Compositions and methods relating to antiviral therapeutics

Abstract

Disclosed herein are formulations for use in enhancing the transduction efficiency of lentiviral vector (LV) particles against different target cells. For example, described herein are formulations for use in enhancing transduction of a paramyxovirus pseudotyped lentivirus vector particle into a target cell that may include a cell penetrating peptide (CPP) comprising at least one of: vectofusion-1 or LAH4-C; and a poloxamer 407, wherein a concentration of the poloxamer 407 is in greater than the concentration of the CPP. Also described herein are methods of using these formulations to enhance transduction of LV particles, including in particular in vivo transduction.

Description

[0001]Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 COMPOSITIONS AND METHODS RELATING TO ANTIVIRAL THERAPEUTICS RELATED APPLICATION INFORMATION This patent claims priority to U.S. provisional patent application no.63 / 548,440 filed on November 14, 2023, herein incorporated by reference in its entirety. STATEMENT OFGOVERNMENTFUNDINGThis invention was made with government support under Grant No. AI180822 awarded by the National Institutes of Health. The government has certain rights in the invention. SEQUENCE LISTING STATEMENT The contents of the electronic sequence listing titled UNC2_42478_601_SequenceListing.xml (Size: 2,865 bytes; and Date of Creation: November 14, 2024) is herein incorporated by reference in its entirety. TECHNICALFIELDThe present disclosure relates to formulations for use in enhancing the transduction efficiency of lentiviral vector particles against target cells. BACKGROUND B Cells occupy a unique niche in humoral immunity: they are involved in production of antibodies (Ab) critical to effective humoral immunity, secretion of molecules for autocrine and paracrine signaling, and antigen presentation (Cyster, J., Cell, 18:177(3):524-540 (2019)). Furthermore, B cells can differentiate into long lived plasma cells, capable of surviving and producing large quantities of Ab continuously for decades (Yu et al., Nature, 455(7212)-2478-2492 (2008)). Engineered B cells that can take advantage of these unique immune functions offer substantial promise for a wide array of therapeutic applications (Levy et al., Thromb. Haemost., 14(12):2478-2492 (2016); Kwakkenbos et al., Nat. Med., 16(1):123-128 (2010); Pesch et al., Front. Immunol., 10:2630 (2019); Wang et al., Mol. Ther. Methods Clin. Dev., 5:76-82 (2017); Edelstein et al., Biochem. Pharmacol., 206:115285 (2022)). Chimeric antigen receptors (CARs) are synthetic receptors that bind specific tumor antigens; the expression of CAR on T-cells results in CAR-T cells that can kill cancer cells. Current CAR-T involves collecting patients’ own T-cells, modifying them to express CAR, Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 and expanding the engineered cells to quantities adequate for reinfusion back into patients. Despite considerable promise, CAR-T is currently limited by a few shortcomings, including time and costs of CAR-T production ex vivo, and overall poor efficacy against solid cancers, including lung cancer. The two factors are related: manipulation and expansion of T-cells outside the body directly reduces the expansion capacity T-cells after reinfusion in patient. Current methods for manufacturing engineered immune cells such as B cells and T cells ex vivo are exceptionally expensive: clinically approved CAR-T therapies currently cost ~$400,000 to manufacture, with infusion and monitoring costing another ~$80,000 (Choi et al., Int. J. Environ. Res. Public Health, 19:19 (2022)). B cells are also notoriously difficult to culture and expand ex vivo (Su et al., J. Immunol., 197(10):4163-4176 (2016)). Further, B cells are difficult to target and transduce by conventionally pseudotyped lentiviral (LV) vectors including VSV-G (Frank et al., Mol. Ther. Methods Clin. Dev., 12:19-31 (2019)), due in part to very low levels of low density lipoprotein receptor compared to T cells even when activated (Amirache et al., Blood, 123(9):1422-1424 (2014)). In addition, endocytosis occurs minimally in B cells unless through the B Cell Receptor Frank et al., Mol. Ther. Methods Clin. Dev., 12:19-31 (2019); McShane et al., Front. Immunol., 13:892169 (2022)), making them incompatible with LVs that deliver cargo DNA into cells through an endocytic escape mechanism. Given these shortcomings associated with VSV-G pseudotyped LVs, paramyxovirus pseudotyped LVs appear to be better suited for transducing B cells. Paramyxoviruses deliver its cargo DNA into cells through a direct membrane fusion mechanism, using distinct glycoproteins for attachment and for membrane fusion (Carneiro V., Molecular Mechanisms of Measles Virus Entry and Exit, 2016). The specificity of paramyxovirus pseudotyped lentivirus can be further enhanced by introducing mutations that ablate the native tropism of the attachment protein, followed by incorporation of a targeting moiety - such as a single chain fragment variable (ScFv) specific to receptors on target cells (Frank et al., Mol. Ther. Methods Clin. Dev., 12:19-31 (2019); Bender et al., PLoS Pathog., 12(6):e1005641 (2016); Funke et al., Mol. Ther., 16(8):1427-1436 (2008); Buchholz et al., Trends Biotechnol., 27(5):259-265 (2009)). Despite these rational improvements, paramyxovirus-based LVs remain generally unable to mediate efficient transduction in vivo. Therefore, a need exists to mediate efficient transduction of lentiviral vectors in vivo. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 SUMMARY Embodiments of the present disclosure include a formulation for use in enhancing the transduction of a lentiviral vector particle into a target cell, the formulation comprising at least one cell penetrating peptide (CPP); and at least one of: (i) a HDAC inhibitor; (ii) a Blimp1 pathway blocker; or (iii) a surfactant, wherein the surfactant is a natural surfactant or a poloxamer. In some embodiments, the formulation further comprises at one mammalian target of rapamycin (mTOR) inhibitor. In some embodiments, the CPP is vectofusion-1, LAH4, LEPTIN30, APOE or any combinations thereof. In some embodiments, the CPP is vectofusion-1. In some embodiments, the HDAC inhibitor is valproic acid, trichostatin A, suberuylanilide hydroxamic acid, PXD101, oxamflatin, LAW824, LBH589, pyroxamide, SK- 7041, SK-7068, tubacin, MS-275 depsipeptide, trapoxin A, apicidin, CHAPs, or any combinations thereof. In some embodiments, wherein the HDAC inhibitor is valproic acid. In some embodiments, the Blimp1 pathway blocker is a Blimp1 siRNA or a Blimp1 shRNA. In some embodiments, the surfactant is a natural surfactant. In some embodiments, the natural surfactant is derived from a mammal, plant, microorganism or any combinations thereof. In some embodiments, the surfactant is a poloxamer. In some embodiments, the poloxamer is poloxamer 407. In some embodiments, the formulation comprises (a) a CPP and a HDAC inhibitor; (b) a CPP and a Blimp1 pathway blocker; (c) a CPP and a surfactant, wherein the surfactant is a natural surfactant or a poloxamer; (d) a CPP, a HDAC inhibitor and a Blimp1 pathway blocker; (e) a CPP, a HDAC inhibitor and a surfactant, wherein the surfactant is a natural surfactant or a poloxamer; (f) a CPP, a Blimp1 pathway blocker and a surfactant, wherein the surfactant is a natural surfactant or a poloxamer; (g) a CPP and a mTOR inhibitor; (h) a CPP a HDAC inhibitor, and a mTOR inhibitor; (i) a CPP, a Blimp1 pathway blocker, and a mTOR inhibitor; (j) a CPP, a surfactant, and a mTOR inhibitor, wherein the surfactant is a natural surfactant or a poloxamer; (k) a CPP, a HDAC inhibitor, a Blimp1 pathway blocker, and a mTOR inhibitor; (l) a CPP, a HDAC inhibitor, a surfactant and a mTOR inhibitor, wherein Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 the surfactant is a natural surfactant or a poloxamer; (m) a CPP, a Blimp1 pathway blocker, and a surfactant, wherein the surfactant is a natural surfactant or a poloxamer; or (n), a CPP, a HDAC inhibitor, a Blimp1 pathway blocker, a surfactant, a mTOR inhibitor, wherein the surfactant is a natural surfactant or a poloxamer. In some embodiments, the mTOR inhibitor is rapamycin. Embodiments of the present disclosure also include a method for transducing a target cell with a lentiviral vector particle, the method comprising the step of: transducing a target cell with a lentiviral vector particle containing one or more genes of interest and formulation for use in enhancing the transduction of a lentiviral vector particle into a target cell. In some embodiments, the method is performed in vivo in a subject. Any of these methods and compositions may be used or configured for use in transducing target cells in blood isolated from a patient (e.g., at bedside) for rapid re-infusion back into a patient. Thus the transducing agent may be combined with the blood ex vivo and the treated blood may be re-introduced to the patient. In some cases the blood may be reintroduced after treating (e.g., by a dialysis technique) to remove the transduction enhancer and / or excess virus, or the like. In some cases the blood including the transduction enhancer may be reintroduced into the patient. Thus, any of the method described herein may include ex vivo engineering followed by reinfusion into a subject. In some embodiments, the lentiviral vector particle is a pseudotyped lentiviral vector particle. In some embodiments, the method further comprises transducing the target cell with the lentiviral vector particle followed by transducing the target cell with the formulation after the transduction with the lentiviral vector particle. In some embodiments, the method further comprises transducing the target cell with the formulation followed by transducing the target cell with the lentiviral vector particle after the transduction with the formulation. In some embodiments, the target cell is a B-cell. In some embodiments, the pseudotyped lentiviral vector particle contains one or more glycoproteins from one or more of: a Nipah virus, a Hendra virus, a measles virus, a Tupaia paramyxovirus, a Newcastle disease virus, a parainfluenza virus, a Sendai virus, a Baboon endogenous retrovirus, RD114 feline endogenous virus, primate type D retroviruses, a Gibbon-ape leukemia virus, a murine stem cell virus, a MERS virus, or any combinations thereof. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 In some embodiments, the pseudotyped lentiviral vector particle contains a glycoprotein from a Nipah virus. In some embodiments, the glycoprotein from the Nipah virus contains one or more mutations, deletions, substitutions or combinations thereof. For example, described herein are formulations for use in enhancing transduction of a paramyxovirus pseudotyped lentivirus vector particle into a target cell (including specifically formulations for use in in vivo transduction of , the formulation comprising a cell penetrating peptide (CPP) comprising at least one of: vectofusion-1 or LAH4-C; and a poloxamer 407, wherein a the poloxamer 407 has a concentration that is greater than 5 times (e.g., 5-fold) the concentration of the CPP. In some cases the CPP may include just vectorfusion-1. In some cases the CPP may include just LAH4-C. In any of these examples the formulation may exclude LAH4-A (e.g., may have less than 1% LAH4-A, less than 0.1%, less than 0.01%, etc.). Any of these formulations may include the virus particle (e.g., the paramyxovirus pseudotyped lentivirus vector particle). In general, the concentration of poloxamer 407 may be greater than the concentration of the CPP (e.g., greater than 1.5x, greater than 2x, greater than 3x, greater than 4x, greater than 5x, greater than 10x, etc.). For example, the concentration of the poloxamer 407 may be greater than 10-fold to the concentration of the CPP. Also described herein are methods of using these TEs. For example, described herein are methods of enhancing transduction of a paramyxovirus pseudotyped lentivirus vector particle into a target cell, the method comprising: transducing the target cell with the paramyxovirus pseudotyped lentivirus vector particle containing one or more genes of interest and a formulation comprising a poloxamer 407 and a cell penetrating peptide (CPP) comprising at least one of: vectofusion-1 or LAH4-C, wherein a concentration of the poloxamer 407 is in greater than 5-fold a concentration of the CPP. Transducing the target cell may comprise transducing in vivo within a subject. The paramyxovirus pseudotyped lentivirus vector particle may comprise one or more glycoproteins from a Nipah-paramyxovirus-based lentivirus vector particle (e.g., F and / or G proteins). The target cell may be a B cell. In some cases the target cell is a T cell. The paramyxovirus pseudotyped lentivirus vector particle may contain one or more glycoproteins from one or more of: a Nipah virus, a Hendra virus, a measles virus, a Tupaia paramyxovirus, a Newcastle disease virus, a parainfluenza virus, a Sendai virus, a Baboon endogenous retrovirus, RD114 feline endogenous virus, primate type D retroviruses, a Gibbon-ape leukemia virus, a murine stem cell virus, a MERS virus, or any combinations thereof. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 The CPP may comprise vectorfusion-1. In some cases the CPP comprises LAH4- (and less than about 1% of LAH4-A, etc.). The concentration of the poloxamer 407 may be greater than 10-fold to the concentration of the CPP. For example, a formulation for use in enhancing transduction of a paramyxovirus pseudotyped lentivirus vector particle into a target cell may include: a cell penetrating peptide (CPP) comprising vectofusion-1; and a poloxamer 407, wherein a concentration of the poloxamer 407 is in greater than 5-fold a concentration of the CPP. The concentration of the poloxamer 407 may be greater than 10-fold (e.g., greater than 20-fold, etc.) of the concentration of the CPP. A method of enhancing transduction of a paramyxovirus pseudotyped lentivirus vector particle into a target T cell or B cell, the method comprising: transducing the target cell with the paramyxovirus pseudotyped lentivirus vector particle containing one or more genes of interest and a formulation comprising a cell penetrating peptide (CPP) comprising vectofusion-1, and a poloxamer 407, wherein a concentration of the poloxamer 407 is in greater than 5 fold a concentration of the CPP. In general, transducing the target cell may comprise transducing in vivo within a subject. The paramyxovirus pseudotyped lentivirus vector particle may comprise a Nipah-paramyxovirus-based lentivirus vector particle. In any of these methods, the target cell may be a B cell and / or a T cell. The paramyxovirus pseudotyped lentivirus vector particle may contain a glycoprotein from one or more of: a Nipah virus, a Hendra virus, a measles virus, a Tupaia paramyxovirus, a Newcastle disease virus, a parainfluenza virus, a Sendai virus, a Baboon endogenous retrovirus, RD114 feline endogenous virus, primate type D retroviruses, a Gibbon-ape leukemia virus, a murine stem cell virus, a MERS virus, or any combinations thereof. The concentration of the poloxamer 407 may be greater than ten times (e.g., 10-fold) the concentration of the CPP. For example, in any of these methods and compositions, the pseudotyped lentiviral vector particle may contain a glycoprotein from a Nipah virus; in some cases, the pseudotyped lentiviral vector particle may contain a G and / or an F protein from the Nipah virus. The glycoprotein from the Nipah virus may contain one or more mutations, deletions, substitutions or combinations thereof. All of the methods and apparatuses described herein, in any combination, are herein contemplated and can be used to achieve the benefits as described herein. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 BRIEF DESCRIPTION OF THE DRAWINGS FIGS.1A-1G: transduction Enhancer (TE) effects on growth and viability. (A-D) Effect of varying concentrations of the individual transduction enhancers on SA13 cell growth kinetics over 72 hours. (E) Effect of TE groups tested in later experiments on SA13 cell growth kinetics over 72 hours. (F) Effect of TE groups tested in later experiments on SA13 cell viability over 72 hours. (G) TE combinations used in each group number. FIGS.2A-2D: Transduction rates and Mean Fluorescence Intensity (MFI) of TE combinations in SA13 cells and Isolated B cells. (A) MFI of GFP in different groups of TE combinations on SA13 cells using a CD20 targeted LV vector containing a MSCV promoter driven GFP-T2A-RFP transgene. (B) MFI of GFP in different groups of TE combinations on SA13 cells using a CD20 targeted LV vector containing an MSCV promoter driven GFP- T2A-RFP transgene. (C) % of SA13 cells expressing both RFP and GFP in each experimental TE group. (D) % of isolated B cells expressing both RFP and GFP in each experimental TE group. FIGS.3A-3E: Transduction rates and MFI of selected TE combinations in ex vivo Peripheral Blood Mononuclear Cells (PBMCs). For all subfigures, Legend in top left applies. (A) % RFP+ cells of CD20Highcells within the PBMC population based on TE group. (B) % RFP+ cell of CD20lowcells within the PBMC population. Insert graph for better visual analysis and display significance (C) % RFP+ cells of CD20- cells within the PBMC population. Insert graph for better visual analysis. No significance observed. (D) GFP Mean Fluorescence Intensity (MFI) for CD20Highcells within the PBMC population. (E) GFP MFI for CD20lowcells within the PBMC population. (F) GFP MFI for CD20- cells within the PBMC population. FIG.4: On target: Off target Ratio in selected TE groups on ex vivo PBMCs. FIGS.5A-5C: In vivo transduction protocol and results. (A) In vivo protocol: PBMCs injected at -4 hrs (day -1), LVs + TEs injected Day 0, Blood drawn days 3, 7, 14. (B) In vivo transduction rates of CD20+ cells (on target transduction). (C) In vivo transduction rates of CD20- cells (off target transduction). FIG.6: Secretion of anti-RSV ScFv-Fc by NLV+TE reprogrammed B cells in situ. Serum concentration of anti-RSV ScFv-Fc in NSG mice at days 3, 7, 14, and 26. Concentrations were measured by ELISA against JSM-24 strain RSV F protein. Uncorrelated Fisher’s LSD test; * p < 0.05 Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 FIGS 6A-6D: Values from urinalysis of mice used for in vivo experimentation, day 15. (A-C) Examining enzymes associated with liver damage. Higher values hints at damage. dashed lines are upper and lower limits of normal, legend is to right of C. (A) ALT enzyme levels in urine. (B) AST levels in urine. (C) BUN levels in urine. (D) Urine Creatinine levels, a good measure of kidney function and potential kidney toxicity. Dashed lines are upper and lower limits of normal, legend is on right. FIG.7: Current Vaccines vs. “CAR-B” cells. Schematic of the approach to generate well defined protective Ab via chimeric Ab reprogrammed (CAR)-B cells vs. conventional vaccines. Diverse Abs are induced with current vaccines over weeks. In contrast, by reprogramming B cells directly in vivo, only the most potent bnAb of interest (red) will be secreted by B cells. FIG.8: B cell transduction efficiency of CD20-targeting NLVs with TE in non- activated human PBMCs. RFP expression (% CD20+ / RFP+ cells) was measured by flow cytometry 5 days after NLV transduction with different combination of TEs. NLVs were mixed with TE immediately prior to addition to PBMCs at MOI of 10 LV per B-cell. * p<0.01, two-way ANOVA (Bonferroni). Virus-to-cell ratio (i.e. MOI) was estimated based on qPCR. Data represent independent experiments with non-activated PBMCs from 3-5 unique donors. FIGS.9A-9B: CD20-targeted NLV transduction of circulating PBMC in NSG mice, without enhancers (blue) or with enhancers (black). (A) CD20+ B-cells. (B) CD3+ and CD14+ cells. * p < 0.05. FIG.10: Comparison of current “CAR-T” vs. our proposed in vivo “CAR-T”. FIGS.11A-11C: Transduction efficiency of NLV-CD3 LVs with TE in non- activated human PBMCs. GFP expression (both percentage and number of CD3+ / GFP+ cells) was measured by flow cytometry 5 days of transduction with different doses of NLV- CD3 (A, B). ***p=0.0001, ****p<0.0001, two-way ANOVA (Bonferroni). LVs were mixed with P407 and VF-1 prior to addition to the PBMCs. Virus-to-cell ratio (i.e. MOI) was estimated based on qPCR. NLV data (n=9) represent 3 independent experiments using non- activated PBMCs from 3 donors, tested against 3 batches of NLVs made independently. (C) Ratio of GFP+ off-target (CD3-) cells vs. target (CD3+) cells. FIGS.12A-12D: CAR expression efficiency and killing assay in transduced non- activated PBMCs using enhancers. (A) % CD19-CAR+ cells among total CD3+ cells were measured by flow cytometry in PBMCs treated with NLV-CD3 (also listed as NiV) or MLV- CD3 (listed as MV), with and without TE. ***p=0.0001, ****p <0.00001, one-way ANOVA. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 (B) Flow cytometry plots of CD3+ effector cells and CD19+ tumor cells after co-culturing of transduced non-activated PBMCs with BV-173 tumor cells. All conditions were normalized to the same tumor cells to effector cells, calculated based on the total number of non- activated PBMCs (i.e. includes both transduced and non-transduced PBMCs). (C) The percentage of CD19+ tumor B cells remaining after a 4-day co-culturing of non-activated PBMCs and BV-173. Data were collected from 3 independent experiments of PBMCs from 3 unique donors, each tested against 5 different batches of LVs. ****p=0.0001, one-way ANOVA. (D) Viability of T-cells incubated with NLV with different TEs. The TE in this example is P407 and VF-1. FIGS.13A-13F: Characterization of in vivo engineered CAR-T cells. (A-B) CAR+ CD3+ T cells in (A) spleen and (B) bone marrow. (C-D) Off-target transduction was quantified by CAR+ but CD3- cells in (C) blood and (D) spleen. (A-D) Mice receiving different interventions: Black: PBS only; Blue: NLV encoding GFP; Orange: NLV encoding CAR; Green: CAR-encoding NLV+TE. (E-F) The number of CD4+ and CD8+ CAR-T cells in (E) blood as well as (F) spleen. The TE in this example refers to P407 and VF-1. FIGS.14A-14C: Characterization of in vivo engineered CAR-T cells. CAR+ T cells (FIG.14A) CD3+, (FIG.14B) CD4+ and (FIG.14C) CD8+ T cells in blood from the two independent studies shown in Figure 5 were further characterized for memory. FIGS.15A-15E: In vivo engineered CAR-T cells eradicates aggressive BV173 tumor. (A) CD19.CAR-T cells in blood. (B-E) NSG mice inoculated with ffLuc+ BV173 tumor were infused with human PBMCs followed by either PBS (Group 1, FIG.15B), NLV carrying a non-specific transgene (Group 2, FIG.15C), NLV delivering CD19.CAR transgene (Group 3, FIG.15D), and NLV delivering the CD19.CAR transgene formulated using the cocktail of transduction enhancers (Group 4, FIG.15E). Tumor burden on different days is monitored by IVIS imaging. Data represents two independent studies. The TE in this example refers to P407 and VF-1. FIGS.16A-16B: NLV+TE induced B7-H3.CAR T cells among whole PBMCS effectively killed A549 lung carcinoma cells (FIG.16A) and human Panc-1 tumor cells (FIG. 16B) in co-culture study. Cells collected after 5-day co-culturing and stained with anti-CD3 antibody to identify T cells and tumor cells (GFP+) by flow cytometry. Two-way ANOVA with Bonferroni correction. *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001. The