasites to go through a single cycle of growth. To ensure consistency between experiments, in each case the acƟvity of a negaƟve control human mAb, EBL040 which binds to the Ebola virus glycoprotein, and three anƟ-PfRH5 mAbs with well- characterized GIA (2AC7, QA5, and 9AD4; or 2AC7, R5.016, and R5.034) were run alongside the test mAbs and were all tested in triplicates. mAbs showing >30% GIA were subsequently tested in an eight step, five-fold diluƟon series with a final assay start concentraƟon of 2 mg / mL to determine interpolated EC values. The resultant data were transformed according to x=log(x) and the transformed data were fiƩed by four-parameter non-linear regression. GIA values were interpolated from the resultant curve. If a mAb did not reach a sufficiently high GIA (i.e. the mAb did not reach 30%, 50% or 80% at any test concentraƟon), then it was assigned a “negaƟve” value of 10,000 μg / mL for that parƟcular EC readout. For screening of intra-PfRH5 mAb interacƟons, single concentraƟon assays were carried out as above, with neutralizing anƟbodies added at a concentraƟon equivalent to their interpolated EC50 value and non-neutralizing anƟbodies held at 0.3 mg / mL. For tesƟng of non-neutralizing anƟbodies in combinaƟon, both mAbs in a pair were held at 0.2 mg / mL. For diluƟon curves, Ɵtrated mAbs were set up in a 7-step, five-fold diluƟon series starƟng at 0.5 mg / mL per mAb. To each Ɵtrated mAb diluƟon, a held concentraƟon of a second mAb (or a premixed combinaƟon of two mAbs) was added at a final concentraƟon of 0.2 mg / mL per held mAb. For each curve, a well containing the second mAb (or premixed combinaƟon) at the test concentraƟon was set up alone within the same assay plate. Curve fiƫng and data processing was carried out as above. For mixed ƟtraƟon curves, two or more mAbs were premixed and set up in an 8-step, five-fold diluƟon series starƟng at 0.5 mg / mL per test mAb. Curve fiƫng and data processing was carried out as above. For synergy curves with polyclonal anƟbody, total IgG (purified from the serum of VAC063 vaccinees13) was set up as above at a starƟng concentraƟon of 14 mg / mL total IgG in a 7-step 2-fold diluƟon curve. For analysis of synergisƟc or antagonisƟc interacƟons, the Bliss addiƟvity was determined based on the measured acƟvity from each anƟbody alone (1 and 2) using the following formula: GIAGIA^ GIAଶ^ାଶ= [1− (1 − 100) × (1 − 100)] × 100 PurificaƟon of IgG For the polyclonal anƟbody (pAb) pool, a pool of human serum from the VAC063 clinical trial was filtered through a 0.22 μM syringe filter (Milipore) and diluted 1:1 in PBS. Total IgG was then purified using a HiTrap Protein G column (CyƟva) on an ÄKTA Pure chromatography system (CyƟva), and the eluted total IgG was buffer exchanged into ICM using a centrifugal concentrator with a 30K MWCO (CyƟva). Total IgG concentraƟon was determined by reading absorbance at 280 nm on a Thermo ScienƟfic™ NanoDrop™ OneC Spectrophotometer. IgG was then depleted for anƟ-RBC anƟbodies by the addiƟon of 1 μg packed 100% hematocrit RBC per 1 μg IgG and incubated at RT with agitaƟon for 1 h. RBC were then pelleted by centrifugaƟon at 1,000 xg for 5 min and the supernatant removed. AnƟ-RH5.1 anƟbody Ɵters or concentraƟons were determined by standardized quanƟtaƟve ELISA methodology as previously reported. AnƟbody Sequence AnnotaƟon All annotaƟon of anƟbody heavy and light chain gene sequences was performed using IMGT V-Quest program version 3.5.31 using default parameters. The IGH locus was selected for heavy chain sequences, IGL for λ light chains and IGK for κ light chains. F+ORF+ in-frame P was used as the IMGT / V- QUEST reference directory set and the opƟon to search for inserƟons and deleƟons was selected. Design of Public Clonotype Germline Revertant mAbs SyntheƟc anƟbodies were designed based on the IGHV3-7 / IGLV1-36 gene combinaƟon. For the germline heavy chains (“HC GL”), amino acids E1 to R98 of the V-region of each public clonotype mAb (R5.034, R5.102, R5.237 and R5.270) were replaced with amino acids E1 to R98 of the germline IGHV3-7∗01 F gene (IMGT accession number: M99649) V-region obtained from IMGT. The sequence for each mAb from R98 was unchanged from the wildtype (WT) mAb, resulƟng in four germline IGHV3- 7 heavy chains, each biased with the CDRH3 J- and D- regions of the respecƟve public clonotype mAb. For the germline IGLV1-36 light chain (“LC GL”), amino acids Q1 to G98 of the germline IGLV1- 36∗01 F gene (IMGT accession number Z73653) V-region were concatenated with amino acids VVFGGGTKLTVL of the germline IGLJ2∗01 F gene (IMGT accension number M15641). Note that R5.034, R5.102 and R5.270 were equally likely to use the IGLJ2∗01 F or IGLJ3∗01 F (IMGT accession number M15642) gene segments, only R5.237 had a greater