Methods of treating viral infections

Abstract

The present disclosure generally relates to viral infections and methods of treating viral infections, in particular viral infections caused by coronaviruses.

Description

[0001] Methods of treating viral infections Cross-reference to related applications The present application claims priority from Australian Provisional Patent Application No. 2023902844 filed on 4 September 2023, the contents of which are incorporated herein by reference in their entirety. Technical Field The present disclosure generally relates to viral infections and methods of treating viral infections, in particular viral infections caused by coronaviruses. Background The COVID-19 pandemic is driven by the SARS-CoV-2 virus and has resulted in over 6.9 million deaths – marking it as arguably the biggest medical emergency of the past century1. As a result of the continuous emergence of subvariants, current vaccines have been losing effectiveness2,3. Two doses of the BNT162b2 (Pfizer–BioNTech) or ChAdOx1 nCoV-19 (AstraZeneca) vaccines offer no protection against the omicron (B.1.1.529) variant 25 weeks after administration4. These vaccines target the ever-mutating SARS-CoV-2 spike protein (S-protein). Cytokine storms can be caused by viral respiratory infections such as those caused by SARS-CoV-1 or SARS-CoV-2. A cytokine storm is a physiological reaction in which the innate immune system causes an uncontrolled and excessive release of cytokines, which are pro- inflammatory signalling molecules. The sudden release in large quantities of these molecules can cause multisystem organ failure and even death5. Accordingly, there remains a need for additional therapies for not only preventing or treating an initial coronavirus infection, but also any immune- mediated inflammation resulting therefrom. Summary The present disclosure is based, in part, on the recognition that existing vaccines and therapeutic agents for the treatment and / or prevention of SARS-CoV-2 infection are limited in their efficacy. The present disclosure provides peptides with potent antiviral and anti- inflammatory activity. The inventors have shown that these peptides have an antiviral effect in vivo and in vitro. For example, it has been shown that exemplary peptides of the disclosure inhibit plaque formation in SARS-CoV-2 infected Vero cells and significantly reduced viral replication in SARS- CoV-2 infected mice. These findings by the inventors provide new compounds with antiviral activity and uses of such compounds e.g., to treat a SARS-CoV-2 infection in a subject. Accordingly, the present disclosure provides a method of treating or preventing a viral infection or a disease, disorder or condition associated therewith in a subject, said method including the step of administering a therapeutically effective amount of a vimentin inhibitor to the subject to thereby treat or prevent the viral infection, wherein the vimentin inhibitor is a cyclic peptide that inhibits or prevents binding of virus to a host cell of the subject. In one example, the disease, disorder or condition associated with the viral infection may be a cytokine storm. In another example, the disease, disorder or condition associated with the viral infection may be inflammation. In another example, the disease, disorder or condition associated with the viral infection may be long COVID-19. Suitably, the viral infection is selected from the group consisting of a coronavirus infection, an influenza virus infection and a respiratory syncytial virus (RSV) infection. In some examples, the viral infection is an influenza virus infection, such as a H3N2 influenza virus infection. In certain examples, the viral infection is a RSV infection, such as an RSV4 infection. The viral infection may be a coronavirus infection. The coronavirus infection may be a COVID-19 or SARS-CoV-2 infection, a SARS-CoV1 infection or a MERS-CoV infection. In one example, the coronavirus infection is a SARS-CoV-2 infection. The SARS-CoV-2 may selected from the group consisting of a Wuhan strain, a Delta strain and an Omicron strain. In one example, the SARS-CoV-2 is the Wuhan strain. In another example, the SARS-CoV-2 is the Delta strain. In another example, the SARS-CoV-2 is the Omicron strain. In any of the methods disclosed herein, the vimentin inhibitor may inhibit or prevent formation of a complex between a viral surface protein and a receptor on the host cell. In one example, the viral surface protein is an S-glycoprotein. In another example, the receptor is the angiotensin converting enzyme-2 (ACE-2) receptor. In any of the methods disclosed herein, the cyclic peptide is cyclo-((2-Nal)-Leu-Ser-(2- Nal)-Arg) or a derivative thereof. In one example, the cyclic peptide is administered at a dose of about 5 mg to about 25 mg. The cyclic peptide may be administered orally or by inhalation. In one example, the subject may be receiving a further treatment for the viral infection. Similarly, any of the methods disclosed herein may include the further step of administering a further treatment for the viral infection to the subject. The further treatment may be or may comprise a further treatment for a SARS-CoV-2 infection. In one example, the further treatment is selected from the group consisting of an antiviral agent, a bronchial muscle / airway relaxant, oxygen, an antibody, and an antibacterial agent. In one example, the antiviral agent is one or more of remdesivir, kaletra, lopinavir, molnupiravir, nirmaterlvir and ritonavir. In another example, the antibody is sarilumab or tocilizumab. In any of the methods disclosed herein, the vimentin inhibitor inhibits or prevents autophagy of the host cell. In any of the methods disclosed herein, the vimentin inhibitor inhibits or prevents an inflammatory response associated with the viral infection. The inflammatory response may be due to or associated with a cytokine storm. In any of the methods disclosed herein, the vimentin inhibitor may reduce the likelihood of long COVID-19 in a subject infected or previously infected with SARS-CoV-2. The present disclosure also provides a method of reducing the infectivity of a virus, said method including the step of contacting the virus with a cyclic peptide that is a vimentin inhibitor to thereby reduce the infectivity of the virus. In one example, the cyclic peptide is cyclo-((2-Nal)-Leu-Ser-(2-Nal)-Arg) or a derivative thereof. The virus may be a SARS-CoV-2 virus, a SARS-CoV1 virus or a MERS-CoV virus. In one example, the virus is a SARS-CoV-2 virus. The present disclosure also provides a method of identifying, designing or producing an agent for use in treating or preventing an infection with a virus, said method including the steps of: (a) contacting a cell with the virus and a candidate agent, wherein the candidate agent is a cyclic peptide; (b) determining whether the candidate agent inhibits the binding of vimentin on the host cell to a viral surface protein of the virus. The method disclosed herein may further include determining whether the candidate agent inhibits a direct physical association between vimentin and the viral surface protein. In one example, the viral surface protein is a S-glycoprotein. In any of the methods disclosed herein, the candidate agent may be a derivative of cyclo- ((2-Nal)-Leu-Ser-(2-Nal)-Arg). The present method may further include the step of isolating and / or purifying an agent that inhibits the binding of vimentin to the viral surface protein. The present method may further include the step of formulating the isolated and / or purified agent into a pharmaceutically acceptable formulation. In one example, the method further includes the step of sterilising the formulation. In another example, the method further includes the step of filling the formulation into a container. The container may be any one or more of a vial, an ampoule, a bag, a blister pack, a bottle, a cartridge, an injection needle, an injection syringe, a single dose container, a strip of multiple single dose containers, or a tube. Also disclosed herein is an agent for use in treating or preventing an infection with a virus, obtained by the methods disclosed herein. Brief description of the drawings The following figures form part of the present specification and are included to further demonstrate certain aspects of the present disclosure. The disclosure may be better understood by reference to one or more of these figures in combination with the detailed description of specific embodiments presented herein. Figure 1. A. Effects of FLM-c2 treatment on plaque formation comparing Wuhan, Delta (Δ) & Omicron (O) variants with DMSO, and the FLM-c2 precursor analogue, cF. B. Plaque images following FLM-c2 treatment compared with cf and DMSO. C. Plaque count of FLM-c2 and cf treated plates in comparison with Cisplatin and Oxiplatin. Figure 2: A. Treatment schedule of FLM-c2 to Delta infected mice treated prophylactically once daily commencing on Day 2 pre-viral infection. B. Plaque forming unit counts in lung and brain tissue of mice treated with either vehicle, 1.4 mg / kg FLM-c2 or 14 mg / kg of FLM-c2 (N = 4). C. Treatment schedule of FLM-c2 to Delta infected mice treated therapeutically once daily commencing on Day 1 post-viral infection. Plaque forming unit counts in lung and brain tissue of mice treated with either vehicle, 1.4 mg / kg FLM-c2 or 14 mg / kg of FLM-c2 (N = 4). Figure 3. A. Predicted binding of FLM-c2 to vimentin coil 2. B. In vitro binding assay showing % binding of hGIIA to vimentin ‘coil 2’ with FLM-c2, LY311727- legacy inhibitor of sPLA2 enzyme activity and withaferin A-vimentin inhibitor. C. Immunofluorescent imagines of Vero cells stained for extracellular vimentin (green) and SARS-CoV-2 (orange) infected with either Mock, Delta or Omicron virus and treated with either DMSO, 50 or 100 µM FLM-c2 for 72 hours. Figure 4: A. FLM-c2 reduces endosomal trafficking of sequestered cargo. B. PC-3 cells treated showing sequestered hGIIA (red) after treatment with DMSO or C. c2 (100 µM), resulting in enlarged and stagnant vesicles. Figure 5. Change in plasma hGIIA concentration following oral administration of FLM-c2 (10 mg daily for six weeks) to men with advanced prostate cancer. Data are % change over baseline. Samples were assayed in triplicate. Baseline concentrations ranged from 1.3 ng / mL (sample 1) to 27.8 ng / mL (sample 9). Figure 6. Inhibitory efficiency of c2 against an influenza virus (a human H3N2 strain). N (Neat): 200 PFU influenza virus; -N: 10-N. Control = DMSO+virus. Figure 7. Inhibitory efficiency of the C2 drug against RSV (RSV 4 clinical isolate). N (Neat): 200 PFU RSV4; -N: 10-N. Control = DMSO+virus. Key to the Sequence Listing SEQ ID NO: 1 Amino acid sequence of vimentin SEQ ID NO: 2 Amino acid sequence of hGIIA protein with signal sequence SEQ ID NO: 3 Amino acid sequence of hGIIA protein without signal sequence Detailed Description General Throughout this specification, unless specifically stated otherwise or the context requires otherwise, reference to a single step, feature, composition of matter, group of steps or group of features or compositions of matter shall be taken to encompass one and a plurality (i.e. one or more) of those steps, features, compositions of matter, groups of steps or groups of features or compositions of matter. Those skilled in the art will appreciate that the present disclosure is susceptible to variations and modifications other than those specifically described. It is to be understood that the disclosure includes all such variations and modifications. The disclosure also includes all of the steps, features, compositions and compounds referred to or indicated in this specification, individually or collectively, and any and all combinations or any two or more of said steps or features. The present disclosure is not to be limited in scope by the specific examples described herein, which are intended for the purpose of exemplification only. Functionally-equivalent products, compositions and methods are clearly within the scope of the present disclosure. Any example of the present disclosure herein shall be taken to apply mutatis mutandis to any other example of the disclosure unless specifically stated otherwise. Unless specifically defined otherwise, all technical and scientific terms used herein shall be taken to have the same meaning as commonly understood by one of ordinary skill in the art (for example, in cell culture, molecular genetics, immunology, immunohistochemistry, protein chemistry, and biochemistry). Unless otherwise indicated, the recombinant DNA, recombinant protein, cell culture, and immunological techniques utilized in the present disclosure are standard procedures, well known to those skilled in the art. Such techniques are described and explained throughout the literature in sources such as, J. Perbal, A Practical Guide to Molecular Cloning, John Wiley and Sons (1984), J. Sambrook et al. Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press (1989), T.A. Brown (editor), Essential Molecular Biology: A Practical Approach, Volumes 1 and 2, IRL Press (1991), D.M. Glover and B.D. Hames (editors), DNA Cloning: A Practical Approach, Volumes 1-4, IRL Press (1995 and 1996), and F.M. Ausubel et al. (editors), Current Protocols in Molecular Biology, Greene Pub. Associates and Wiley-Interscience (1988, including all updates until present), Ed Harlow and David Lane (editors) Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory, (1988), and J.E. Coligan et al. (editors) Current Protocols in Immunology, John Wiley & Sons (including all updates until present). Throughout this specification, unless the context requires otherwise, the word "comprise", or variations such as "comprises" or "comprising", is understood to imply the inclusion of a stated step or element or integer or group of steps or elements or integers but not the exclusion of any other step or element or integer or group of elements or integers. The term “and / or”, e.g., “X and / or Y” shall be understood to mean either “X and Y” or “X or Y” and shall be taken to provide explicit support for both meanings or for either meaning. Any discussion of documents, acts, materials, devices, articles or the like which has been included in the present specification is not to be taken as an admission that any or all of these matters form part of the prior art base or were common general knowledge in the field relevant to the present disclosure as it existed before the priority date of each of the appended claims. As used herein, the singular forms of “a”, “and” and “the” include plural forms of these words, unless the context clearly dictates otherwise. For example, a reference to “a bacterium” includes a plurality of such bacteria, and a reference to “an allergen” is a reference to one or more allergens. Throughout the present specification, various aspects and components of the disclosure can be presented in a range format. The range format is included for convenience and should not be interpreted as an inflexible limitation on the scope of the present disclosure. Accordingly, the description of a range should be considered to have specifically disclosed all the possible sub- ranges as well as individual numerical values within that range, unless specifically indicated. For example, description of a range such as from 1 to 5 should be considered to have specifically disclosed sub-ranges such as from 1 to 3, from 1 to 4, from 1 to 5, from 2 to 4, from 2 to 5, from 3 to 5 etc., as well as individual and partial numbers within the recited range, for example, 1, 2, 3, 4, 5, 5.5 and 6, unless where integers are required or implicit from context. This applies regardless of the breadth of the disclosed range. Where specific values are required, these will be indicated in the specification. The term “about” in relation to a numerical value x is optional and means, for example, any number within (i.e., plus or minus) 1%, 5% or 10% of the referenced number. In certain examples, the term “about” encompasses the exact number recited. The term “substantially” does not exclude “completely” (e.g., a composition which is “substantially free” from Y may be completely free from Y). All computer programs, algorithms, gene and protein accession numbers and their associated sequences, patents, patent applications and scientific literature referred to herein is incorporated herein by reference. Methods of treating In one broad form, the present disclosure provides a method of treating or preventing a viral infection or a disease, disorder or condition associated therewith in a subject, said method including the step of administering a therapeutically effective amount of a vimentin inhibitor to the subject to thereby treat or prevent the viral infection, wherein the vimentin inhibitor is a cyclic peptide that inhibits or prevents binding of virus to a host cell of the subject. In a related form, the present disclosure relates to the use of a vimentin inhibitor in the manufacture of a medicament for treating or preventing a viral infection or a disease, disorder or condition associated therewith in a subject, wherein the vimentin inhibitor is a cyclic peptide that inhibits or prevents binding of virus to a host cell of the subject. In a further form, the present disclosure provides for the use of a vimentin inhibitor in a method of treating or preventing a viral infection or a disease, disorder or condition associated therewith in a subject, wherein the vimentin inhibitor is a cyclic peptide that inhibits or prevents binding of virus to a host cell of the subject. As used herein, the terms “treating”, “treat” or “treatment” and variations thereof, refer to clinical intervention designed to alter the natural course of the individual or cell being treated during the course of clinical pathology. Desirable effects of treatment include decreasing the rate of disease progression, ameliorating or palliating the disease state, and remission or improved prognosis. As used herein, the terms “prevent”, “prevented”, or “preventing”, refer to a prophylactic treatment which increases the resistance of a subject to developing the disease or condition or, in other words, decreases the likelihood that the subject will develop the disease or condition as well as a treatment after the disease or condition has begun in order to reduce or eliminate it altogether or prevent it from becoming worse. These terms also include within their scope preventing the disease or condition from occurring in a subject which may be predisposed to the disease or condition but has not yet been diagnosed as having it. As used herein, the term “subject” refers to any animal, for example, a mammalian animal, including, but not limited to humans, non-human primates, livestock (e.g., sheep, horses, cattle, pigs, donkeys), companion animals (e.g., pets such as dogs and cats), laboratory test animals (e.g., mice, rabbits, rats, guinea pigs), performance animals (e.g., racehorses, camels, greyhounds) or captive wild animals. In various examples, the “subject” is a human. Typically, the terms “subject” and “patient” are used interchangeably herein, particularly in reference to a human subject. The methods disclosed herein may be a method of treating or preventing a disease, disorder or condition involving a viral infection, in a subject having or susceptible to the disease, disorder or condition. Accordingly, in a particular form, the present disclosure provides a method of treating or preventing a viral infection or a disease, disorder or condition associated therewith in a subject. Suitably, the viral infection described herein is at least partly mediated by vimentin. In this regard, vimentin can facilitate binding of a surface protein of a virus to a host cell, such as a surface protein or receptor thereon. In one example, the viral infection is a coronavirus infection. In one example, the subject may be receiving further treatment for the viral infection. In some examples, the disease, disorder or condition may be a disease, disorder or condition associated with a viral infection. In particular examples, the disease, disorder or condition is long COVID-19. As used herein, “long COVID-19” refers to when symptoms of a SARS-CoV-2 infection remain, or develop, long after the initial SARS-CoV-2 infection. These symptoms include, but are not limited to, extreme fatigue, shortness of breath, heart palpitations, chest pain or tightness, problems with memory and / or concentration (e.g., “brain fog”), changes to taste and / or smell and joint or muscle pain. In any of the methods disclosed herein, the method may include the further step of administering a further treatment for the viral infection to the subject. The further treatment may be administered simultaneously with or before or after treatment with the vimentin inhibitor. In one example, the further treatment is administered to the subject simultaneously with the vimentin inhibitor. In another example, the further treatment is administered to the subject before the vimentin inhibitor. In another example, the further treatment is administered to the subject after the vimentin inhibitor. In one example, the further treatment is or comprises a further treatment for a SARS-CoV-2 infection. Suitable further treatments for SARS-CoV-2 infection are known in the art. For example, suitable further treatments include but are not limited to, corticosteroids, an antiviral agent, a bronchial muscle / airway relaxant, oxygen, an antibody, and an antibacterial agent. In one example, the corticosteroid is dexamethasone. Suitable examples of bronchial muscle / airway relaxants are known in the art and include but are not limited to, xanthine derivatives such as theophylline, beta-2 agonists such as salbutamol, levalbuterol or pirbuterol or anticholinergic drugs such as aclidinium bromide, tiotropium bromide, glycopyrrolate bromide or umeclidinium bromide. Suitable examples of antibacterial agents include, but are not limited to, azithromycin, doxycycline, clarithromycin, ceftriaxone, erythromycin, amoxicillin, amoxicillin-clavulanic acid, ampicillin, gentamicin, benzylpenicillin, piperacillin / tazobactam, ciprofloxacin, ceftazidime, cefepime, vancomycin, meropenem, and cefuroxime. In one example, the antiviral agent is one or more of remdesivir, kaletra (lopinavir / ritonavir), lopinavir, molnupiravir, nirmatrelvir and ritonavir. In another example, the antibody is sarilumab or tocilizumab. In another example, the further treatment is treatment with a janus kinase (JAK) inhibitor, such as baricitinib. Any of the methods disclosed herein may reduce the infectivity of a virus, said method including the step of contacting the virus with a cyclic peptide that is a vimentin inhibitor to thereby reduce the infectivity of the virus. Coronavirus infection The Coronaviruses are a group of related RNA viruses that cause diseases in mammals and birds. In humans and birds, they cause respiratory tract infections that can range from mild to lethal. Mild illnesses in humans include some cases of the common cold (which is also caused by other viruses, predominantly rhinoviruses), while more lethal varieties can cause SARS, MERS and COVID-19. Coronaviruses are large, roughly spherical particles with unique surface projections. They are enclosed in an envelope embedded with a number of protein molecules. The lipid bilayer envelope, membrane proteins, and nucleocapsid protect the virus when it is outside the host cell. The viral envelope is made up of a lipid bilayer in which the membrane (M), envelope (E) and spike (S) structural proteins are anchored. In one example, the coronavirus infection is a SARS-CoV-2 infection. COVID-19 is caused by the SARS-CoV-2 virus, which enters human cells via an S-protein interaction with the human ACE2 receptor6. It is envisaged that the SARS-CoV-2 virus provided herein may be of any strain known in the art. Moreover, the present methods may also be applied to future and emerging strains of the virus. To this end, it is contemplated that the methods described herein may be applicable across SARS-CoV-2 virus strains broadly owing to the role the cyclic peptides described herein play in binding vimentin, a critical co-factor in facilitating interaction of host cell ACE2 receptor with the S-protein of the SARS-CoV-2 virus. In any of the methods disclosed herein, the SARS-CoV-2 virus may be selected from the group consisting of a Wuhan strain, a Delta strain and an Omicron strain. In one example, the SARS-CoV-2 is the Wuhan strain. In another example, the SARS-CoV-2 is the Delta strain. In another example, the SARS-CoV-2 is the Omicron strain. Influenza viruses Suitably, the virus described herein is an influenza virus. Influenza viruses are enveloped RNA viruses that belong to the family of Orthomyxoviridae (Palese and Shaw (2007) Orthomyxoviridae: The Viruses and Their Replication, 5th ed. Fields' Virology, edited by B. N. Fields, D. M. Knipe and P. M. Howley. Wolters Kluwer Health / Lippincott Williams & Wilkins, Philadelphia, USA, p1647-1689). Influenza A and B viruses are major human pathogens, causing a respiratory disease that ranges in severity from sub-clinical infection to primary viral pneumonia which can result in death. The clinical effects of infection vary with the virulence of the influenza strain and the exposure, history, age, and immune status of the host. The natural hosts of influenza viruses are predominantly avian, but influenza viruses, particularly influenza A viruses (including those of avian origin) can also infect and cause illness in humans and other animal hosts (bats, canines, pigs, horses, sea mammals, and mustelids). The influenza viruses referred to herein encompass any virus type, subtype or strain including, but not limited to, naturally occurring strains, variants or mutants, mutagenized viruses, reassortant viruses and / or genetically modified viruses (e.g., modified by reverse genetics or recombinant DNA technology). The influenza virus of the present disclosure can be an influenza A virus or an influenza B virus. According to some examples, the influenza virus is an influenza A virus. In alternative examples, the influenza virus is an influenza B virus. The influenza A or B virus may be any strain of virus. By way of examples, the influenza A virus provided herein may include a HA subtype selected from H1, H2, H3, H4, H5, H6, H7, H8, H9, H10, H11, H12, H13, H14, H15 and H16. In some examples, the influenza A virus is of a H1 subtype (i.e., contains a modified HA protein of a H1 subtype). In other examples, the influenza A virus is of a H2 subtype (i.e., contains a modified HA protein of a H2 subtype). In particular examples, the influenza