TE used in this example is P407 and VF-1, unless indicated otherwise. FIG.17: NLV+TE transduced human T cells kill NSCLC cells in vitro. FFluc- GFP-A549 cells were co-cultured with PBMCs transduced by NLV, NLV+TE, VSV-G, and Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 VSV-G+TE that carry B7H3-CAR. E:T(PBMC: A549)=2:1. Data were collected from 2 donors with 2 different batches of NLV. One-way FIGS.18A-18D: NLV system carrying B7H3.CAR eliminates tumors in NSCLC metastatic model. FIG.18A shows a schematic of a metastatic model in NSG mice using the FFluc-A549 cell line, followed by PBMC infusion and NLV with enhancer treatment. FIG. 18B shows representative images of tumor bioluminescence (BLI) in male (left) and female (right) mice. FIGS.18C and 18D show the kinetics of tumor growth (n = 5 male +4 female mice / group) from the animals of FIG.18A-18B. Animals were rechallenged with 3x106cells on day 24. *P=0.0226; ***p=0.0009, two-way ANOVA with Bonferroni correction. FIG.19B shows a Kaplan–Meier survival curve of the mice (Chi-square test). FIGS.19A and 19B: FIG.19A shows the percentage of CAR-T cells (gated from hCD3+ population) and FIG.19B shows human CD8+ T cells in the blood on day 21 of NLV and NLV+enhancer treatment. △ represents females and □ represents males. FIGS.20A-20D: A T cell line (SUP-T1) based DOE screen strategy to identify optimal TE compositions for CD3-targeted NLV. FIG.20A schematically illustrates screening of 15 TEs that are first screened in SUP-T1 cells utilizing DOE methodology guided by JMP software, followed by focus screening of the top 5 candidates across a range of concentration. FIG.20B is a table showing results from the first DOE screen (encompassing combinations of 3 or 4 TEs per condition), with specific TE sorted based on decreasing levels of average transduction rates (%GFP+ cells) achieved across all conditions containing the particular TE as part of the combination. FIG.20C illustrates results from the second DOE screen, based on combinations of the top 5 TEs identified from the first DOE screen. Given the structural similarity of TE #13 and #14, only TE #13 was advanced into the second screen. Data represents all conditions tested in the DOE screen that involved the particular TE at the specific concentrations tested. FIG.20D shows a JMP analysis of the magnitude of the effect and p-values from the first DOE screen revealed that LAH4, P407, and VF-1 (TE #1, #13, and #4) each exerted appreciable, statistically-significant positive improvement to transduction of SUP-T1 cells. FIG.21: A PBMC-based DOE screen strategy to identify optimal TE cocktail for CD3-targeted NLV. FIG.21A schematically illustrates 15 TEs are first screened in PBMC cells utilizing DOE methodology guided by JMP software, followed by focus screening of the top 5 candidates across a range of concentration. FIG.21B shows results from the first DOE screen (encompassing combinations of 3 or 4 TEs per condition), with specific TE sorted based on decreasing levels of average transduction rates (%GFP+ cells) achieved across all Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 conditions containing the particular TE as part of the combination. FIG.21C shows results from the second DOE screen, based on combinations of the top 5 TEs identified from the first DOE screen. Data represents all conditions tested in the DOE screen that involved the particular TE at the specific concentrations tested. FIG.21D shows a JMP analysis of the magnitude of the effect and p-values from the first DOE screen revealed that P407 and LAH4 (enhancers #13 and #1) each exerted appreciable, statistically-significant positive improvement to transduction of SUP-T1 cells. FIGS.22A-22C: Characterization of NLV transduction of CD3+ T cells in PBMCs at different concentrations of TEs (VF-1 + P407 or LAH4 + P407), with and without metformin (ME). FIG.22A is a graph of the percentage of CD4+ cells, and FIGS.22B is a graph of CD8+ T cells that were transduced in the presence of different concentrations of TE combinations (n=3). FIG.22C is a table showing the conditions tested (corresponding to conditions 1-19). FIG.23A-23B: transduction enhancers promote cytotoxic activity of PBMCs against Daudi cancer cells. FIG.23A is a graph showing data from day 2 after transduction, FIG.23B is a graph showing day 4 after transduction. FIGS.24A-24E: SUP-T1 DOE Screening Experiments. FIG.24A shows raw data- DOE #1 (Transduction), FIG.24B shows raw data- DOE #1 (Toxicity), FIG.24C shows raw data- DOE #2 (Transduction), FIG.24D shows raw data- DOE #2 (Toxicity), and FIG.24E shows DOE#2 JMP Significance Ranking. FIGS.25A-25E: PBMC DOE Screening Experiments. FIG.25A shows raw data- DOE #1 (Transduction), FIG.25B shows raw data- DOE #1 (Toxicity), FIG.25C shows raw data- DOE #2 (Transduction), FIG.25D shows raw data- DOE #2 (Toxicity), and FIG.25E shows DOE#2 JMP Significance Ranking. FIGS.26A-26C: Aggregate T-cell PBMC phenotype and total GFP levels relative to all PBMCs. FIG.26A is a graph showing that enhancers do not significantly alter total CD4+ and FIG.26B is a graph of the total CD8+ levels in PBMCs independent of transduction. FIG.26C is a graph of the percent total transduction in PBMCs independent of cell phenotype (n=3 for all panels). FIG.27 is a bar chart showing the effect of the end region of the LAH4 polypeptide (e.g., LAH4-A and LAH4-C forms) on enhancing transduction of target cells, such as T cells. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 DETAILED DESCRIPTION Section headings as used in this section and the entire disclosure herein are merely for organizational purposes and are not intended to be limiting. Definitions Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art. In case of conflict, the present document, including definitions, will control. Preferred methods and materials are described below, although methods and materials similar or equivalent to those described herein can be used in practice or testing of the present disclosure. All publications, patent applications, patents and other references mentioned herein are incorporated by reference in their entirety. The materials, methods, and examples disclosed herein are illustrative only and not intended to be limiting. Terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting of the invention. For example, as used herein, the singular forms "a", "an" and "the" are intended to include the plural forms as well, unless the context clearly indicates otherwise. It will be further understood that the terms "comprises" and / or "comprising," when used in this specification, specify the presence of stated features, steps, operations, elements, and / or components, but do not preclude the presence or addition of one or more other features, steps, operations, elements, components, and / or groups thereof. As used herein, the term "and / or" includes any and all combinations of one or more of the associated listed items and may be abbreviated as " / ". Spatially relative terms, such as "under", "below", "lower", "over", "upper" and the like, may be used herein for ease of description to describe one element or feature's relationship to another element(s) or feature(s) as illustrated in the figures. It will be understood that the spatially relative terms are intended to encompass different orientations of the device in use or operation in addition to the orientation depicted in the figures. For example, if a device in the figures is inverted, elements described as "under”, or "beneath" other elements or features would then be oriented "over" the other elements or features. Thus, the exemplary term "under" can encompass both an orientation of over and under. The device may be otherwise oriented (rotated 90 degrees or at other orientations) and the spatially relative descriptors used herein interpreted accordingly. Similarly, the terms "upwardly", "downwardly", "vertical", "horizontal" and the like are used herein for the purpose of explanation only unless specifically indicated otherwise. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 Although the terms “first” and “second” may be used herein to describe various features / elements (including steps), these features / elements should not be limited by these terms, unless the context indicates otherwise. These terms may be used to distinguish one feature / element from another feature / element. Thus, a first feature / element discussed below could be termed a second feature / element, and similarly, a second feature / element discussed below could be termed a first feature / element without departing from the teachings of the present invention. In general, any of the apparatuses and methods described herein should be understood to be inclusive, but all or a sub-set of the components and / or steps may alternatively be exclusive and may be expressed as “consisting of” or alternatively “consisting essentially of” the various components, steps, sub-components or sub-steps. As used herein in the specification and claims, including as used in the examples and unless otherwise expressly specified, all numbers may be read as if prefaced by the word "about" or “approximately,” even if the term does not expressly appear. The phrase “about” or “approximately” may be used when describing magnitude and / or position to indicate that the value and / or position described is within a reasonable expected range of values and / or positions. For example, a numeric value may have a value that is + / - 0.1% of the stated value (or range of values), + / - 1% of the stated value (or range of values), + / - 2% of the stated value (or range of values), + / - 5% of the stated value (or range of values), + / - 10% of the stated value (or range of values), etc. Any numerical values given herein should also be understood to include about or approximately that value, unless the context indicates otherwise. For example, if the value "10" is disclosed, then "about 10" is also disclosed. Any numerical range recited herein is intended to include all sub-ranges subsumed therein. It is also understood that when a value is disclosed that "less than or equal to" the value, "greater than or equal to the value" and possible ranges between values are also disclosed, as appropriately understood by the skilled artisan. For example, if the value "X" is disclosed the "less than or equal to X" as well as "greater than or equal to X" (e.g., where X is a numerical value) is also disclosed. It is also understood that the throughout the application, data is provided in a number of different formats, and that this data, represents endpoints and starting points, and ranges for any combination of the data points. For example, if a particular data point “10” and a particular data point “15” are disclosed, it is understood that greater than, greater than or equal to, less than, less than or equal to, and equal to 10 and 15 are considered disclosed as well as between 10 and 15. It is also understood that each unit between two particular units Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 are also disclosed. For example, if 10 and 15 are disclosed, then 11, 12, 13, and 14 are also disclosed. Although various illustrative embodiments are described above, any of a number of changes may be made to various embodiments without departing from the scope of the invention as described by the claims. Optional features of various device and system embodiments may be included in some embodiments and not in others. Therefore, the foregoing description is provided primarily for exemplary purposes and should not be interpreted to limit the scope of the invention as it is set forth in the claims. The examples and