idenƟty to the IGLJ3∗02 (IMGT accession number D87023) gene segment. SyntheƟc genes were cloned into AbVec expression vectors as described above. For the producƟon of heavy chain revertant anƟbodies (HC GL), HEK293F cells were transfected with expression plasmids containing one of the four germline IGHV3-7 heavy chains, and the cognate WT light chain of the respecƟve public clonotype mAb. For the producƟon of light chain revertant anƟbodies (LC GL), cells were transfected with expression plasmids containing one of the four WT public clonotype mAb heavy chains and their respecƟve germline IGLV1-36 light chain. For the producƟon of full revertants (“Full GL”), cells were transfected with expression plasmids containing one of the four germline IGHV3-7 heavy chains and the respecƟve germline IGLV1-36 light chain. To generate the public clonotype CDRH3 knockout anƟbodies (“CDRH3_KO”), the 9 amino acids from posiƟons 99 to 107 in the CDRH3 of each anƟbody (IMGT numbering) were replaced with a ‘randomized’ sequence of amino acids with a matched length – HQSGKLVNMN. No amino acid in this sequence was conserved with respect to the equivalent posiƟon in any of the public clonotype CDRH3 sequences. The ‘randomized’ region was chosen to test the effects of altering amino acids derived from somaƟc hypermutaƟon of rearrangement, whilst preserving the largely conserved and germline templated sequences at the N- (posiƟons 97-98) and C- (posiƟons 108-109) termini of the 13 amino acid CDRH3. CDRH3 knockout heavy chains were cloned into expression vectors as described above. Cells were transfected with expression plasmids containing the respecƟve CDRH3 knockout heavy chain for each public clonotype anƟbody and its cognate WT light chain. Fab Cloning and Expression To express recombinant Fabs, heavy chain plasmids were generated using primers to amplify the heavy chain VH and CH1 domain only (5’ – GAG GAT GGT CAT GTA TCA TC and 5’ – CGC AAG CTT CTA AGT TTT GTC ACA AGA TTT GGG C) and then used to transfect Expi293F cells in combinaƟon with the corresponding light chain plasmids. Fab-containing supernatants were purified by affinity chromatography with either a HiTrap LambdaFabSelect column (17548211, CyƟva) or a HiTrap Protein G column (17040501, CyƟva) on an ÄKTA Pure chromatography system as per manufacturer’s instrucƟons. ProducƟon of RH5ΔNL:Fab Complexes for X-ray Crystallography Fabs and RH5ΔNL protein (7G8 sequence with Y203) were produced as described above, and buffer exchanged into HEPES-buffered saline (HBS, 25 mM HEPES, 150 mM NaCl, pH 7.5) using a 10K MWCO centrifugal concentrator device (CyƟva). RH5ΔNL was subjected to limited proteolysis at a concentraƟon of 1-2 mg / mL, with the addiƟon of 1 μL GluC protease (P8100S, NEB) at 1 mg / mL per mg of RH5ΔNL (1:1000 wt / wt). Protein was incubated at RT for 4-16 h. Fabs were then added at a 5% molar excess. The complex was incubated for 1 h at RT. The complex was then subjected to surface lysine methylaƟon by the addiƟon of 20 μL per mL of complex of 1 M dimethylamine borane complex (ABC) (Santa Cruz Biotechnology, sc-252506) and 40 μL per mL of complex of 1 M formaldehyde prepared from 37% stock (Thermo Fisher, 10630813). The complex was incubated for 1 h at RT, followed by a further addiƟon of 20 μL ABC and 20 μL formaldehyde per mL of complex. AŌer a further 1 h incubaƟon, 20 μL ABC per mL of complex was added and the soluƟon was incubated at 4 °C overnight. Aggregates were removed by spinning the sample in a centrifugal filter device (UFC40GV00, Milipore) at 4000 xg for 10 min. The flow-through was concentrated to <2 mL if necessary and run onto a Superdex 16 / 600200 pg SEC column (CyƟva) that had been pre-equilibrated in Tris-buffered saline (25 mM Trizma, 150 mM NaCl, pH 7.4). Complex containing fracƟons were pooled and concentrated to 8-12 mg / mL using a centrifrugal concentrator with a 10K MWCO (CyƟva) for crystal screening. Structure DeterminaƟon by X-ray Crystallography All crystallizaƟon was conducted using vapour diffusion in MRC 3 Lens siƫng drop crystallizaƟon plates (SwisSci, High Wycombe, UK) and 150 nL drops (raƟo 100 nL protein soluƟon (8 mg / μL:50 nL screen condiƟon) dispensed using a Mosquito nano-pipeƫng robot (STP Labtech, Melbourn, UK). CrystallizaƟon plates were incubated at 20 °C with crystals appearing between 4 and 28 days. The crystals were mounted with LithoLoops (Molecular Dimension, Rotherham, UK) using the CrystalShiŌer crystal harvesƟng robot (Oxford LabTech, UK) and cryo-protected in a soluƟon of 25% Ethylene Glycol. DiffracƟon quality crystals of complex of RH5ΔNL:R5.034:R5.028 Fabs were obtained from PEG / Ion Screen (Hampton Research, Aliso Viojo, CA) condiƟon H6 (0.02 M Calcium chloride dihydrate, 0.02 M Cadmium chloride hydrate, 0.02 