A virus is of a H3 subtype (i.e., contains a modified HA protein of a H3 subtype). Moreover, such viruses may contain the influenza A virus NA subtypes N1, N2, N3, N4, N5, N6, N7, N8 or N9. In some examples, the NA protein is of an N1, N2, N3 or N5 subtype. More particularly, the NA protein can be of an N1, N2 or N3 subtype. In certain examples, the influenza A virus can be a strain selected from the group consisting of H1N1, H1N2, H2N1, H2N2, H2N3, H3N1, H3N2, H3N8, H5N1, H7N1, H7N2, H7N3, H7N7, H9N2, and H10N7. According to some examples, the influenza A virus is a H1N1 strain. In alternative examples, the influenza A virus is a H3N2 strain. Respiratory syncytial viruses Suitably, the virus described herein is a RSV. RSV, which belongs to the virus family of Paramyxoviridae, is one of the most contagious pathogens and makes a substantial contribution to severe respiratory tract infections in infants, the elderly and immunocompromised patients. It is named Respiratory Syncytial Virus (RSV) because it produces a unique cell fusion effect in cultured cells. RSV can be divided into two strains or subtypes, RSV-A and RSV-B, based on differences in surface antigens. The virus is transmitted via air droplets and intimate contact. Respiratory syncytial virus contains 10 genes, encodes 11 proteins, of which the surface glycoprotein fusion protein (F protein) and attachment protein (G protein) are the most major viral antigens that provoke the body’s production of protective antibodies. Because the G protein has large difference among subtypes, the F protein is highly conserved among the subtypes, and the F protein directly mediates fusion of virus and cell, penetration of the virus and formation of syncytia, the protein is a main target protein for stimulating the body to generate protective antibodies. Herein, “respiratory syncytial virus” or “RSV” refers to any respiratory syncytial virus or RSV molecule known to those of skill in the art. For example, RSV can include any particular virus strain, subtype, variant, serotype, or isolate known in the art. For example, RSV can be from a mammal. In other examples, RSV can be from a human. Vimentin Vimentin is a type III intermediate filament (IF) protein that is expressed in mammalian cells including mesenchymal cells. IF proteins are found in all animal cells and bacterial cells. IFs, along with tubulin-based microtubules and actin-based microfilaments, comprise the cytoskeleton. Vimentin is the major cytoskeletal component of mesenchymal cells. Vimentin has been shown to play a role in supporting and anchoring the position of organelles in the cytosol. Vimentin may be attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Amongst other functions, vimentin is responsible for maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions. The protein sequence of vimentin is publicly available (e.g., P08670) and exemplary amino acid sequences are set forth in SEQ ID NO: 1 below. Thus, the vimentin amino acid sequence may be a protein which is at least 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% identical to the amino acid sequence set forth in SEQ ID NO: 1, or a fragment or derivative thereof. Vimentin protein sequence (SEQ ID NO: 1) MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVY ATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDK VRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNL AEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKL HEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKF ADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFA VEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRI SLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE The vimentin protein comprises a number of different domains. For example, the structural organization of a vimentin monomer comprises a central, mostly α-helical “rod” domain flanked by intrinsically disordered non–α-helical N-terminal (“head”) and C-terminal (“tail”) domains. The rod consists of two equally sized α-helical subdomains termed coil 1 (146 amino acids) and coil 2 (140 amino acids), which are connected by the 16 amino acid–long non–α-helical linker segment L12. Coil 1 is divided into a short coil 1A and a longer coil 1B segment. Linker L1 connecting the coil 1A and B subdomains is 8 amino acids long and evolutionarily highly conserved; similar to other intrinsically disordered domains, it may optionally form a distinct structure. Indeed, in the crystal of a larger fragment derived from coil 1, linker L1 adopts an α- helical fold without being involved in the coiled-coil formation of coil 1A and coil 1B. Coil 2 represents a continuous α-helix in which the first 35 amino acids form hendecad repeats establishing a right-handed helix with a very large pitch. Hence, in the dimer, the two chains essentially form parallel helices, which are designated as “paired bundle” or pb (Premchandar et al., 2016 J Biol Chem 291(48):24931-24950). It has been described previously that SARS-CoV-2 may interact with the intermediate filament vimentin, which can be expressed on the cell surface. Vimentin acts as a co-receptor for SARS-CoV-2, binding to a unique motif on the S-protein, facilitating protein binding to the ACE2 receptor in both cis and trans infections7-12. Without wishing to be bound by any theory, it is believed that the anti-viral action of the vimentin inhibitors described herein at least partly relates to their ability to inhibit or prevent S-protein binding to the ACE2 receptor. hGIIA Vimentin has also been suggested as interacting with human group IIA-secretedphospholipase A2 (hGIIA). Accordingly, the vimentin inhibitor described herein may additionallybe a hGIIA inhibitor. The protein sequence of hGIIA is publicly available (e.g., P14555) and exemplary amino acid sequences are set forth in SEQ ID NO: 2 and SEQ ID NO: 3 below. Thus, the hGIIA amino acid sequence may be a protein which is at least 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% identical to the amino acid sequence set forth in SEQ ID NO: 2, SEQ ID NO: 3 or a fragment or derivative thereof. The sequence in SEQ ID NO: 2 includes a signal peptide at the beginning of the protein (i.e., amino acid residues 1 to 20 of SEQ ID NO: 2), with the sequence for the mature hGIIA protein beginning at Asn 21 of SEQ ID NO: 2, which is absent in the mature protein of SEQ ID NO: 3. hGIIA protein sequence with signal sequence (SEQ ID NO: 2) MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKD ATDRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATC FARNKTTYNKKYQYYSNKHCRGSTPRC hGIIA protein sequence without signal sequence (SEQ ID NO: 3) NLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKR GCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFARNKTTYNKKYQYYSNK HCRGSTPRC Terms used generally herein to describe sequence relationships between respective nucleotides or polypeptides include “sequence identity”, “percentage of sequence identity” and “substantial identity”. Because respective nucleotides or polypeptides may each comprise (i) only one or more portions of a complete nucleotide or polypeptide sequence that are shared by the nucleotides or amino acids, and (ii) one or more portions which are divergent between the nucleotides or amino acids, sequence comparisons are typically performed by comparing sequences over a “comparison window” to identify and compare local regions of sequence similarity. A “comparison window” refers to a conceptual segment of typically 6, 9 or 12 contiguous residues that is compared to a reference sequence. The comparison window may comprise additions or deletions (i.e., gaps) of about 20% or less as compared to the reference sequence for optimal alignment of the respective sequences. Optimal alignment of sequences for aligning a comparison window may be conducted by computerised implementations of algorithms (Geneworks program by Intelligenetics; GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package Release 7.0, Genetics Computer Group, 575 Science Drive Madison, WI, USA, incorporated herein by reference) or by inspection and the best alignment (i.e. resulting in the highest percentage homology over the comparison window) generated by any of the various methods selected. Reference also may be made to the BLAST family of programs as for example disclosed by Altschul et al., 1997, Nucl. Acids Res. 253389, which is incorporated herein by reference. A detailed discussion of sequence analysis can be found in Unit 19.3 of CURRENT PROTOCOLS IN MOLECULAR BIOLOGY Eds. Ausubel et al. (John Wiley & Sons Inc NY, 1995-1999). The term “sequence identity” is used herein in its broadest sense to include the number of exact nucleotide or amino acid matches having regard to an appropriate alignment using a standard algorithm, having regard to the extent that sequences are identical over a window of comparison. Thus, a “percentage of sequence identity” is calculated by comparing two optimally aligned sequences over the window of comparison, determining the number of positions at which the identical nucleic acid base (e.g., A, T, C, G, U) or amino acid residue occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the window of comparison (i.e., the window size), and multiplying the result by 100 to yield the percentage of sequence identity. For example, “sequence identity” may be understood to mean the “match percentage” calculated by the DNASIS computer program (Version 2.5 for windows; available from Hitachi Software engineering Co., Ltd., South San Francisco, California, USA). Vimentin inhibitor As used herein, the term “vimentin inhibitor” shall be taken to mean an agent which hinders, reduces, restrains or prevents vimentin activity in a subject when administered in an effective amount relative to vimentin activity in a subject to which a vimentin inhibitor has not been administered. Vimentin activity may be inhibited in any measurable amount. Inhibition of vimentin activity may be complete or may be partial. Thus, the methods disclosed herein may comprise at least partial inhibition of vimentin activity. For example, the activity of vimentin may be reduced by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or 100% following administration of a vimentin inhibitor. (e.g., relative to the same measurement of activity before administration of the vimentin inhibitor). Vimentin activity may be measured through any suitable means known in the art, or any of the methods disclosed herein. For example, vimentin activity may be measured through assays which measure the level of one or more inflammatory markers, such as inflammatory cytokines, inflammatory prostaglandins or the proliferation of prostate cancer cells. In another example, the level of binding of vimentin to hGIIA and / or a level of hGIIA concentration and / or activity (e.g., blood / circulating or tissue levels) may be measured as a proxy of vimentin activity. Any suitable methods for determining the nature of the binding interaction between vimentin and hGIIA and / or hGIIA levels, such as circulating hGIIA levels, may be used. It will be understood by a person skilled in the art that inhibition may be achieved at the protein level. In one example, the vimentin inhibitor may inhibit or prevent formation of a complex between a viral surface protein and a receptor on the host cell. In one example, the viral surface protein is an S-glycoprotein. The inhibitor may be a direct inhibitor of a vimentin-S-glycoprotein interaction. For example, the inhibitor may bind to vimentin to inhibit its function by changing its conformation or by affecting or blocking its binding site such that it is no longer able to bind to the S-glycoprotein, such as by steric interference. Any vimentin inhibitor, such as those disclosed herein, may be capable of disrupting a vimentin-S- glycoprotein interaction, such that the endogenous function of the vimentin-S-glycoprotein complex is inhibited. In one example, the vimentin inhibitor inhibits or prevents autophagy of the host cell. In another example, the vimentin inhibitor inhibits or prevents an inflammatory response associated with the viral infection. Suitably, the inflammatory response is at least partly mediated or facilitated by hGIIA. In this regard, the vimentin inhibitor may inhibit or prevent an increase or promote a decrease in a level of hGIIA, such as circulating (e.g., blood, serum or plasma level) or tissue (e.g., lung) hGIIA levels, associated with the viral infection. According to certain examples, the vimentin inhibitor inhibits a catalytic activity and / or a non-catalytic activity of hGIIA. More particularly, the vimentin inhibitor suitably inhibits a non-catalytic activity of hGIIA. In one example, the vimentin inhibitor is a cyclic peptide. For example, the vimentin inhibitor may be a cyclic peptide of the following formula: A1-A2-A3-A4-A5 in which: A1 is F or Y or W or 2NapA; A2 is L or I; A3 is S or T; A4 is F or Y or W or 2NapA; and A5 is R or K. In one example, the peptide inhibitor or cyclic peptide is selected from the group consisting of cFLSYK, cFLSYR and c(2NapA)LS(2NapA)R. When used herein the term “cFLSYK” means “cyclic FLSYK”, “cFLSYR” means “cyclic FLSYR” and “c(2NapA)LS(2NapA)R” means “cyclic (2NapA)LS (2NapA)R”. The terms “2NapA” and “2-Nal” are abbreviations for 2- naphthylalanine. In one example, the peptide inhibitor or cyclic peptide is