illustrations included herein show, by way of illustration and not of limitation, specific embodiments in which the subject matter may be practiced. As mentioned, other embodiments may be utilized and derived there from, such that structural and logical substitutions and changes may be made without departing from the scope of this disclosure. Such embodiments of the inventive subject matter may be referred to herein individually or collectively by the term “invention” merely for convenience and without intending to voluntarily limit the scope of this application to any single invention or inventive concept, if more than one is, in fact, disclosed. Thus, although specific embodiments have been illustrated and described herein, any arrangement calculated to achieve the same purpose may be substituted for the specific embodiments shown. This disclosure is intended to cover any and all adaptations or variations of various embodiments. Combinations of the above embodiments, and other embodiments not specifically described herein, will be apparent to those of skill in the art upon reviewing the above description. The terms “comprise(s),” “include(s),” “having,” “has,” “can,” “contain(s),” and variants thereof, as used herein, are intended to be open-ended transitional phrases, terms, or words that do not preclude the possibility of additional acts or structures. The singular forms “a,” “an” and “the” include plural references unless the context clearly dictates otherwise. The present disclosure also contemplates other embodiments “comprising,” “consisting of” and “consisting essentially of,” the embodiments or elements presented herein, whether explicitly set forth or not. For the recitation of numeric ranges herein, each intervening number there between with the same degree of precision is explicitly contemplated. For example, for the range of 6- 9, the numbers 7 and 8 are contemplated in addition to 6 and 9, and for the range 6.0-7.0, the number 6.0, 6.1, 6.2, 6.3, 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, and 7.0 are explicitly contemplated. The term "administering" means providing a composition (a formulation as described herein), pharmaceutically active agent (e.g., a lentiviral vector particle) or both a Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 composition (e.g., a formulation as described herein) and pharmaceutically active agent (a lentiviral vector particle) to a subject, and includes, but is not limited to, administering by a medical professional and / or self-administration (e.g., the subject receiving treatment). As used herein, the term “antibody” collectively refers to immunoglobulins or immunoglobulin-like molecules including by way of example and without limitation, IgA, IgD, IgE, IgG and IgM, combinations thereof, and similar molecules produced during an immune response in any vertebrate, for example, in mammals such as humans, goats, rabbits and mice, as well as non-mammalian species, such as shark immunoglobulins. The term “antibody” includes intact immunoglobulins and “antibody fragments” or “antigen binding fragments” that specifically bind to a molecule of interest (or a group of highly similar molecules of interest) to the substantial exclusion of binding to other molecules (for example, antibodies and antibody fragments that have a binding constant for the molecule of interest that is at least 103M−1greater, at least 104M−1greater or at least 105M−1greater than a binding constant for other molecules in a biological sample). The term “antibody” also includes genetically engineered forms such as chimeric antibodies (for example, humanized murine antibodies), heteroconjugate antibodies (such as, bispecific antibodies). See also, Pierce Catalog and Handbook, 1994-1995 (Pierce Chemical Co., Rockford, Ill.); Kuby, J., Immunology 3rdunology, Ed., W.H. Freeman & Co., New York, 1997. More particularly, “antibody” refers to a polypeptide ligand comprising at least a light chain or heavy chain immunoglobulin variable region which specifically recognizes and binds an epitope of an antigen. Antibodies are composed of a heavy and a light chain, each of which has a variable region, termed the variable heavy (VH) region and the variable light (VL) region. Together, the VHregion and the VLregion are responsible for binding the antigen recognized by the antibody. Typically, an immunoglobulin has heavy (H) chains and light (L) chains interconnected by disulfide bonds. There are two types of light chain, lambda (λ) and kappa (κ). There are five main heavy chain classes (or isotypes) which determine the functional activity of an antibody molecule: IgM, IgD, IgG, IgA and IgE. Each heavy and light chain contains a constant region and a variable region, (the regions are also known as “domains”). In combination, the heavy and the light chain variable regions specifically bind the antigen. Light and heavy chain variable regions contain a “framework” region interrupted by three hypervariable regions, also called “complementarity-determining regions” or “CDRs”. The extent of the framework region and CDRs have been defined (see, Kabat et al., Sequences of Proteins of Immunological Interest, U.S. Department of Health and Human Services, 1991, Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 which is hereby incorporated by reference). The Kabat database is now maintained online. The sequences of the framework regions of different light or heavy chains are relatively conserved within a species. The framework region of an antibody, that is the combined framework regions of the constituent light and heavy chains, largely adopt β-sheet conformation and the CDRs form loops which connect, and in some cases form part of, the β- sheet structure. Thus, framework regions act to form a scaffold that provides for positioning the CDRs in correct orientation by inter-chain, non-covalent interactions. The CDRs are primarily responsible for binding to an epitope of an antigen. The CDRs of each chain are typically referred to as CDR1, CDR2, and CDR3, numbered sequentially starting from the N-terminus, and are also typically identified by the chain in which the particular CDR is located. Thus, a VH CDR3 is located in the variable domain of the heavy chain of the antibody in which it is found, whereas a VLCDR1 is the CDR1 from the variable domain of the light chain of the antibody in which it is found. An antibody that binds PD-L1 will have a specific VH region and the VL region sequence, and thus specific CDR sequences. Antibodies with different specificities (i.e. different combining sites for different antigens) have different CDRs. Although it is the CDRs that vary from antibody to antibody, only a limited number of amino acid positions within the CDRs are directly involved in antigen binding. These positions within the CDRs are called specificity determining residues (SDRs). The term “antibody” is further intended to encompass digestion fragments, specified portions, derivatives and variants thereof, including antibody mimetics or comprising portions of antibodies that mimic the structure and / or function of an antibody or specified fragment or portion thereof, including single chain antibodies and fragments thereof. Examples of binding fragments encompassed within the term “antigen binding portion” of an antibody include a Fab fragment, a monovalent fragment consisting of the VL, VH, CL and CH, domains; a F(ab′)2 fragment, a bivalent fragment comprising two Fab fragments linked by a disulfide bridge at the hinge region; a Fd fragment consisting of the VHand CH, domains; a Fvfragment consisting of the VLand VHdomains of a single arm of an antibody, a dAb fragment (Ward et al. (1989) Nature 341:544-546), which consists of a VHdomain; and an isolated complementarity determining region (CDR). Furthermore, although the two domains of the Fv fragment, VL and VH, are coded for by separate genes, they can be joined, using recombinant methods, by a synthetic linker that enables them to be made as a single protein chain in which the VL and VH regions pair to form monovalent molecules (known as single chain Fv(scFv)). Bird et al. (1988) Science 242:423-426 and Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 Huston et al. (1988) Proc. Natl. Acad Sci. USA 85:5879-5883. Single chain antibodies are also intended to be encompassed within the term “fragment of an antibody.” Any of the above-noted antibody fragments are obtained using conventional techniques known to those of skill in the art, and the fragments are screened for binding specificity and neutralization activity in the same manner as are intact antibodies. “Antibody fragments” or “antigen binding fragments” include proteolytic antibody fragments (such as F(ab′)2 fragments, Fab′ fragments, Fab′-SH fragments and Fab fragments as are known in the art), recombinant antibody fragments (such as sFv fragments, dsFv fragments, bispecific sFv fragments, bispecific dsFv fragments, F(ab)′2fragments, single chain Fv proteins (“scFv”), disulfide stabilized Fvproteins (“dsFv”), diabodies, and triabodies (as are known in the art), and camelid antibodies (see, for example, U.S. Patent Nos.6,015,695; 6,005,079; 5,874,541; 5,840,526; 5,800,988; and 5,759,808). An scFv protein is a fusion protein in which a light chain variable region of an immunoglobulin and a heavy chain variable region of an immunoglobulin are bound by a linker, while in dsFvs, the chains have been mutated to introduce a disulfide bond to stabilize the association of the chains. As used herein, the term “autoimmune disease” refers to a disease due to an overactive immune response of the body against substances and / or tissues normally present in the body. Accordingly, by specifically targeting immune cells involved in this overactive immune response, the lentiviral vector particles and formulations described herein are useful tools for the prevention and / or treatment of autoimmune disease. Autoimmune diseases include in particular acute disseminated encephalomyelitis, acute hemorrhagic leukoencephalitis, Addison's disease, Agammaglobulinemia, Alopecia areata, amyotrophic lateral sclerosis, ankylosing spondylitis, antiphospholipid syndrome, antisynthetase syndrome, atopic allergy, autoimmune aplastic anemia, autoimmune cardiomyopathy, autoimmune enteropathy, autoimmune hemolytic anemia, autoimmune hepatitis, autoimmune inner ear disease, autoimmune lymphoproliferative syndrome, autoimmune peripheral neuropathy, autoimmune pancreatitis, autoimmune polyendocrine syndrome, autoimmune progesterone dermatitis, autoimmune thrombocytopenic purpura, autoimmune urticaria, autoimmune uveitis, Balo disease, Balo concentric sclerosis, Bechets syndrome, Berger's disease, Bickerstaff's encephalitis, Blau syndrome, bullous pemphigoid, Castleman's disease, celiac disease, chronic inflammatory demyelinating polyneuropathy, chronic recurrent multifocal osteomyelitis, Churg-Strauss syndrome, cicatricial pemphigoid, Cogan syndrome, cold agglutinin disease, complement component 2 deficiency, cranial arteritis, CREST Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 syndrome, Crohn's disease, Cushing's syndrome, cutaneous leukocytoclastic angiitis, Dego's disease, Dercum's disease, dermatitis herpetiformis, dermatomyositis, diabetes mellitus type 1, diffuse cutaneous systemic sclerosis, Dressler's syndrome, discoid lupus erythematosus, eczema, enthesitis-related arthritis, eosinophilic fasciitis, eosinophilic gastroenteritis, epidermolysis bullosa acquisita, erythema nodosum, essential mixed cryoglobulinemia, Evan's syndrome, firodysplasia ossificans progressiva, fibrosing aveolitis, gastritis, gastrointestinal pemphigoid, giant cell arteritis, glomerulonephritis, goodpasture's syndrome, Grave's