M Cobalt(II) chloride hexahydrate, 20% w / v Polyethylene glycol 3,350). All diffracƟon data were collected at Diamond Light Source (Proposal ID: mx28172). IniƟally samples were sent to i03 for UnaƩended Data CollecƟon (NaƟve Experiment; 12.7 keV, 1.7 Å, 2 x 360° sweeps, 1st at chi=0 and 2nd at chi=30), before being transferred to i24 for manual data collecƟon (4.00Å, 360°). Data Processing and Model Refinement Datasets for RH5ΔNL:R5.034:R5.028 were manually processed on the Diamond Cluster using DIALSs, confirming the auto-processed xia2.DIALS65 output from SynchWeb / iSpyB. All subsequent processing was done on local computers using the CCP4i GUI or on CCP4 Cloud. RH5ΔNL:R5.034 data was truncated at 3.2 Å and 4 Å, respecƟvely. Although the apparent crystal symmetry was orthorhombic, refinement failed to reduce R-free as would usually be expected. Data for the putaƟve complex of RH5ΔNL:R5.034:R5.028 were reprocessed in P21 with a beta angle of ∼90° and pseudomerohedral twinning is suspected; however, there was no evidence of R5.028 Fab in the data, suggesƟng it was lost during crystal formaƟon with just RH5ΔNL:R5.034 remaining. Molecular replacement was done with Phaser using homology model coordinates downloaded from the Protein Data Bank (PDB) based on a sequence similarity search. The following homology models were used for: i) RH5ΔNL (PDB: 4WAT); and ii) R5.251 Variable, Heavy (PDB: 6OC7); Constant, Heavy (PDB: 6OC7); Variable, Light (PDB: 5XKU); Constant, Light (PDB: 5XKU); and iii) R5.034 Variable, Heavy (PDB: 5X8M); Constant, Heavy (PDB: 1BJ1); Variable, Light (PDB: 5WL2); Constant, Light (PDB: 3H0T). Subsequent model refinement and building was performed in Coot and REFMAC. Once stable models had been built they were put through the PDB-REDO pipeline to be opƟmized, and LORESTR for further low- resoluƟon refinement. ComputaƟonal PredicƟon of GIA from mAb Gene Usage Subject gene usage was one-hot encoded using the R package mltools (v0.3.5). To assess the relaƟonship more robustly between gene usage and GIA %, only pairs of genes that occurred in at least 4 individuals were considered. Further filtering was applied to select only gene pairs whose mean associated GIA % was outside a conservaƟvely selected 33% deviaƟon from the dataset mean (below 42% GIA %, or above 82% GIA %). An addiƟonal requirement was added that GIA % values associated with gene pairs must be either enƟrely above or below the dataset mean and not spanning. To assess staƟsƟcal significance, 1000 rounds of permutaƟon were run, where gene use was scrambled across the dataset and the same filtering was performed to search for significant gene pairs. A P value (P < 0.001) was calculated from the tail probability of the generated null distribuƟon. An R markdown for the analysis is available. R5.034 and R5.034LS Binding KineƟcs to RH5.1 SPR was carried out using the Biacore™ X100 machine and soŌware. Purified recombinant R5.034 or R5.034LS was immobilized on Sensor Chip Protein G (CyƟva) through a 30 s injecƟon of 16 nM anƟbody. RH5.1 protein was diluted in PBS + P20 running buffer (137 mM NaCl, 2.7 mM KCl, 10mM Na2HPO4, 1.8 mM KH2PO4, 0.005% surfactant P20 (CyƟva)) to yield a final concentraƟon of 15.6 nM. Samples were injected for 180 s at 30 μL / min before dissociaƟon for 800 s. The chip was then regenerated with a 45 s injecƟon of 10 mM glycine pH 1.5. AnƟbody kineƟcs were determined through a two-fold, five-step diluƟon curve. Data were analyzed using the Biacore X100 EvaluaƟon soŌware v2.0.2. A global Langmuir 1:1 interacƟon model was used to determine anƟbody kineƟcs. R5.034 and R5.034LS Binding KineƟcs to Human FcRn SPR was carried out using the Biacore™ X100 machine and soŌware. Recombinant human FcRn protein (Acro Biosystems) was immobilized onto a CM5 Sensor Chip (CyƟva) using the standard amine coupling protocol yielding ∼200 response units (RU). R5.034 and R5.034LS were diluted to a final concentraƟon of 6.4 μM and 1.6 μM, respecƟvely, in either MES pH 6.0 (20 mM MES, 150 mM NaCl) or TBS pH 7.4 (20 mM Tris-HCl, 150 mM NaCl) running buffer. Samples were injected for 180 s at 30 μL / min before dissociaƟon for 600 s. The chip was regenerated with a 30 s injecƟon of PBS pH 7.4. Affinity was determined using a two-fold, nine-step diluƟon curve. Data were analyzed using the Biacore X100 EvaluaƟon soŌware v2.0.2, and the equilibrium dissociaƟon constant was determined from a plot of steady state binding levels. Example 1: IsolaƟon of human monoclonal anƟbodies against RH5 240 human mAbs were isolated from vaccinees in a clinical trial and produced as recombinant IgG1 molecules. A pictorial diagram showing the vaccinaƟon regimens and sampling of the Phase IIa clinical vaccine trial (ClinicalTrials.gov NCT02927145 (1)) from whi...