cyclo-((2-Nal)-Leu- Ser-(2-Nal)-Arg) (FLM-c2). In other examples, the peptide inhibitor or cyclic peptide is a derivative of cyclo-((2-Nal)- Leu-Ser-(2-Nal)-Arg) (FLM-c2). Such a derivative for use according to the present disclosure is suitably a functional FLM-c2 peptide. By “functional FLM-c2 peptide” is meant a peptide able to bind to vimentin, and thereby prevent or inhibit viral binding to a cell. Determining whether a FLM-c2 peptide derivative is functional may be assessed by any method or means known in the art. In various examples, the peptide inhibitor or cyclic peptide provided herein is not cFLSYR. In other examples, the peptide inhibitor or cyclic peptide provided herein is not cFLSYK. As used herein, “derivatives” refers to proteins or peptides, inclusive of fragments or variants thereof, that have been altered, for example by conjugation or complexing with other chemical moieties, such as by post-translational modification (e.g., phosphorylation, acetylation and the like), modification of glycosylation (e.g., adding, removing or altering glycosylation), lipidation and / or inclusion of additional amino acid sequences as would be understood in the art. Derivatives contemplated by the disclosure include, but are not limited to, modification to side chains, incorporation of unnatural amino acids and / or their derivatives during peptide, or protein synthesis and the use of crosslinkers and other methods which impose conformational constraints on the cyclic peptides of the disclosure. In this regard, the skilled person is referred to Chapter 15 of CURRENT PROTOCOLS IN PROTEIN SCIENCE, Eds. Coligan et al. (John Wiley & Sons NY 1995-2008) for more extensive methodology relating to chemical modification of proteins. Further derivatives may include conjugates of the cyclic peptide, such as c2. The term “conjugated” can be used in the context of the present disclosure to describe the cyclic peptide conjugated to another compound or structure, such as a label or carrier molecule or protein. Accordingly, in one example, the cyclic peptide is “conjugated”. The cyclic peptide may be modified via conjugation or complexing with other chemical moieties, such as chemical modification (e.g., cross-linking, acetylation, biotinylation, oxidation or reduction) and / or conjugation with labels (e.g., fluorophores, enzymes, radioactive isotopes) and / or other functional elements (e.g., a half-life extender, a tissue-specific targeting moiety), as are known in the art. In one example, the cyclic peptide derivative may be a pharmaceutically acceptable salt, solvate or prodrug thereof. The cyclic peptide may be utilized per se or in the form of a pharmaceutically acceptable salt, ester, amide, solvate, prodrug, or isomer, as appropriate. For example, it may be provided as a pharmaceutically acceptable salt. If used, a salt of the cyclic peptide should be both pharmacologically and pharmaceutically acceptable, but non-pharmaceutically acceptable salts may conveniently be used to prepare the free active compound or pharmaceutically acceptable salts thereof and are not excluded from the scope of this disclosure. Such pharmacologically and pharmaceutically acceptable salts can be prepared by reaction of the cyclic peptide with an organic or inorganic acid, using standard methods detailed in the literature. The cyclic peptide may be in the form of any pharmaceutically acceptable salt. The term “pharmaceutically acceptable salts” refers to salts prepared from pharmaceutically acceptable non- toxic bases or acids including inorganic or organic bases and inorganic or organic acids. Examples of salts derived from inorganic bases can include aluminium, ammonium, calcium, copper, ferric, ferrous, lithium, magnesium, manganic salts, manganous, potassium, sodium, zinc, and the like. Exemplary salts derived from pharmaceutically acceptable organic non-toxic bases include salts of primary, secondary, and tertiary amines, substituted amines including naturally occurring substituted amines, cyclic amines, and basic ion exchange resins, such as arginine, betaine, caffeine, choline, N,N'-dibenzylethylenediamine, diethylamine, 2-diethylaminoethanol, 2- dimethylaminoethanol, ethanolamine, ethylenediamine, N-ethyl-morpholine, N- ethylpiperidine, glucamine, glucosamine, histidine, hydrabamine, isopropylamine, lysine, methylglucamine, morpholine, piperazine, piperidine, polyamine resins, procaine, purines, theobromine, triethylamine, trimethylamine, tripropylamine, tromethamine, and the like. When the cyclic peptide, such as c2, disclosed herein is basic, acid addition salts may be prepared from pharmaceutically acceptable non-toxic acids, including inorganic and organic acids. Such acids include acetic, benzenesulfonic, benzoic, camphorsulfonic, carboxylic, citric, ethanesulfonic, formic, fumaric, gluconic, glutamic, hydrobromic, hydrochloric, isethionic, lactic, maleic, malic, mandelic, methanesulfonic, malonic, mucic, nitric, pamoic, pantothenic, phosphoric, propionic, succinic, sulfuric, tartaric, p-toluenesulfonic acid, TFA, and the like. Acid addition salts of the cyclic peptide, are prepared in a suitable solvent from the peptide and an excess of an acid, such as hydrochloric, hydrobromic, sulfuric, phosphoric, acetic, TFA, citric, tartaric, maleic, succinic or methanesulfonic acid. In particular examples, the cyclic peptide, or more particularly c2, is in the form of an acetate salt. The cyclic peptide can also exist in solvated forms, including solvates of the free peptide or solvates of a salt of the compound, as well as unsolvated forms. The term “solvate” is used herein to describe a molecular complex comprising the compound of the invention and one or more pharmaceutically acceptable solvent molecules, for example, ethanol. The term “hydrate” is employed when said solvent is water. It is to be understood that all polymorphs, including mixtures of different polymorphs, are included within the scope of the cyclic peptide analogues or derivatives described herein. Esters of the cyclic peptide may be prepared through functionalization of hydroxyl and / or carboxyl groups that may be present within the compound. Amides and prodrugs may also be prepared using techniques known to those skilled in the art. For example, amides may be prepared from esters, using suitable amine reactants, or they may be prepared from an anhydride or an acid chloride by reaction with ammonia or a lower alkyl amine. Moreover, esters and amides of compounds of the invention can be made by reaction with a carbonylating agent (e.g., ethyl formate, acetic anhydride, methoxyacetyl chloride, benzoyl chloride, methyl isocyanate, ethyl chloroformate, methanesulfonyl chloride) and a suitable base (e.g., 4- dimethylaminopyridine, pyridine, triethylamine, potassium carbonate) in a suitable organic solvent (e.g., tetrahydrofuran, acetone, methanol, pyridine, Ν,Ν-dimethylformamide) at a temperature of 0 °C to 60 °C. As used herein, the term “prodrug” means a derivative of a compound that can hydrolyze, oxidize, or otherwise react under biological conditions (in vitro or in vivo) to provide a cyclic peptide described herein. Prodrugs may become active upon such reaction under biological conditions, or they may have activity in their unreacted forms. Examples of prodrugs contemplated for the present disclosure include, but are not limited to, cyclic peptides that comprise biohydrolyzable moieties, such as biohydrolyzable amides, biohydrolyzable esters, biohydrolyzable carbamates, biohydrolyzable carbonates, biohydrolyzable ureides, and biohydrolyzable phosphate analogues. Other examples of prodrugs include derivatives of compounds described herein that comprise —NO, —NO2, —ONO, or —ONO2 moieties. Prodrugs can typically be prepared using well-known methods, such as those described by BURGER'S MEDICINAL CHEMISTRY AND DRUG DISCOVERY (1995) 172-178, 949-982 (Manfred E. Wolff ed., 5th ed). Without wishing to be bound by any theory, the inventors have found previously that FLM- c2 binds to amino acid residues within the amino acid residues numbered 347 to 357, and 342 to 350 which are located on vimentin coil 2. The cyclic peptide or peptide inhibitor may bind to any one or more amino acids within coil 2 as defined herein. The cyclic peptide or peptide inhibitor may bind to residues 347 to 357 of vimentin. The cyclic peptide or peptide inhibitor may bind to residues 342 to 350 of vimentin. The cyclic peptide or peptide inhibitor may bind to any one or more of the following residues on vimentin: M347, N350, F341, V353, E354 or N357. The molecular modelling analysis performed herein has indicated that these residues may directly contact an effective vimentin inhibitor. The cyclic peptide or peptide inhibitor may bind to any one or more of the following residues on vimentin: M347, F341 and E354. The cyclic peptide or peptide inhibitor may at least bind to residues M347, F341 and E354 on vimentin. In the Examples herein, the cyclic peptide FLM-c2 (cyclo-((2-Nal)-Leu-Ser-(2-Nal)-Arg)), shows potent antiviral activity – inhibiting SARS-CoV-2 infection in both in vitro and in vivo models. Without wishing to be bound by theory, it is believed that this anti-viral activity is a result of FLM-c2’s multimodal function; acting as a ‘vimentin blocker’, as well as an autophagy inhibitor and / or an anti-inflammatory agent. Dosage and administration The therapeutically effective dose level for any particular patient or subject, will depend upon a variety of factors familiar to one skilled in the art, including, for example: the viral infection being treated and / or the severity of the infection, the age, body weight, general health, sex and diet of the patient, the time of administration, the route of administration, the duration of the treatment, drugs used in combination or coincidental with the treatment, together with other related factors well known in medicine. It will be understood, however, that the specific dose level and frequency of dosage for any particular patient may be varied and will depend upon a variety of factors including the activity of the specific compound employed, the metabolic stability and length of action of that compound, the age, body weight, general health, gender, diet, mode and time of administration, rate of excretion, drug combination, the severity of the particular condition, a patient's body surface area, whether the patient is undergoing therapy, and any specific contraindications. In one example, the vimentin inhibitor, inclusive of the cyclic peptide or the analogue, variant or derivative thereof described herein, is administered at a dose of about 1.0 mg / kg to about 100 mg / kg (e.g., about 1.0, 1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 2.0, 2.5, 3.0, 3.5, 4.0, 4.5, 5.0, 5.5, 6.0, 6.5, 7.0, 7.5, 8.0, 8.5, 9.0, 9.5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100 mg / kg or any range therein). In one example, the vimentin inhibitor or the cyclic peptide is administered at a dose of 1.4 mg / kg. In another specific example, the vimentin inhibitor or the cyclic peptide is administered at a dose of about 2 mg / kg to about 50 mg / kg. In other examples, the vimentin inhibitor or the cyclic peptide is administered at a dose of about 5 mg / kg to about 25 mg / kg. In further examples, the vimentin inhibitor or the cyclic peptide is administered at a dose of about 10 mg / kg to about 15 mg / kg. In one example, the vimentin inhibitor or the cyclic peptide or the analogue, variant or derivative thereof is administered at a dose of about 1.0 mg / kg / day to about 100 mg / kg / day. In one example, the vimentin inhibitor or the cyclic peptide is formulated for oral administration at a dose of about 1.0 mg / kg / day to about 100 mg / kg / day. In one specific example, the vimentin inhibitor or the cyclic peptide or the analogue, variant or derivative thereof is administered, such as administered orally, at a dose of about 1.4 mg / kg / day. Further, it will be apparent to one of ordinary skill in the art that the optimal quantity and spacing of dosing may depend on the viral infection being treated, the form, route and site of administration, the nature of individual dosages and the particular individual being treated. Also, such optimum conditions can be determined by conventional techniques. In any of the methods disclosed herein, the vimentin inhibitor or the cyclic peptide or the analogue, variant or derivative thereof may be administered daily for a period of at least about 1 day (e.g., about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60 days or any range therein), or at least about 2 days, or at least about 3 days, or at least about 4 days, or at least about 5 days, or at least about 6 days, or at least about 7 days, or at least about 8 days, or at least about 9 days, or at least about 10 days, or at least about 11 days, or at least about 12 days, or at least about 13 days or at least about 2 weeks or any range therein. In one example, the vimentin inhibitor or the cyclic peptide or the analogue, variant or derivative thereof is orally administered daily for a period of at least about 2 weeks. In any of the uses disclosed herein, the medicament or composition may be formulated for oral administration of the vimentin inhibitor or the cyclic peptide or the analogue, variant or derivative thereof for a period of at least about 