Claims

Claims 1. An anƟ-PfRH5 anƟbody that specifically binds to a PfRH5 sequence, wherein the anƟbody binds to an epitope on PfRH5 but does not cross-block the binding of an anƟbody comprising a heavy chain variable region and a light chain variable region having the sequence of SEQ ID NO: 79 and SEQ ID NO: 80 respecƟvely to the PfRH5 sequence; opƟonally wherein the anƟbody interacts with: one or more residues selected from the list consisƟng of: ILE 193, THR 199, GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, THR 216, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or one or more residues selected from the list consisƟng of: LYS 212, THR 216, LYS 219, VAL 220, LYS 327, ILE 328, and ASP 331 of SEQ ID NO: 65; and wherein said anƟbody does not interact with all the aforemenƟoned residues, and opƟonally wherein binding is determined by X-ray crystallography or cryo-electron microscopy (cryo-EM).

2. An anƟ-PfRH5 anƟbody that specifically binds to a PfRH5 sequence comprising SEQ ID NO: 65, wherein the anƟbody interacts with: one or more residues selected from the list consisƟng of: ILE 193, THR 199, GLY 201, LYS 202, CYS 203, ILE 204, ALA 205, VAL 206, ASP 207, ALA 208, PHE 209, LYS 211, LYS 212, ILE 213, GLU 215, THR 216, ASP 331, ASN 334, TYR 335, ASN 338, LEU 339, and GLN 342 of SEQ ID NO: 65; and / or one or more residues selected from the list consisƟng of: LYS 212, THR 216, LYS 219, VAL 220, LYS 327, ILE 328, and ASP 331 of SEQ ID NO: 65; and wherein said anƟbody does not interact with all the aforemenƟoned residues, and opƟonally wherein binding is determined by X-ray crystallography or cryo-electron microscopy (cryo-EM).

3. The anƟbody according to claim 1 or 2, which binds to a disconƟnuous epitope consisƟng of: LYS 202, ILE 204, ALA 205, ALA 208, PHE 209, LYS 212, ILE 213, THR 216, LYS 219, ASN 323, ASP 324, PHE 325, ASN 326, LYS 327, ILE 328, MET 330, ASP 331, LYS 333, ASN 334, TYR 335, THR 337, ASN 338, LEU 339, GLU 341 and GLN 342 of SEQ ID NO:

65.

4. The anƟbody according to any one of claims 1-3, which binds to a disconƟnuous epitope consisƟng of: (a) an amino acid sequence selected from the list consisƟng of: SEQ ID NO: 85,SEQ ID NO: 86, SEQ ID NO: 81 and SEQ ID NO: 83; and (b) an amino acid sequence selected from the group consisƟng of: SEQ ID NO: 89 or SEQ ID NO: 90, SEQ ID NO: 82, SEQ ID NO: 84, SEQ ID NO: 87 and SEQ ID NO:

88.

5. The anƟbody according to any one of claims 1-4, comprising a heavy chain or fragment thereof and a light chain or fragment thereof, wherein each of the heavy and light chains, or fragments thereof, comprise a variable region and said variable regions each comprise three CDR sequences; wherein: the heavy chain CDR sequences comprise SEQ ID NO: 1, 2 and 3, and the light chain CDR sequences comprise SEQ ID NO: 4, 5 and 6; the heavy chain CDR sequences comprise SEQ ID NO: 7, 8 and 9, and the light chain CDR sequences comprise SEQ ID NO: 10, 11 and 12; the heavy chain CDR sequences comprise SEQ ID NO: 13, 14 and 15, and the light chain CDR sequences comprise SEQ ID NO: 16, 17 and 18; the heavy chain CDR sequences comprise SEQ ID NO: 19, 20 and 21, and the light chain CDR sequences comprise SEQ ID NO: 22, 23 and 24; the heavy chain CDR sequences comprise SEQ ID NO: 25, 26 and 27 and the light chain CDR sequences comprise SEQ ID NO: 28, 29 and 30; or the heavy chain CDR sequences comprise SEQ ID NO: 31, 32 and 33, and the light chain CDR sequences comprise SEQ ID NO: 34, 35 and 36.

6. An anƟ-PfRH5 anƟbody comprising a heavy chain or fragment thereof and a light chain or fragment thereof, wherein each of the heavy and light chains, or fragments thereof, comprise a variable region and said variable regions each comprise three CDR sequences; wherein: the heavy chain CDR sequences comprise SEQ ID NO: 1, 2 and 3, and the light chain CDR sequences comprise SEQ ID NO: 4, 5 and 6; the heavy chain CDR sequences comprise SEQ ID NO: 7, 8 and 9, and the light chain CDR sequences comprise SEQ ID NO: 10, 11 and 12; the heavy chain CDR sequences comprise SEQ ID NO: 13, 14 and 15, and the light chain CDR sequences comprise SEQ ID NO: 16, 17 and 18; the heavy chain CDR sequences comprise SEQ ID NO: 19, 20 and 21, and the light chain CDR sequences comprise SEQ ID NO: 22, 23 and 24;the heavy chain CDR sequences comprise SEQ ID NO: 25, 26 and 27 and the light chain CDR sequences comprise SEQ ID NO: 28, 29 and 30; or the heavy chain CDR sequences comprise SEQ ID NO: 31, 32 and 33, and the light chain CDR sequences comprise SEQ ID NO: 34, 35 and 36.

7. The anƟbody of any one of claims 1-6, wherein the anƟbody comprises: a heavy chain comprising SEQ ID NO: 37 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 38 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 39 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 40 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 41 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 42 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 43 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 44 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 45 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 46 or a sequence having 80% sequence idenƟty thereto; or a heavy chain comprising SEQ ID NO: 47 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 48 or a sequence having 80% sequence idenƟty thereto.

8. The anƟbody of any one of the preceding claims, wherein the anƟbody is a monoclonal anƟbody.

9. The anƟbody of any one of the preceding claims, wherein the anƟbody is a neutralising anƟbody.

10. The anƟbody of any one of the preceding claims, wherein the anƟbody is fully human or humanised.

11. The anƟbody of any one of the preceding claims, wherein the anƟbody is a full-length anƟbody.

12. The anƟbody of any one of claims 1-9, wherein the anƟbody is a scFv, Fv, Fab or Fab’ fragment.

13. The anƟbody of any one of the preceding claims, wherein the anƟbody has a growth inhibitory acƟvity (GIA) of at least 50% against a plurality of geneƟc strains of the blood-stage Plasmodium parasite, preferably wherein the EC50GIA value is lower than 10 µg / mL.