1 day (e.g., about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180 days or any range therein), or at least about 2 days, or at least about 3 days, or at least about 4 days, or at least 5 days, or at least about 6 days, or at least about 7 days, or at least about 8 days, or at least about 9 days, or at least about 10 days, or at least about 11 days, or at least about 12 days, or at least about 13 days or at least about 2 weeks or any range therein. In one example, the medicament may be formulated for oral administration of the vimentin inhibitor or the cyclic peptide or the analogue, variant or derivative thereof daily for a period of at least about 2 weeks. Those skilled in the art will appreciate that in accordance with the presently disclosed methods and uses, the vimentin inhibitor or cyclic peptide or the compositions disclosed herein may be administered alone or in conjunction with one or more additional agents as part of a combination therapy. For example, the vimentin inhibitor or cyclic peptide or composition disclosed herein may be administered together with one or more additional compounds selected from the group consisting of: an anti-inflammatory agent (e.g., a corticosteroid), an antiviral agent, a bronchial muscle / airway relaxant, oxygen, an antibody, and an antibacterial agent. Any suitable mode of administration, such as oral, rectal, parenteral, sublingual, buccal, intravenous, intranasal, intra-articular, intra-muscular, intra-dermal, subcutaneous, inhalational, intraocular, intraperitoneal, intracerebroventricular, transdermal and the like, may be used. For example, the vimentin inhibitor or cyclic peptide may be administered orally, intravenously or by inhalation. In one example, the vimentin inhibitor or cyclic peptide is administered orally. In another example, the vimentin inhibitor or cyclic peptide is administered by inhalation. To this end, the vimentin inhibitor or cyclic peptide can be included in a pharmaceutical composition suitable for being aerosolised. Cytokine storm In any of the methods described herein, the disease, disorder or condition associated with a viral infection may be a cytokine storm. The term “cytokine storm” may be used interchangeably with the terms “cytokine cascade” and “hypercytokinemia” and will be understood to refer to a series of cellular events that result in an acute and severe immune reaction that comprises a positive feedback loop between cytokines and immune cells that in turn leads to significantly elevated levels of various cytokines. Cytokines that are induced during cytokine storm can include one or more of the following: IL4, IL2, IL1β, IL12, IL18, IL6, IL8, IL10, TNF-α, IFNγ, CCL2, CCL3, CCL4, CCL5, CXCR9, CXCR10 and CXCR12. Cytokine storm is generally characterized by a clinical presentation of overwhelming systemic inflammation, hyperferritinemia, haemodynamic instability and multi-organ failure. Additionally, if left untreated, a cytokine storm can be fatal. The trigger for cytokine storm is an uncontrolled immune response resulting in continuous activation and expansion of immune cells, lymphocytes, and macrophages, which produce significant amounts of cytokines, resulting in a cytokine storm. The cytokine storm described herein may be associated with a viral infection. By way of example, the cytokine storm may result from infection by a virus, such as a human coronavirus (e.g., COVID-19 or SARS-CoV2, SARS-CoV1 and MERS-CoV). In certain examples, the subject has or is at risk of developing a severe reaction to the infection, which may include cytokine storm, sepsis, septic shock, multiple organ dysfunction syndrome (MODS), and / or toxic shock syndrome. Methods of screening In light of the present disclosure, the person skilled in the art may conduct screening assays to identify, design or produce an agent for use in treating or preventing an infection with a virus. It is envisaged that any method known in the art to assess vimentin binding and / or activity, such as those described herein, may be utilised for the present method. In one example, the binding of the inhibitor or agent to vimentin may be assessed through an enzyme immunoassay. In other examples, the level of binding of vimentin to hGIIA and / or a level of hGIIA concentration and / or activity may be assessed. The binding of the viral surface protein of the virus to the host cell receptor in the present of the inhibitor or agent to vimentin may also be assessed by methods known in the art. The effect of the presence of the candidate agents on viral replication or viral activity may also be assessed. This may be achieved, for example, through determining the level of viral plaque formation or cytopathic effect in virally infected cells suitable for the virus being tested (e.g., Vero cells, MDCK cells, Hep2 cells, LLC cells) or viral replication in infected mice. In another example, the effect of the presence of the candidate agents on inflammation may also be assessed. This may be achieved, for example, by determining the level of expression and / or activity of one or more markers of inflammation (e.g., a prostaglandin, cytokine, or any other known marker of inflammation, such as hGIIA). Thus, the present disclosure provides methods to identify, design or produce an agent for use in treating or preventing an infection with a virus when administered to a cell, tissue, or subject. Such methods may be carried out in vivo, for example in animal subjects; or using in vitro and / or ex vivo assays, such as described herein. For example, disclosed herein is a method of identifying, designing or producing an agent for use in treating or preventing an infection with a virus, said method including the steps of: (a) contacting a cell with the virus and a candidate agent, wherein the candidate agent is a cyclic peptide; (b) determining whether the candidate agent inhibits binding of the virus to the cell. In one example, the cell is simultaneously contacted with the virus and the candidate agent. In another example, the cell is contacted with the candidate agent before contacting with the virus. In another example, the cell is contacted with the virus before being contacted with the candidate agent. In particular examples, step (b) includes determining whether the candidate agent inhibits the binding or interaction of vimentin on the host cell to a viral surface protein of the virus. In one example, step (b) includes determining whether the candidate agent inhibits a direct physical association between vimentin and the viral surface protein. The viral surface protein may be a S-glycoprotein. In various examples, step (b) includes determining whether the candidate agent inhibits an interaction between a receptor on the cell, such as an ACE2 receptor, and the viral surface protein. In one example, the candidate agent may be a derivative or variant of cyclo-((2-Nal)-Leu- Ser-(2-Nal)-Arg), such as those derivatives and variants described herein. In one example, the methods disclosed herein may further include the step of isolating and / or purifying an agent that inhibits the binding of vimentin to the viral surface protein. In one particular example, the method further includes the step of formulating the isolated and / or purified agent into a pharmaceutically acceptable formulation. It is also contemplated that the candidate agent or inhibitor may be rationally designed or engineered de novo based on desired or predicted structural characteristics or features that indicate the candidate agent could block or inhibit binding of vimentin to a viral surface protein. In other examples, the candidate agent may be identified by screening a library of molecules without initial selection based on desired or predicted structural characteristics or features that indicate the candidate modulator could block or inhibit binding of vimentin to a viral surface protein. Such libraries may comprise randomly generated or directed libraries of proteins or peptides, and more particularly cyclic peptides, libraries of naturally-occurring molecules and / or combinatorial libraries of synthetic organic molecules. Non-limiting examples of techniques applicable to the design and / or screening of candidate agents may employ X-ray crystallography, NMR spectroscopy, computer assisted screening of structural databases, computer-assisted modelling or biochemical or biophysical techniques which detect molecular binding interactions, as are well known in the art. Biophysical and biochemical techniques which identify molecular interactions include competitive radioligand binding assays, co-immunoprecipitation, fluorescence-based assays including fluorescence resonance energy transfer (FRET) binding assays, electrophysiology, analytical ultracentrifugation, label transfer, chemical cross-linking, mass spectroscopy, microcalorimetry, surface plasmon resonance and optical biosensor-based methods, such as provided in Chapter 20 of CURRENT PROTOCOLS IN PROTEIN SCIENCE Eds. Coligan ei l., (John Wiley & Sons, 1997) Biochemical techniques such as two-hybrid and phage display screening methods are provided in Chapter 1 of CURRENT PROTOCOLS IN PROTEIN SCIENCE Eds. Coligan et al, (John Wiley & Sons, 1997). Accordingly, an earlier step of the method may include identifying a plurality of candidate agents that are selected according to broad structural and / or functional attributes, such as an ability to bind coil 2 of vimentin. Additionally, the present method may further include one or more of the steps of: selecting a candidate agent that inhibits or blocks binding of vimentin on the host cell to a viral surface protein of the virus; isolating or purifying the candidate agent; formulating the candidate agent into a pharmaceutical formulation; and adding the candidate agent or the pharmaceutical formulation to packaging and / or a container, such as a vial, ampoule, bag, blister pack, bottle, cartridge, injection needle, injection syringe, single dose container, strip of multiple single dose containers, or tube. Compositions Compositions comprising a cyclic peptide that inhibits vimentin activity or a compound that disrupts the vimentin-hGIIA interaction, together with an acceptable carrier or diluent, are useful in the methods disclosed herein. Therapeutic compositions can be prepared by mixing the desired compounds having the appropriate degree of purity with optional pharmaceutically acceptable carriers, excipients, or stabilizers (see, e.g., Remington's Pharmaceutical Sciences, 16th edition, Osol, A. ed. (1980)), in the form of lyophilized formulations, aqueous solutions or aqueous suspensions. Acceptable carriers, excipients, or stabilizers are preferably nontoxic to recipients at the dosages and concentrations employed, and include buffers such as Tris, HEPES, PIPES, phosphate, citrate, and other organic acids; antioxidants including ascorbic acid and methionine; preservatives (such as octadecyldimethylbenzyl ammonium chloride; hexamethonium chloride; benzalkonium chloride, benzethonium chloride; phenol, butyl or benzyl alcohol; alkyl parabens such as methyl or propyl paraben; catechol; resorcinol; cyclohexanol; 3-pentanol; and m-cresol); low molecular weight (less than about 10 residues) polypeptides; proteins, such as serum albumin, gelatin, or immunoglobulins; hydrophilic polymers such as polyvinylpyrrolidone; amino acids such as glycine, glutamine, asparagine, histidine, arginine, or lysine; monosaccharides, disaccharides, and other carbohydrates including glucose, mannose, or dextrins; sugars such as sucrose, mannitol, trehalose or sorbitol; salt-forming counter-ions such as sodium; and / or non- ionic surfactants such as TWEEN™, PLURONICS™ or polyethylene glycol (PEG). Additional examples of such carriers include ion exchangers, alumina, aluminum stearate, lecithin, serum proteins, such as human serum albumin, buffer substances such as glycine, sorbic acid, potassium sorbate, partial glyceride mixtures of saturated vegetable fatty acids, water, salts, or electrolytes such as protamine sulfate, disodium hydrogen phosphate, potassium hydrogen phosphate, sodium chloride, colloidal silica, magnesium trisilicate, polyvinyl pyrrolidone, and cellulose-based substances. Therapeutic compositions to be used for in vivo administration should be sterile. This is readily accomplished by filtration through sterile filtration membranes, prior to or following lyophilization and reconstitution. The composition may be stored in a lyophilized form or in solution if to be administered systemically. If in a lyophilized form, it is typically formulated in combination with other ingredients for reconstitution with an appropriate diluent at the time for use. An example of a liquid formulation is a sterile, clear, colourless unpreserved solution filled in a single-dose vial for subcutaneous injection. Single or multiple administrations of the compositions are administered depending on the dosage and frequency as required and tolerated by the patient. The dosage and frequency will typically vary according to factors specific for each patient depending on the specific therapeutic or prophylactic agents administered, the severity and type of disease or condition, the route of administration, as well as age, body weight, response, and the past medical history of the patient. Suitable regimens can be selected by one skilled in the art by considering such factors and by following, for example, dosages reported in the literature and recommended in the Physician's Desk Reference (56th ed., 2002). Generally, the dose is sufficient to treat or ameliorate symptoms or signs of disease without producing unacceptable toxicity to the patient. EXAMPLES Example 1. Antiviral activity of cyclic peptides In this Example, the inventors sought to determine whether the cyclic peptides had antiviral activity in vivo and in vitro against SARS-CoV-2. Plaque Assay Vero cells were plated (6.25 x 105cells / mL) on a 24-well plate.24 hours later, cells were treated with either DMSO control, cyclic peptides FLM-cF or FLM-c2 (0.1-100 µM), infected with either Wuhan-1, Delta (B.1.617.2) and Omicron (B.1.1.592) variants at 1.46 x 105plaque forming units (PFU) / mL. 1% Methyl cellulose was also added to restrict viral spread through media. Cells were left for 72 hours at 37°C and 5% CO2. After incubation, cells were fixed in 4% PFA and stained with crystal violet, with plaque count determined using the Chemidoc MP (BioRad). Animal Studies For prophylactic administration, C57BL / 6 K18-hACE-expressing transgenic mice were treated intravenously (retroorbital) with either DMSO control (1.4%, n = 4) FLM-c2 at either 1.4 or 14 mg / kg / day (both n=4) once daily commencing two days prior to infection with 105PFU of delta variant via nasal injection. After three days of treatment, animals were sacrificed, lungs and brain were harvested and homogenized in PBS for PFU analysis. For therapeutic administration, the C57BL / 6 K18-hACE-expressing transgenic mouse line was infected with 105PFU of delta variant via nasal injection on Day 1. Treatment commenced 24 hours after infection, After three days of treatment, animals were sacrificed, lungs and brain were harvested and homogenized in PBS for PFU analysis. Results Plaque assays were used as a direct measure of viral pathology to identify a lead compound for therapeutic benefit. Cyclic peptides FLM-cF (cyclo-(Phe-Leu-Ser-Tyr-Arg) and FLM-c2 (0.1- 100 µM), Oxaliplatin and Cisplatin (2 µM), as well as DMSO or H2O control were tested for their antiviral activity. While other treatments showed no or limited effect, FLM-c2 showed potent antiviral activity against all tested variants (Wuhan, Delta and Omicron) with and IC50 of ~60 µM (Fig.1C). FLM-c2’s therapeutic benefit was determined in a previously established animal model for SARS-CoV-213. The Delta variant was chosen due to its larger pathological load in this model. Vehicle control (1.4% DMSO, n = 4) or FLM-c2 (1.4 or 14 mg / kg / day, n = 4) was administered therapeutically (24 hours after infection) via retro-orbital injection for three days (Fig. 2a). Treatment using 1.4 mg / kg / day of FLM-c2 treatment showed significantly reduced PFU in both, with 75 % of animals showing no viral particles in lung tissue (Fig.2b). These data demonstrate the anti-viral activity of c2 in relation to viruses whose infectivity is mediated by vimentin. Example 2. Binding of cyclic peptides to the second coil of Vimentin In this Example, vimentin binding compounds were tested for their ability to inhibit the hGIIA-vimentin interaction using a colorimetric enzyme immunoassay (EIA). Purified vimentin fragments (full length or coil 2) were seeded to a 96 well microplate at 15 μg / mL with a 100 μL / well volume. After an overnight incubation at 4°C, the plate was emptied. Each well was then blocked overnight at 4°C with 200 μL of 1% BSA in PBS. The plate was emptied and washed with PBST (PBS + 0.05% Tween20). hGIIA solution was prepared with and without inhibitors. A working solution of 100 ng / mL of hGIIA in PBS with 0.1% BSA was used to dilute stock solutions of inhibitors prepared in DMSO to final concentrations ranging between 0.01-200 uM. hGIIA working solution with 0.4% DMSO served as a positive control, as the final DMSO concentration in all samples did not exceed 0.4%. PBS with 0.1% BSA serving as negative control. Samples were incubated at room temperature for 30 mins. A 100 μL volume of each prepared hGIIA- inhibitor mixture was added to wells in triplicate and incubated at 37°C for two hours. The 4A1- AP conjugate was diluted to 1 μg / mL 0.1% BSA in PBS. Plates were then emptied and washed twice with PBST (200 μL / well), then the prepared 4A1-AP conjugate was added (100 μL / well) and incubated for one hour at 37°C. The AP substrate p-nitro-phenyl phosphate (PNPP) powder was reconstituted in carbonate buffer (8 mM Na2CO3, 36 mM NaHCO3, 2 mM MgCl2, pH 9.8) to a 1 mg / mL concentration. After incubation with 4A1-AP conjugate, plates were then emptied and washed three times with 200 μL / well volume of PBST, followed by washing twice with carbonate buffer, also at 200 μL / well volume. The prepared PNPP solution was added (100 μL / well) and the plates were wrapped in aluminium foil to protect from light and incubated at 37°C for 60 mins. The absorbance was read at 405 nm by a Victor X4 plate reader. Molecular Modelling Studies The crystal structure of vimentin coil 2 dimer was used (PDB 1gk4; Strelkov, S. et al, (2002) Conserved Segments 1A and 2B of the Intermediate Filament Dimer: Their Atomic Structures and Role in Filament Assembly. EMBO J 21: 1255 ) was used as the target in the modelling study. FLM-c2 molecule was docked to the crystal structure of vimentin dimer using software quCBit (www.medchemsoft.com) and the predicted binding structure of FLM-c2 to vimentin dimer is shown in Figure 3A. Results Vimentin has been observed as a co-receptor for SARS-CoV-2, mediating ACE2 binding and internalisation of the virus6-9. Previous findings have identified that SARS-CoV-2 has a specific affinity for vimentin near its C-terminus7. The inventors have previously shown that the secreted protein hGIIA binds to vimentin, specifically to coil 2 of vimentin (Vimentin inhibitors PCT / AU2021 / 050791). Here, the inventors show through molecular modelling that FLM-c2 binds to this same region of vimentin as hGIIA (Fig.3a). In vitro enzyme immunoassay shows FLM-c2 completely inhibits hGIIA binding to coil 2 vimentin, with an IC50 of 56.5 µM (Fig.3b). Vimentin inhibitor Withaferin A and hGIIA inhibitor LY311727 had no effect on interaction (Fig. 3b). Vimentin is detected on the surface of Vero cells, and FLM-c2 treatment reduces the SARS-COV- 2 signal detected (Fig.3C). Example 3. Vimentin inhibitors inhibit endocytosis and autophagy hGIIA vesicle tracking PC-3, cells were seeded in a 24-well glass-bottom senso plate (Greiner Bio-One) at 50,000 cells / well and incubated overnight. Cells were then incubated with 200 ng / mL hGIIA / AF647 and with and without inhibitor FLM-c2 at 50 μM and 100 μM for 24 hours. Cells were live imaged at 37 °C and 5% CO2 using a LSM 800 (Zeiss) using both EC-Plan Neofluar 20x / 0.5 M27 air immersion and Plan-apochromat 63x / 1.40 oil M27 objectives at a frame rate of 633 ms. hGIIA movement was imaged over 3 min and analysed using Imaris 8.2.0 (Bitplane) using the spot creation wizard. Briefly, average hGIIA punctate diameter was measured at 0.8 μm, which was used along with fluorescent intensity to calibrate spot creation for each hGIIA punctate. Vesicle speed, total displacement and vesicle size were measured and exported to Prism 8 (GraphPad, San Diego, CA) for presentation and statistical analysis. Results High levels of FLM-c2 (50-100 µM) also resulted in significantly reduced intracellular trafficking of sequestered hGIIA (Fig. 4A), resulting in stagnant and enlarged endosomes compared to DMSO control(Fig.4B and 4C). Another FLM-C2 prominent mechanism of action is its autophagy regulation. It has been demonstrated that phosphorylated vimentin interacts with signalling molecules such as 14-3-3, beclin 1, Akt1, involving cellular functions such as autophagy and cell migration14. Vimentin is involved in trafficking, localization and size of vesicles – which is targeted by FLM-c2. In prostate cancer cells, FLM-c2 potently inhibits endosomal trafficking (Fig.4A) resulting in enlarged and stagnant vesicles (Fig. 4B, 4C). These findings indicate that FLM-c2 inhibits autophagic flux, critical for viral replication. This mechanism of action is similar to that of thapsigargin, which is documented to have a potent antiviral effect15. However, FLM-c2 is less toxic while still having a powerful antiviral effect. Example 4. Vimentin inhibitors reduce serum hGIIA concentration in humans In this Example, the inventors determine whether FLM-c2 reduces serum hGIIA levels. Administration of FLM-c2 to humans and hGIIA plasma concentration measurement The clinical trial PLA001 was undertaken with approval from the Liverpool Hospital Human Ethics Committee (HREC / 16 / LPOOL / 102). As part of this trial nine men were treated with 10 mg FLM-c2 in capsule form once daily for six weeks. Blood samples were taken at baseline (Day 1) and at the end of study (Day 43). hGIIA levels in plasma were determined by enzyme immunosorbent assay (Cayman Chemicals, Ann Arbor M, product number 501380). Results FLM-c2 is an orally-active inhibitor of prostate tumour growth in xenograft models of prostate cancer. To determine the oral bioavailability and tolerability of FLM-c2 in humans, the compound was administered to humans in a first in man clinical trial PLA001, conducted at Liverpool Hospital Sydney (HREC / 16 / LPOOL / 102). In this trial, nine men, with advanced prostate cancer were administered FLM-c2 orally by capsule at 10 mg daily for six weeks. Serum was collected prior to administration and at the end of the study (Day 43). As shown in Figure 5. FLM-c2 administration resulted in a reduction in plasma hGIIA concentration in six of nine patients. In addition to FLM-c2’s multi-modal antiviral activity presented here, FLM-c2 was originally developed as an inhibitor of hGIIA – an amplifier of inflammation. hGIIA is also over- expressed in human airway epithelium and macrophages during COVID-19, leading to an increase in proinflammatory factors or cytokine storm16. Recently, hGIIA expression was identified as the key biomarker of COVID-19 mortality17. In contrast to corticosteroid regulators (such as dexamethasone), which is immunosuppressive, FLM-c2 functions by inhibiting hGIIA’s pathologic catalysis-independent activity and decreases serum hGIIA levels in men with advanced prostate cancer (Figure 5). Due to FLM-c2 dual function as both as an antiviral and anti- inflammatory, FLM-c2 presents distinct advantages over current therapeutics. FLM-c2 is a cyclic pentapeptide derived from the primary amino acid sequence of the proinflammatory enzyme human Group IIA secreted phospholipase A2 (sPLA2-IIA, Group IIA sPLA2, hGIIA)18-20. FLM-c2 has previously been reported as an anti-inflammatory18-20, reducing production of the eicosanoid prostaglandin E2 in synovial cells of patients with arthritis. Serum hGIIA has recently been reported as a key determinant of COVID-19 mortality. In combination with Blood Urea Nitrogen the serum level of hGIIA is predictive of disease severity and death from COVID-1917. This Example highlights FLM-c2’s usefulness as a therapeutic agent during all stages of COVID-19 pathology. Furthermore, its host-directed mechanism of action and effectiveness against SARS-CoV-2 indicates its antiviral activity may extend to other viral infections particularly those mediated by vimentin. Example 5. Investigating the inhibitory efficiency of the C2 drug against influenza Materials & Methods MDCK cells were seeded at 5000-10,000 cells / well overnight before pretreating cells with either DMSO or c2 (final concentration of DMSO maintained at 0.1%) at different doses for 24h. On the day of infection, the media was replaced before infecting cells with varying doses of a H3N2 influenza strain (0.0001-0.01 MOI) in the presence of c2 at the required concentration. After 3-4 days, media was removed and fixed in crystal violet / methanol and counted plaques. The % virus inhibition is calculated relative to control (DMSO + virus). Results As demonstrated in Figure 6, 10 µM c2 significantly reduced the cytopathic effect of the H3N2 influenza virus on MDCK cells. This inhibitory effect of 10 µM c2 was also evident against multiple viral doses. Example 6. Investigating the inhibitory efficiency of the C2 drug against RSV Materials & Methods Hep2 cells were seeded at 5000-10,000 cells / well overnight before pretreating cells with either DMSO or c2 (final concentration of DMSO maintained at 0.1%) at different doses for 24h. On the day of infection, the media was replaced before infecting cells with varying doses of an RSV 4 clinical isolate (0.0001-0.01 MOI) in the presence of c2 at the required concentration. After 3-4 days, media was removed and fixed in crystal violet / methanol and counted plaques. The % virus inhibition is calculated relative to control (DMSO + virus). Results As demonstrated in Figure 7, c2 significantly reduced the cytopathic effect of the RSV virus on Hep2 cells. This inhibitory effect of c2 was observed across a range of drug doses. It will be appreciated by persons skilled in the art that numerous variations and / or modifications may be made to the above-described embodiments, without departing from the broad general scope of the present disclosure. The present embodiments are, therefore, to be considered in all respects as illustrative and not restrictive.