14. The anƟbody according to any one of the preceding claims, wherein the anƟbody binds to PfRH5 with a binding affinity in the range of 30 pM to 5 nM range.

15. The anƟbody of any one of the preceding claims, further comprising a signal pepƟde; wherein opƟonally the signal pepƟdes direct secreƟon from human cells, and preferably said signal pepƟde is a mammalian signal pepƟde from Ɵssue plasminogen acƟvator.

16. An anƟbody molecule or anƟgen-binding fragment thereof that competes for binding to PfRH5 with an anƟbody or anƟgen-binding fragment thereof according to any one of the preceding claims.

17. An anƟbody molecule or anƟgen-binding fragment thereof that binds to the same epitope as an anƟbody or anƟgen-binding fragment thereof according to any one of claims 1 to 15.

18. An isolated nucleic acid sequence, or pair of isolated nucleic acid sequences, encoding the heavy and / or the light chain(s) of an anƟbody as defined in any one of the preceding claims; opƟonally wherein the anƟbody comprises: a heavy chain comprising SEQ ID NO: 37 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 38 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 39 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 40 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 41 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 42 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 43 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 44 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 45 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 46 or a sequence having 80% sequence idenƟty thereto; or a heavy chain comprising SEQ ID NO: 47 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 48 or a sequence having 80% sequence idenƟty thereto.

19. A vector or pair of vectors encoding the heavy and / or the light chain(s) of an anƟbody as defined in any one of claims 1 to 17; opƟonally wherein the anƟbody comprises: a heavy chain comprising SEQ ID NO: 37 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 38 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 39 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 40 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 41 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 42 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 43 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 44 or a sequence having 80% sequence idenƟty thereto; a heavy chain comprising SEQ ID NO: 45 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 46 or a sequence having 80% sequence idenƟty thereto; or a heavy chain comprising SEQ ID NO: 47 or a sequence having 80% sequence idenƟty thereto and a light chain comprising SEQ ID NO: 48 or a sequence having 80% sequence idenƟty thereto.

20. The vector or pair of vectors according to claim 19, wherein the vector is capable of expression in a mammalian cell; preferably a Chinese hamster ovary (CHO) cell.

21. The vector or pair of vectors according to claim 19 or 20, wherein the vector is capable of expression in a heterologous protein expression system.

22. The vector or pair of vectors according to any one of claims 19 to 21, wherein the vector is a viral vector, opƟonally wherein the viral vector is a human or simian adenovirus, an adeno- associated virus (AAV), or a pox virus, preferably an AdHu5, ChAd63, ChAdOX1, ChAdOX2 or modified vaccinia Ankara (MVA) vector.

23. A host cell comprising an isolated nucleic acid sequence or pair of isolated nucleic acid sequences according to claim 18 or a vector or pair of vectors as defined in any one of claims 19 to 22.

24. A composiƟon comprising one or more anƟbody as defined in any one of claims 1 to 17 and opƟonally comprising one or more of a pharmaceuƟcally acceptable excipient, diluent, or carrier.

25. A composiƟon comprising a vector or pair of vectors according to any one of claims 19 to 22 and opƟonally comprising one or more of a pharmaceuƟcally acceptable excipient, diluent, or carrier.

26. The composiƟon according to claim 25, wherein the vector is selected from a viral vector, RNA vaccine, or DNA plasmid.

27. An anƟbody, isolated DNA molecule, vector, or composiƟon according to any one of claims 1 to 26 for use in therapy.

28. An anƟbody, isolated DNA molecule, vector, or composiƟon according to any one of claims 1 to 26 for use in treaƟng and / or prevenƟng malaria.

29. An anƟbody, isolated DNA molecule, vector, or composiƟon according to any one of claims 1 to 26 for use as an immuno-prophylacƟc therapeuƟc, wherein the anƟbody has a growth inhibitory acƟvity (GIA) of at least 50% against the blood-stage Plasmodium parasite; wherein opƟonally: the growth inhibitory acƟvity (GIA) of at least 50% is against a plurality of geneƟc strains of the blood-stage Plasmodium parasite, preferably wherein the EC50GIA value is less than 10 µg / mL; and / or the Plasmodium parasite is Plasmodium falciparum.

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