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New England Journal of Medicine, 386(16), pp.1532-1546. 5. Montazersaheb, S., Hosseiniyan Khatibi, S.M., Hejazi, M.S. et al. COVID-19 infection: an overview on cytokine storm and related interventions. Virol J 19, 92 (2022). https: / / doi.org / 10.1186 / s12985-022-01814-1 6. Hoffmann, M., Kleine-Weber, H., Schroeder, S., Krüger, N., Herrler, T., Erichsen, S., Schiergens, T.S., Herrler, G., Wu, N.H., Nitsche, A. and Müller, M.A., 2020. SARS-CoV- 2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. cell, 181(2), pp.271-280. 7. Suprewicz, Ł., Swoger, M., Gupta, S., Piktel, E., Byfield, F.J., Iwamoto, D.V., Germann, D.A., Reszeć, J., Marcińczyk, N., Janmey, P. and Schwarz, J.M., 2021. Vimentin binds to SARS-CoV-2 spike protein and antibodies targeting extracellular vimentin block in vitro uptake of SARS-CoV-2 virus-like particles. BioRxiv. 8. Suprewicz, Ł., Swoger, M., Gupta, S., Piktel, E., Byfield, F.J., Iwamoto, D.V., Germann, D., Reszeć, J., Marcińczyk, N., Carroll, R.J. and Janmey, P.A., 2022. Extracellular Vimentin as a Target Against SARS‐CoV‐2 Host Cell Invasion. Small, 18(6), p.2105640. 9. Amraei, R., Xia, C., Olejnik, J., White, M.R., Napoleon, M.A., Lotfollahzadeh, S., Hauser, B.M., Schmidt, A.G., Chitalia, V., Mühlberger, E. and Costello, C.E., 2022. Extracellular vimentin is an attachment factor that facilitates SARS-CoV-2 entry into human endothelial cells. Proceedings of the National Academy of Sciences, 119(6), p.e2113874119. 10. Lalioti, V., González-Sanz, S., Lois-Bermejo, I., González-Jiménez, P., Viedma-Poyatos, Á., Merino, A., Pajares, M.A. and Pérez-Sala, D., 2022. Cell surface detection of vimentin, ACE2 and SARS-CoV-2 Spike proteins reveals selective colocalization at primary cilia. Scientificreports, 12(1), pp.1-19. 11. 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Claims

CLAIMS:

1. A method of treating or preventing a viral infection or a disease, disorder or condition associated therewith in a subject, said method including the step of administering a therapeutically effective amount of a vimentin inhibitor to the subject to thereby treat or prevent the viral infection, wherein the vimentin inhibitor is a cyclic peptide that inhibits or prevents binding of virus to a host cell of the subject.

2. The method of claim 1, wherein the viral infection is selected from the group consisting of a coronavirus infection, an influenza virus infection and a respiratory syncytial virus (RSV) infection.

3. The method of claim 1 or claim 2, wherein the viral infection is a coronavirus infection.

4. The method of claim 3, wherein the coronavirus infection is a SARS-CoV-2 infection.

5. The method of claim 4, wherein the SARS-CoV-2 is selected from the group consisting of a Wuhan strain, a Delta strain and an Omicron strain.

6. The method of any one of claims 1 to 5, wherein the vimentin inhibitor inhibits or prevents formation of a complex between a viral surface protein and a receptor on the host cell.

7. The method of claim 6, wherein the viral surface protein is an S-glycoprotein.

8. The method of claim 6 or claim 7, wherein the receptor is the angiotensin converting enzyme-2 (ACE-2) receptor.

9. The method of any one of claims 1-8, wherein the cyclic peptide is cyclo-((2-Nal)-Leu-Ser- (2-Nal)-Arg) or a derivative thereof.

10. The method of any one of claims 1-9, wherein the cyclic peptide is administered at a dose of 1.4 mg / kg.

11. The method of any one of claims 1 to 10, wherein the cyclic peptide is administered orally or by inhalation.

12. The method of any one of claims 1 to 11, wherein the subject is receiving a further treatment for the viral infection.

13. The method of any one of claims 1 to 11, including the further step of administering a further treatment for the viral infection to the subject.

14. The method of claim 12 or claim 13, wherein the further treatment is or comprises a further treatment for a SARS-CoV-2 infection.

15. The method of claim 14, wherein the further treatment is selected from the group consisting of an anti-inflammatory agent, an antiviral agent, a bronchial muscle / airway relaxant, oxygen, an antibody, and an antibacterial agent.

16. The method of claim 15, wherein the antiviral agent is one or more of remdesivir, kaletra, lopinavir, molnupiravir, nirmaterlvir and ritonavir.

17. The method of claim 15, wherein the antibody is sarilumab or tocilizumab.

18. The method of any one of claims 1 to 17, wherein the vimentin inhibitor inhibits or prevents autophagy of the host cell.

19. The method of any one of claims 1 to 18, wherein the vimentin inhibitor inhibits or prevents an inflammatory response associated with the viral infection.

20. A method of reducing the infectivity of a virus, said method including the step of contacting the virus with a cyclic peptide that is a vimentin inhibitor to thereby reduce the infectivity of the virus.

21. The method of claim 20, wherein the cyclic peptide is cyclo-((2-Nal)-Leu-Ser-(2-Nal)-Arg) or a derivative thereof.

22. The method of claim 20 or claim 21, wherein the virus is a SARS-CoV-2 virus.

23. A method of identifying, designing or producing an agent for use in treating or preventing an infection with a virus, said method including the steps of: (a) contacting a cell with the virus and a candidate agent, wherein the candidate agent is a cyclic peptide; (b) determining whether the candidate agent inhibits the binding of vimentin on the host cell to a viral surface protein of the virus.

24. The method of claim 23, wherein step (b) includes determining whether the candidate agent inhibits a direct physical association between vimentin and the viral surface protein.

25. The method of claim 23 or claim 24, wherein the viral surface protein is a S-glycoprotein.

26. The method of any one of claims 23 to 25, wherein the candidate agent is a derivative of cyclo-((2-Nal)-Leu-Ser-(2-Nal)-Arg).

27. The method of any one of claims 23 to 26, further including the step of isolating and / or purifying an agent that inhibits the binding of vimentin to the viral surface protein.

28. The method of claim 27, further including the step of formulating the isolated and / or purified agent into a pharmaceutically acceptable formulation.

29. The method of claim 28, further including the step of sterilising the formulation.

30. The method of claim 28 or claim 29, further including the step of filling the formulation into a container.

31. The method of claim 30, wherein the container is any one or more of a vial, an ampoule, a bag, a blister pack, a bottle, a cartridge, an injection needle, an injection syringe, a single dose container, a strip of multiple single dose containers, or a tube.

32. An agent for use in treating or preventing an infection with a virus, obtained by the method of any one of claims 23 to 31.

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