disease, Guillain-Barré syndrome (GBS), Hashimoto's encephalitis, Hashimoto's thyroiditis, hemolytic anaemia, Henoch-Schonlein purpura, herpes gestationis, hypogammaglobulinemia, idiopathic inflammatory demyelinating disease, idiopathic pulmonary fibrosis, idiopathic thrombocytopenic purpura, IgA nephropathy, inclusion body myositis, inflammatory demyelinating polyneuropathy, interstitial cystitis, juvenile idiopathic arthritis, juvenile rheumatoid arthritis, Kawasaki's disease, Lambert-Eaton myasthenic syndrome, leukocytoclastic vasculitis, lichen planus, lichen sclerosus, linear IgA disease (LAD), Lou Gehrig's disease, lupoid hepatitis, lupus erythematosus, Majeed syndrome, Meniere's disease, microscopic polyangiitis, Miller-Fisher syndrome, mixed connective tissue disease, morphea, Mucha-Habermann disease, multiple sclerosis, myasthenia gravis, myositis, neuropyelitis optica, neuromyotonia, ocular cicatricial pemphigoid, opsoclonus myoclonus syndrome, ord thyroiditis, palindromic rheumatism, paraneoplastic cerebellar degeneration, paroxysmal nocturnal hemoglobinuria (PNH), Parry Romberg syndrome, Parsonnage-Turner syndrome, pars planitis, pemphigus, pemphigus vulgaris, permicious anemia, perivenous encephalomyelitis, POEMS syndrome, polyarteritis nodosa, polymyalgia rheumatica, polymyositis, primary biliary cirrhosis, primary sclerosing cholangitis, progressive inflammatory neuropathy, psoriasis, psoriatic arthritis, pyoderma gangrenosum, pure red cell aplasia, Rasmussen's encephalitis, Raynaud phenomenon, relapsing polychondritis, Reiter's syndrome, restless leg syndrome, retroperitoneal fibrosis, rheumatoid arthritis, rheumatoid fever, sarcoidosis, Schmidt syndrome, Schnitzler syndrome, scleritis, scleroderma, Sjögren's syndrome, spondylarthropathy, Still's disease, stiff person syndrome, subacute bacterial endocarditis, Susac's syndrome, Sweet's syndrome, Sydenham chorea, sympathetic ophthalmia, Takayasu's arteritis, temporal arteritis, Tolosa-Hunt syndrome, transverse myelitis, ulcerative colitis, undifferentiated connective tissue disease, undifferentiated spondylarthropathy, vasculitis, vitiligo and Wegener's granulomatosis. As used herein, “Blimp1” refers to a B lymphocyte-induced maturation protein-1, a zinc-finger-containing DNA-binding transcriptional repressor that is a “master regulator” of Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 hematopoietic stem cells and plays a critical role in the development of plasma B cells, T cells, dendritic cells, macrophages, and osteoclasts. As used herein, a “Blimp1 pathway blocker” or “Blimp1 inhibitor” as used interchangeably herein, refers a molecule that reduces or inhibits the expression (e.g., mRNA or protein) of Blimp1 in cells, such as in B cells. An example of a Blimp1 pathway blocker or Blimp1 inhibitor is a Blimp1 siRNA or Blimp1 shRNA. As used herein, the term “cancer” refers encompasses any type of cancer, such as glioblastoma, neuroblastoma, B cell lymphoma, T cell lymphoma, breast cancer, hepatocellular carcinoma, cancer arising from hematopoietic cells, including leukemia, in particular B-CLL (B-cell Chronic lymphocytic leukaemia), CML (Chronic Myelogenous Leukemia) or T cell based leukemia such as ATL (acute T cell leukemia), ALL (Acute Lymphoblastic Leukemia), AML (Acute Myeloid Leukemia) and / or melanoma. As used herein, a “cell penetrating peptide” or “CPP” as used interchangeably herein refers to a peptide of 40 amino acids or less which has a positive charge that facilitates its penetration into cells across a cell membrane. Cellular uptake of a CPP occurs either through direct translocation or endocytosis. Cell penetrating peptides facilitate the cellular intake and update of bioactive cargo in cells, including molecules ranging from nanosize particles to small chemical compounds (e.g., small molecules) to large fragments of DNA. The “cargo” can be attached or associated with a cell penetrating peptide though chemical linkage via covalent bonds or by non-covalent interactions. Cell penetrating peptides for use in the present disclosure can have a length of 5 to 40 amino acids, 5 to 35 amino acids, 5 to 30 amino acids, or 5 to 25 amino acids. Examples of cell penetrating peptides include, but are not limited to, vectofusion-1 (VF-1), LAH4, LEPTIN30, and APOE. Other CPPs for use in the present disclosure can be found at the CPPsite2.0 Database of Cell-Penetrating Peptides (Agrawal P., Bhalla S., Usmani S.S., Singh S., Chaudhary K., Raghava G.P.S., Gautam A. CPPsite 2.0^: A repository of experimentally validated cell-penetrating peptides. Nucleic Acids Res.2016;44:1098–1103). As used herein, the term “HDAC inhibitor” or “histone deacetylase inhibitor” refers to molecules that reducing chromatin binding to histones. Examples of HDAC inhibitors include, but are not limited to, (a) valproic acid (VA); (b) hydroxamates, such as trichostatin A, suberuylanilide hydroxamic acid, PXD101, oxamflatin, LAW824, LBH589, pyroxamide, SK-7041, SK-7068 or tubacin; (c) benzamides, such as MS-275; (d) cyclic tetrapeptides such as depsipeptide, trapoxin A, apicidin or CHAPs; and (e) any combinations of (a)-(d). Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 The term "an effective amount" as used herein refers to the amount of the formulation described herein in Section 2 that is needed to increase the transduction efficiency of a lentiviral vector particle or lentiviral vector in a target cell. An effective amount can be determined by comparing the transduction efficiency of a lentiviral vector particle or lentiviral vector in a target cell using the formulations described herein compared to the transduction efficiency of a lentiviral vector particle or lentiviral vector in the absence of the formulations described herein (e.g., a control). An increase in the transduction efficiency at least 1%, at least 2%, at least 3%, at least 4%, at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, or at least 75% would be an effective amount. As used herein “mammalian target of rapamycin” or “mTOR” as used interchangeably herein, refers to a serine / threonine-specific protein kinase that belongs to a family of phosphatidylinositol-3-kinase (PI3K) related kinases. mTOR regulates cellular metabolism, growth and proliferation by forming and signaling through two protein complexes mTORC1 and mTORC2. As used herein a “mammalian target inhibitor of rapamycin inhibitor” or “mTOR inhibitor” refers to a molecule that inhibits the mammalian target of rapamycin (mTOR). As used herein, examples of mTOR inhibitors that can be used in the present disclosure include rapamycin (Rapa), sirolimus, everolimus, temsirolimus, metform, or mTOR kinase inhibitors, such as, PP242, PP30, Torin-1, Ku-0063794, WAY-600, WYE-687, or WYE-354. As used herein, a “natural surfactant” refers to surfactants derived from a natural source, such as a mammal, plant and / or a microorganism. For example, a natural surfactant can be obtained from (a) cells and / or organs of a mammal, such as, for example, phosphatidylcholines, lysophosphatidylcholine (LPC), dipalmitoylphosphatidylcholine, or phospholipids; (b) plants, such as, for example, saponins, coco glucoside, decyl glucoside, lauryl glucoside, coco betaine, or disodium laureth sulfosuccinate; or (c) microorganisms (e.g., fungi, yeast and bacteria), such as, for example, surfactants produced by Pseudomonas aeruginosa, Bacillus subtilis Candida albicans, or Acinetobacter calcoaceticus; or (d) any combinations of (a)-(c). The terms "parenteral administration", "administered parenterally" or “parental route” as used herein mean modes of administration other than enteral and topical administration, usually by injection, and includes, without limitation, intravenous, intrathecal, intramuscular, intraarterial, intrathecal, intracapsular, intraorbital, intraocular, intracardiac, Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 intradermal, intraperitoneal, transtracheal, subcutaneous, subcuticular, intraarticular, subcapsular, subarachnoid, intraspinal and intrasternal injection and infusion. As used herein, the term “poloxamer” refers to amphiphilic block copolymers having the general formula HO(C2H4O)a(C3H6O)b(C2H4O)aH and the structure shown below. poloxamer can be used in the present disclosure, although as described herein some poloxamers have preferred characteristics and / or effects. For example, poloxamer 407 (P407) has been shown to have a significant enhancing effect in paramyxovirus pseudotyped lentivirus, particularly in combination with peptide VF-1 (vectofusion-1). By way of example, poloxamers that can be used in the present disclosure include, but are not limited to, Poloxamer 124, Poloxamer 188, Poloxamer 237, Poloxamer 338 and Poloxamer 407 which have the properties provided in the below table. Poloxomer Physical Form a b Average Molecular weight central hydrophobic block of polypropylene glycol flanked by two hydrophilic blocks of polyethylene glycol (PEG). The approximate lengths of the two PEG blocks is 101 repeat units, while the approximate length of the propylene glycol block is 56 repeat units. The terms "prevent," "preventing," "prevention," "prophylactic treatment," and the like refer to reducing the probability of developing a disease, disorder, or condition in a subject, who does not have, but is at risk of or susceptible to developing a disease, disorder, and / or condition. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 A "subject" can include a human subject for medical purposes, such as for the treatment of an existing disease, disorder, condition or the prophylactic treatment for preventing the onset of a disease, disorder, or condition or an animal subject for medical, veterinary purposes, or developmental purposes. Suitable animal subjects include mammals including, but not limited to, primates, e.g., humans, monkeys, apes, gibbons, chimpanzees, orangutans, macaques and the like; bovines, e.g., cattle, oxen, and the like; ovines, e.g., sheep and the like; caprines, e.g., goats and the like; porcines, e.g., pigs, hogs, and the like; equines, e.g., horses, donkeys, zebras, and the like; felines, including wild and domestic cats; canines, including dogs; lagomorphs, including rabbits, hares, and the like; and rodents, including mice, rats, guinea pigs, and the like. An animal may be a transgenic animal. In some embodiments, the subject is a human including, but not limited to, fetal, neonatal, infant, juvenile, and adult subjects. Further, a "subject" can include a patient afflicted with or suspected of being afflicted with a disease, disorder, or condition. Thus, the terms "subject" and "patient" are used interchangeably herein. Subjects also include animal disease models (e.g., rats or mice used in experiments, and the like). The term "subject suspected of having" means a subject exhibiting one or more clinical indicators of a disease, disorder and / or condition. In some embodiments, the disease is an autoimmune disease. In yet other embodiments, the disease or condition is cancer. The term "subject in need thereof" means a subject identified as in need of a therapy or treatment. As used herein the term “target cell” or “target cells” refers to cells of the hematopoietic system (including T cells, B cells (including naïve B cells and / or memory B cells), monocytes, Th1 cells, Th2 cells, Treg cells, mast cells, dendritic cells (DCs), natural killer (NK) cells, natural killer T (NKT) cells, macrophages, hematopoietic stem cells, progenitor T and / or B cells, erythroblasts, platelets and / or neutrophils), plasma cells, stroma cells, endothelial cells, liver cells, muscle cells, cells of the nervous system, diseased cells or any combinations thereof. The term “therapeutically effective amount” refers to a quantity of lentiviral vector particle or lentiviral vector that confers a therapeutic effect on the treated subject. The therapeutic effect may be objective (i.e., measurable by some test or marker) or subjective (i.e. subject gives an indication of or feels an effect). As known by a person skilled in the art, effective doses will vary depending on route of administration, the size and / or weight of the subject, as well as the possibility of co-usage with other therapeutic agents. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 As used herein, the term “transduction” refers to a virus-mediated transfer of nucleic acids into one or more cells. The term "treating" a disease in a subject or "treating" a subject having a disease refers to subjecting the subject to a pharmaceutical treatment, e.g., the administration of a drug, composition and / or pharmaceutically active agent, such that at least one symptom of the disease disorder, and / or condition is decreased or prevented from worsening. As used herein, “vectofusion-1” or “VF-1” as used interchangeably herein, refers to a 26-mer cationic amphipathic peptide having the amino acid sequence: KKALLHAALAHLLALAHHLLALLKKA (SEQ ID NO:1). VF-1 is described by Fenard et al., Mol. Ther. Nucleic Acids, 2(5):1-10 (May 2013). As used herein, “LAH4” refers to an amphipathic peptide having the amino acid seqeunce: KKALLALALHHLAHLALHLALALKKA (SEQ ID NO:2). See Kichler et al., “Cationic amphipathic histidine-rich peptides for gene delivery,” Biochimica et Biophysica Acta (BBA) - Biomembranes, Volume 1758, Issue 3, 2006, pages 301-307. VF-1 may also be referred to as LAH4-A4, and exhibit the same overall composition of amino acids as LAH4 (e.g., LAH4-L1) but the distribution along the sequence and three-dimensional structure is different between these two. Further, as described herein the end-cap modification of the LAH4 amino acid sequence may be important achieving enhancements. End-cap modifications may include a carboxyl end cap (LAH4-C) from and an amide end cap (LAH4- A). In some cases the LAH4-C form may be preferred and may exclude the LAH4-A form (e.g., may have less than 1% of the LAH4-A form, less than 0.1%, less than 0.01%, etc.). Unless otherwise defined herein, scientific and technical terms used in connection with the present disclosure shall have the meanings that are commonly understood by those of ordinary skill in the art. For example, any nomenclatures used in connection with, and techniques of, cell and tissue culture, molecular biology, immunology, microbiology, genetics and protein and nucleic acid chemistry and hybridization described herein are those that are well known and commonly used in the art. The meaning and scope of the terms should be clear; in the event, however of any latent ambiguity, definitions provided herein take precedent over any dictionary or extrinsic definition. Further, unless otherwise required by context, singular terms shall include pluralities and plural terms shall include the singular. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 Transduction Enhancer (TE) Formulations In one aspect, the present disclosure relates to liquid formulations that enhance the transduction efficiency of lentiviral vector particles (See, Section 3) against different types of target cells, such as T-cells and B-cells. In particular, the compositions (e.g., transduction enhancers, TEs) described herein may be surprisingly effective for use with paramyxovirus pseudotyped lentiviruses, even as compared with other TE combinations. As will be described in greater detail herein certain combinations of TE components (e.g., CPP and surfactants) and / or one or more compositions may work surprisingly better than even other CPP and surfactant components, particularly in the context of paramyxovirus pseudotyped lentiviruses. In general, the formulations described herein can be administered simultaneously with a lentiviral vector particle or lentiviral vector containing a sequence or target gene of interest. For example, in some aspects, the formulations described herein and lentiviral vector particles or lentiviral vectors can be mixed together as a pre-mix at least 5 minutes, at least 10 minutes, at least 20 minutes, at least 30 minutes, at least 40 minutes, at least 50 minutes or at least 60 minutes prior to administration to a subject. In other aspects, the formulation and the lentiviral vector particle or lentiviral vector containing a target gene of interest are administered separately and sequentially and in any order. For example, in some aspects, the formulation described herein can be administered prior to or after the administration of the lentiviral vector particle or lentiviral vector. In some aspects, the formulation is administered at least 1 minutes, at least 2 minutes, at least 3 minutes, at least 4 minutes, at least 5 minutes, at least 6 minutes, at least 7 minutes, at least 8 minutes, at least 9 minutes, at least 10 minutes, at least 15 minutes, at least 20 minutes, at least 25 minutes, at least 30 minutes, at least 40 minutes, at least 50 minutes, at least 60 minutes, at 1.5 hours, at least 2 hours, at least 3 hours, at least 4 hours, at least 5 hours, at least 6 hours, at least 7 hours, at least 8 hours, at least 9 hours, or at least 10 hours prior to the administration of the lentiviral vector particles or lentiviral vectors. In other aspects, the formulation is administered at least 1 minutes, at least 2 minutes, at least 3 minutes, at least 4 minutes, at least 5 minutes, at least 6 minutes, at least 7 minutes, at least 8 minutes, at least 9 minutes, at least 10 minutes, at least 15 minutes, at least 20 minutes, at least 25 minutes, at least 30 minutes, at least 40 minutes, at least 50 minutes, at least 60 minutes, at 1.5 hours, at least 2 hours, at least 3 hours, at least 4 hours, at least 5 hours, at least 6 hours, at least 7 hours, at least 8 hours, at least 9 hours, or at least 10 hours after the administration of the lentiviral vector particles or lentiviral vectors. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 The formulations of the present disclosure comprise (a): at least one cell penetrating peptide (CPP); and (b) at least one of: (i) a HDAC inhibitor; (ii) a Blimp1 pathway blocker; or (iii) a surfactant, wherein the surfactant is a natural surfactant or a poloxamer. In some aspects, the formulations comprise: (a) at least one CPP and at least one HDAC inhibitor; (b) at least one CPP and at least one Blimp1 pathway blocker; (c) at least one CPP and at least one natural surfactant; (d) at least one CPP and at least one poloxamer; (e) at least one CPP, at least one HDAC inhibitor, and at least one Blimp1 pathway blocker; (f) at least one CPP, at least one HDAC inhibitor, and at least one natural surfactant; (g) at least one CPP, at least one HDAC inhibitor, and at least one poloxamer; (h) at least one CPP, at least one Blimp1 pathway blocker and at least one natural surfactant; (i) at least one CPP, at least one Blimp1 pathway blocker, and at least one poloxamer; (j) at least one CPP, at least one HDAC inhibitor, at least one Blimp1 pathway blocker, and at least one natural surfactant; (k) at least one CPP, at least one HDAC inhibitor, at least one Blimp1 pathway blocker, and at least one poloxamer; and (l) any combinations thereof. In still further aspects, the formulation comprises: (a) from about 1 µg / mL to about 20 µg / mL of at least one CPP; (b) from about 20 µg / mL to about 200 µg / mL of at least on HDAC inhibitor; (c) from about 20 µg / mL to about 200 µg / mL of at least one Blimp1 pathway blocker; (d) from about 10 µg / mL to about 1000 µg / mL of a surfactant, such as a natural surfactant or a poloxamer. In still further aspects, the formulation comprises: (a) from about 2 µg / mL to about 15 µg / mL of at least one CPP; (b) from about 30 µg / mL to about 150 µg / mL of at least on HDAC inhibitor; (c) from about 30 µg / mL to about 150 µg / mL of at least one Blimp1 pathway blocker; (d) from about 30 µg / mL to about 800 µg / mL of a surfactant, such as a natural surfactant or a poloxamer. In yet other aspects, the formulation comprises at least one CPP and at least one HDAC inhibitor. In still other aspects, the at least one CPP is vectofusion-1 and the at least one HDAC is valproic acid. In yet other aspects, the formulation comprises at least one CPP and at least one poloxamer. In still further aspects, the at least one CPP is vectofusion-1 and the at least one poloxamer is poloxamer 407. In yet other aspects, the formulation contains, in addition to at least one cell penetrating peptide (CPP) and at least one of: (i) a HDAC inhibitor; (ii) a Blimp1 pathway blocker; or (iii) a surfactant, wherein the surfactant is a natural surfactant or a poloxamer, at least one mammalian target of rapamycin (mTOR) inhibitor. The amount of at least one mTOR inhibitor in the formulation is from about 0.1 µg / mL to about 1 µg / mL. In still further Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 aspects, the amount of the at least one mTOR inhibitor in the formulation is from about 0.25 µg / mL to about 0.75 µg / mL. Thus, in still other aspects, formulations comprise: (a) at least one CPP, at least one HDAC inhibitor, and at least one mTOR inhibitor; (b) at least one CPP, at least one Blimp1 pathway blocker, and at least one mTOR inhibitor; (c) at least one CPP, at least one natural surfactant, and at least one mTOR inhibitor; (d) at least one CPP, at least one poloxamer and at least one mTOR inhibitor; (e) at least one CPP, at least one HDAC inhibitor, at least one Blimp1 pathway blocker, and at least one mTOR inhibitor; (f) at least one CPP, at least one HDAC inhibitor, at least one natural surfactant, and at least one mTOR inhibitor; (g) at least one CPP, at least one HDAC inhibitor, at least one poloxamer, and at least one mTOR inhibitor; (h) at least one CPP, at least one Blimp1 pathway blocker, at least one natural surfactant and at least one mTOR inhibitor; (i) at least one CPP, at least one Blimp1 pathway blocker, at least one poloxamer, and at least one mTOR inhibitor; (j) at least one CPP, at least one HDAC inhibitor, at least one Blimp1 pathway blocker, at least one natural surfactant, and at least one mTOR inhibitor; (k) at least one CPP, at least one HDAC inhibitor, at least one Blimp1 pathway blocker at least one poloxamer and at least one mTOR inhibitor; and (l) any combinations thereof. Lentiviral Vector Particles or Lentiviral Vectors The lentiviral vector particles for use in combination with the formulations described herein in Section 2 comprise a vector which contains at least one sequence or gene (e.g., 1, 2, 3, 4, or 5) of interest. Other sequences may be included, such as sequences that allow the vector to be packaged into the lentivirus vector particle and sequences that promote expression of the sequence(s) of interest following transduction of the target cell. The vector can be derived from any of a large number of suitable, available lentiviral based vectors, including those identified for human gene therapy applications, such as those described by Pfeifer and Verma, Annu. Rev. Genomics Hum. Genet.2:177-211, (2001), which is herein incorporated by reference. Lentiviral vectors that can be used include those based on Human Immunodeficiency Virus (HIV-1), HIV-2, feline immunodeficiency virus (FIV), equine infectious anemia virus (EIAV), Simian Immunodeficiency Virus (SIV), Caprine Arthritis Encephalitis Virus (CAEV), maedi / visna virus, or any combinations thereof. Lentiviruses are useful in various types of treatment and therapy because of their ability to infect both Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 dividing and non-dividing cells, thereby eliminating the need for the target cells to be dividing (or stimulating the target cells to divide). In some aspects, the vector is pseudotyped, meaning that the lentiviral vector particle contains glycoproteins (such as envelope glycoproteins) that are derived from at least another virus other than a lentivirus. For example, the vector can be pseudotyped with glycoproteins derived from a virus of the Paramyxoviridae family, such as a virus of the Morbillivirus genus or the Henipavirus genus, the Vesiculovirus genus. In other aspects, the vector can be pseudotyped with glycoproteins derived from a virus of the Narmovirus genus, the Alphavirus genus, the Avulavirus genus, the Orthopneumovirus genus, the Lyssavirus genus, the Gammaretrovirus genus, the Betacoronavirus genus, the Betacoronavirus genus, a Baboon endogenous retrovirus (BaEV) or any combinations thereof. The viruses of the Morbillivirus and Henipavirus genuses use two types of glycoproteins to enter into a target cell: an attachment protein (called glycoprotein G in a virus of the Henipavirus genus or glycoprotein H in a virus of the Morbillivirus genus) and a glycoprotein F (also called fusion protein or protein F). The protein F mediates the fusion of viral membranes with the cellular membranes of the host cell. The glycoprotein G / H recognizes the receptor on the target membrane and supports the F protein in its membrane fusion function. Examples of a virus of the Morbillivirus genus that can be used include measles virus, Canine distemper virus, Cetacean morbillivirus, Peste-des-petits-ruminants virus, Phocine distemper virus, Rinderpest virus A virus or combinations thereof. Examples of a virus of the Henipavirus genus that can be used include Nipah virus, Cedar virus, Hendra virus and combinations thereof. In some aspects, the modified enveloped glycoproteins are derived from the envelope glycoprotein G and the glycoprotein F of a Nipah virus, such as described in U.S. Patent No.11,608,509, which is herein incorporated by reference. In another aspect, the glycoprotein G and / or glycoprotein F of the Nipah virus can contain one or more mutations, deletions, substitutions or combinations thereof, such as those described in U.S. Patent No.11,608,509. For example, other viruses in the Nipah and Hendra class (e.g., henipavirus) that may be included as part of a paramyxovirus pseudotyped lentivirus (LV) particle / vectors that may be used with the TEs described here, likely because they act at the cell membrane, may include: Cedar henipavirus, Ghanaian bat henipavirus, Langya henipavirus and / or Mojiang henipavirus. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 Examples of a virus of the Narmovirus genus that can be used include Tupaia paramyxovirus (TPMV). Examples of a virus of the Avulavirus genus that can be used include Newcastle disease virus (NDV). Examples of a virus of the Orthopneumovirus genus that can be used include Respiratory syncytial virus (RSV). Examples of a virus of the Lyssavirus genus that can be used include Rabies viruses (RVs). Examples of a virus of the Gammaretrovirus genus that can be used include Gibbon-ape leukemia virus (GaLV), Moloney murine leukemia virus (MoMLV), and Murine Stem Cell Virus (MSCV). Examples of a virus of the Betacoronavirus genus that can be used include MERS- CoV and SARS-CoV. In some aspects, the Baboon endogenous retrovirus (BaEV) can be used. In addition, the glycoproteins used from any of these above viruses can contain one or more mutations, deletions, substitutions, or combinations thereof compared to the native or wildtype sequence. Additionally, the vector incorporates a variety of safety features. Such safety features can include a self-inactivating long terminal repeat (LTR) and a non-integrating genome. For example, the vector can comprise sequences from a lentivirus genome, such as the HIV-1 genome or the SIV genome. The vector may comprise sequences from the 5′ and 3′ LTRs of a lentivirus, and in particular, may comprise the R and U5 sequences from the 5′ LTR of a lentivirus and an inactivated or self-inactivating 3′ LTR from a lentivirus. The LTR sequences may be LTR sequences from any lentivirus from any species. For example, LTR sequences from HIV, SIV, FIV or BIV can be used. As discussed above, the vector may comprise an inactivated or self-inactivating 3′ LTR (See, for example, U.S. Patent Publication No.2010 / 0323403, which is herein incorporated by reference). Generally, a self-inactivating vector has a deletion of the enhancer and promoter sequences from the 3′ LTR, which is copied over into the 5′ LTR during vector integration. In some aspects, the U3 element of the 3′ LTR may contain a deletion of its enhancer sequence, the polypurine tract (PPT), the TATA box, Sp1 and NF- kappa B sites. As a result of the self-inactivating 3′ LTR, the provirus that is generated following entry and reverse transcription will comprise an inactivated 5′ LTR. The rationale is to improve safety by reducing the risk of mobilization of the vector genome and the Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 influence of the LTR on nearby cellular promoters. The self-inactivating 3′ LTR may be constructed using routine techniques known in the art. In some aspects, the U3 sequence from the lentiviral 5′ LTR may be replaced with a promoter sequence in the vector, such as a heterologous promoter sequence. This can increase the titer of virus recovered from the packaging cell line. An enhancer sequence may also be included. Any enhancer / promoter combination that increases expression of the viral RNA genome in the packaging cell line may be used. For example, a CMV enhancer / promoter sequence can be used, such as described in U.S. Patent Nos.5,385,839 and 5,168,062, which are herein incorporated by reference. Alternatively, an EF1-alpha promoter can be used. In further aspects, the risk of insertional mutagenesis is minimized by constructing the lentiviral vector to be integration defective. A variety of approaches can be used to produce a non-integrating vector genome. These approaches can involve engineering a mutation(s) into the integrase enzyme component of the pol gene, such that it encodes a protein with an inactive integrase. The vector can be modified to prevent integration by, for example, mutating or deleting one or both attachment sites, or making the 3′ LTR-proximal polypurine tract (PPT) non-functional through deletion or modification. Additionally, non- genetic approaches can also be used, such as by using one or more pharmacological agents that inhibit one or more functions of integrase. These approaches are not mutually exclusive, meaning that one or more of them can be used at a time. For example, both the integrase and attachment sites can be non-functional, or the integrase and PPT site can be non-functional, or the attachment sites and PPT site can be non-functional, or all of them can be non- functional. As discussed above, in one aspect, a non-functional integrase can be made and used. Integrase cleaves viral double-stranded blunt-ended DNA and joins the ends to 5′- phosphates in the two strands of a chromosomal target site. Integrase has three functional domains: N-terminal domain, which contains a zinc-binding motif (HHCC), the central domain core, which contains the catalytic core and a conserved DD35E motif (D64, D116, E152 in HIV-1), and a C-terminal domain, which has DNA binding properties. Point mutations can be introduced into integrase to disrupt normal function. Many integrase mutations are known in the art and can be used (such as, for example, Philpott and Thrasher, Human Gene Therapy, 18:483 (2007); Apolonia, Thesis submitted to University College London, pp, 82-97 (April 2009); Engelman et al., J Virol, 69: 2729, (1995); Nightingale et al., Mol Therapy, 13: 1121 (2006), each of which are herein incorporated by Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 reference). The sequence encoding the integrase protein can be deleted or mutated to render the protein inactive, preferably without significantly impairing reverse transcriptase activity or nuclear targeting, thereby only preventing integration of the provirus into the target cell genome. Acceptable mutations can reduce integrase catalysis, strand transfer, binding to att sites, binding to host chromosomal DNA, and other functions. For example, a single aspartic acid to asparagine substitution at residue 35 of HIV or SIV integrase completely abolishes viral DNA integration. Deletions of integrase are generally confined to the C-terminal domain. Deletion of coding sequence for residues 235-288 result in a useful non-functional integrase (Engelman et al., J Virol.69:2729 (1995)). By way of additional examples, mutations can be generated, for example, Asp64 (residue numbers are given for HIV-1, corresponding residue numbers for integrase from other lentiviruses or retroviruses can be readily determined by one of ordinary skill) (e.g., D64E, D64V), Asp116 (e.g., D116N), Asn120 (e.g., N120K), Glu152, Gln148 (e.g., Q148A), Lys156, Lys159, Trp235 (e.g. W235E), Lys264 (e.g., K264R), Lys266 (e.g., K266R), Lys273 (e.g., K273R). Other mutations can be constructed and tested for integration, transgene expression, and any other desirable parameter. Assays for these functions are well known in the art. Mutations can be generated by any of a variety of techniques known in the art, such as site-directed mutagenesis and chemical synthesis of nucleic acid sequence. One or more mutations can be made in an integrase. For example, an integrase have a mutation at a single amino acid, at two amino acids, at three amino acids, at four amino acids, at five amino acids and so on. Alternatively, or in combination with the use of integrase mutant(s), the attachment sites (att) in U3 and U5 can also be mutated. Integrase binds to these sites and the 3′-terminal dinucleotide is cleaved at both ends of the vector genome. A CA dinucleotide is located at the recessed 3′ end; the CA is required for processing, mutation of the nucleotides blocks integration into the host chromosome. The A of the CA dinucleotide is an important nucleotide for integration, and mutations at both ends of the genome provide useful results. Integration can also be inhibited by mutation or deletion of polypurine tract (PPT) (See, WO 2009 / 076524 which is herein incorporated by reference), located proximally to the 3′ LTR. The PPT is a polypurine sequence of about 15 nucleotides that can serve as a primer binding site for plus-strand DNA synthesis. Mutations or deletions of PPT targets the reverse transcription process. As discussed above, a PPT can be made non-functional by mutation or by deletion. The entire 15 nucleotides (nt) of the PPT can be deleted or shorter deletions of 14 nt, 13, nt, 12 nt, 11 nt, 10 nt, 9 nt, 8 nt, 7 nt, 6 nt, 5 nt, 4 nt, 3 nt and 2 nt can be made. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 The described approaches to make a vector genome non-integrating can be used individually or in combination. Using more than one approach may be used to build a fail- safe vector through redundant mechanisms. Thus, PPT mutations or deletions can be combined with att site mutations or deletions or with Integrase mutations or PPT mutations or deletions can be combined with both att site mutations or deletions and Integrase mutations. Similarly, att site mutations or deletions and Integrase mutations may be combined with each other or with PPT mutations or deletions. An additional approach to enhancing the safety of the pseudotyped lentiviral particles involves modifying the vector comprising the gag / pol genes to remove sites of potential recombination with the lentiviral vector. This approach can be used individually or in combination with any of the approaches described herein. For example, the gag and pol genes can be mammalian or human “codon optimized”, i.e., at least 50%, 60%, 70%, 75%, 80%, 85%, 90% of 95% of the codons of the gag and / or pol genes are replaced with codons that encode the same amino acid but that are preferred by mammalian cells, e.g., human cells, thus improving or optimizing expression in the mammalian, e.g. human, cells. To codon optimize the gag and pol genes, a polynucleotide is generated that alters the “wildtype” codons to codons more frequently utilized in the human genome. In HIV, however, certain portions of the genome should retain substantially the original codons (e.g., at least 75%, 80%, 85%, 90%, 95% or 100% of the original codons) in order to permit frameshifting that is required to synthesize Gag and Pol starting from the same initiation codon of its mRNA. As discussed herein, the viral vector comprises a sequence or gene of interest that is desirable to express in target cells. In some aspects, the sequence or gene of interest is located between the 5′ LTR and 3′ LTR sequences. In other aspects, the sequence or gene of interest is in a functional relationship with other genetic elements, for example transcription regulatory sequences including promoters or enhancers, to regulate expression of the sequence or gene of interest in a particular manner. In certain instances, useful transcriptional regulatory sequences include those that are highly regulated with respect to activity, both temporally and spatially. Expression control elements that may be used for regulating the expression of the components are known in the art and include, but are not limited to, inducible promoters, constitutive promoters, secretion signals, enhancers and other regulatory elements. The sequence or gene of interest and any other expressible sequence is typically in a functional relationship with internal promoter / enhancer regulatory sequences. An “internal” promoter / enhancer is one that is located between the 5′ LTR and the 3′ LTR sequences in the Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 viral vector construct and is operably linked to the sequence or gene of interest. The internal promoter / enhancer may be any promoter, enhancer or promoter / enhancer combination known to increase expression of a gene with which it is in a functional relationship. A “functional relationship” and “operably linked” means that the sequence is in the correct location and orientation with respect to the promoter and / or enhancer that the sequence or gene of interest will be expressed when the promoter and / or enhancer is contacted with the appropriate molecules. The internal promoter / enhancer selected is based on the desired expression pattern of the sequence or gene of interest and the specific properties of known promoters / enhancers. Thus, the internal promoter may be constitutively active. Non-limiting examples of constitutive promoters that may be used include the promoter for ubiquitin (U.S. Patent No. 5,510,474 and WO 98 / 32869, each of which is incorporated by reference), CMV (U.S. Patent Nos.5,385,839 and 5,168,062, which are herein incorporated by reference), beta-actin (Gunning et al., Proc. Natl. Acad. Sci. USA 84:4831-4835 (1989), which is herein incorporated by reference) PGK (Adra et al., Gene, 60:65-74 (1987); Singer-Sam et al., Gene, 32:409-417 (1984); and Dobson et al., Nucleic Acids Res.10:2635-2637 (1982), each of which is incorporated by reference), EF1-alpha (Qin J.Y., et al., PLoS One.2010;5:e10611 (2010), which is herein incorporated by reference), MND (Astrakhan, A., et al., Blood, 119:4395-4407 (2012), which is herein incorporated by reference), MCU3 (Zufferey et al., J. Virol., 73:2886-2892 (1999), which is herein incorporated by reference), and SFFV (Baum C., et al., J. Virol., 69:7541-7547 (1995), which is herein incorporated by reference). In some aspects, the promoter used to control expression of the sequence or gene of interest encoded by the pseudotyped lentiviral vector is an intron-deficient promoter. In other aspects, the human Ubiquitin-C (UbiC) promoter is used to control expression of the antigens encoded by the pseudotyped lentiviral vector genome. In still other aspects, the UbiC promoter is modified to remove introns, i.e., the promoter is intron deficient. Alternatively, the promoter may be a tissue specific promoter. Examples of tissue specific promoters include, but are not limited to, CD11b (Dziennis S., et al., Blood, 85:319- 329 (1995), which is herein incorporated by reference), ALB (Pinkert C.A., et al., Genes Dev., 1:268-276 (1987), which is herein incorporated by reference), TBG (Yan Z., et al., Gene, 506:289-294 (2012), which is herein incorporated by reference), and MHC (Subramaniam, A., et al., J. Biol. Chem., 26:24613-24520 (1991, which is herein incorporated by reference)). In addition, promoters may be selected to allow for inducible expression of the sequence or gene of interest. A number of systems for inducible expression are known in Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 the art, including the tetracycline responsive system, the lac operator-repressor system, as well as promoters responsive to a variety of environmental or physiological changes, including heat shock, metal ions, such as metallothionein promoter, interferons, hypoxia, steroids, such as progesterone or glucocorticoid receptor promoter, radiation, such as VEGF promoter. A combination of promoters may also be used to obtain the desired expression of the gene of interest. The artisan of ordinary skill will be able to select a promoter based on the desired expression pattern of the gene in the organism or the target cell of interest. In some aspects, the vector comprises at least one RNA Polymerase II or III responsive promoter. This promoter can be operably linked to the sequence or gene of interest and can also be linked to a termination sequence. In addition, more than one RNA Polymerase II or III promoters may be incorporated. RNA polymerase II and III promoters are well known in the art. Examples of suitable RNA polymerase III promoters can be found, for example, in Paule and White, Nucleic Acids Research, 28:1283-1298 (2000), which is incorporated herein by reference. RNA polymerase II or III promoters also include any synthetic or engineered DNA fragment that can direct RNA polymerase II or III to transcribe downstream RNA coding sequences. Additionally, the RNA polymerase II or III (Pol II or III) promoter or promoters used as part of the viral vector genome can be inducible. The vector can also contain an internal enhancer to increase expression of the sequence or gene of interest. For example, a CMV enhancer (Boshart et al., Cell, 41:521(1985), which is incorporated herein by reference) can be used. Many enhancers in viral genomes, such as HIV, CMV, and in mammalian genomes have been identified and characterized and available in GenBank. Additionally, an enhancer can be used in combination with a heterologous promoter. The selection of an appropriate enhancer for use in the vector can be used using routine techniques known in the art. Generally, the lentiviral vector contains a promoter that is recognized by a target cell and that is operably linked to a sequence or gene of interest, viral components, and to other sequences discussed herein. A promoter is an expression control element formed by a nucleic acid sequence that permits binding of RNA polymerase and transcription to occur. Promoters may be inducible, constitutive, temporally active, or tissue specific. The activity of inducible promoters is induced by the presence or absence of biotic or abiotic factors. Inducible promoters can be used to turn on or off the expression of genes to which they are operably linked in certain stages of development of an organism, its manufacture, or in a particular tissue. Inducible promoters can be grouped as chemically-regulated promoters, and physically-regulated promoters. Chemically-regulated promoters include, not are not limited Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 to, alcohol-regulated promoters (e.g., alcohol dehydrogenase I (alcA) gene promoter), tetracycline-regulated promoters (e.g., tetracycline-responsive promoter), steroid-regulated promoter (e.g., rat glucocorticoid receptor (GR)-based promoter, human estrogen receptor (ER)-based promoter, moth ecdysone receptor-based promoter, and the promoters based on the steroid / retinoid / thyroid receptor superfamily), metal-regulated promoters (e.g., metallothionein gene-based promoters), and pathogenesis-related promoters (e.g., Arabidopsis and maize pathogen-related (PR) protein-based promoters). Physically- regulated promoters include, but are not limited to, temperature-regulated promoters (e.g., heat shock promoters), and light-regulated promoters (e.g., soybean SSU promoter). Appropriate promoters can be selected using routine techniques in the art based on the specific circumstances. Many different promoters are well known in the art, as are methods for operably linking the promoter to the gene to be expressed. Both native promoter sequences and heterologous promoters can be used to direct expression in the packaging cell and target cell. In some aspects, heterologous promoters are used as they generally permit greater transcription and higher yields of the desired protein as compared to the native promoter. The promoter can be obtained, for example, from the genomes of viruses such as polyoma virus, fowlpox virus, adenovirus, bovine papilloma virus, avian sarcoma virus, cytomegalovirus, a retrovirus, hepatitis-B virus and Simian Virus 40 (SV40). The promoter may also be, for example, a heterologous mammalian promoter, e.g., the actin promoter or an immunoglobulin promoter, a heat-shock promoter, or the promoter normally associated with the native sequence, provided such promoters are compatible with the target cell. In some aspects, the promoter is the naturally occurring viral promoter in a viral expression system. Transcription may be increased by inserting an enhancer sequence into the vector(s). Enhancers are typically cis-acting elements of DNA, usually about 10 to 300 bp in length, that act on a promoter to increase its transcription. Many enhancer sequences are now known from mammalian genes (globin, elastase, albumin, alpha-fetoprotein, and insulin) and from eukaryotic cell viruses. Examples include the SV40 enhancer on the late side of the replication origin (bp 100-270), the cytomegalovirus early promoter enhancer, the polyoma enhancer on the late side of the replication origin, and adenovirus enhancers. The enhancer may be spliced into the vector at a position 5′ or 3′ to the antigen-specific polynucleotide sequence, but is preferably located at a site 5′ from the promoter. The vector (e.g., expression vectors) may also contain sequences necessary for the termination of transcription and for stabilizing the mRNA. These sequences are often found Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 in the 5′ and, occasionally 3′, untranslated regions of eukaryotic or viral DNAs or cDNAs and are well known in the art. The viral vector may also contain additional genetic elements. The types of elements that may be included in the construct are not limited in any way and may be chosen to achieve a particular result. For example, a signal that facilitates nuclear entry of the viral genome in the target cell may be included. An example of such a signal is the HIV-1 flap signal. Further, elements may be included that facilitate the characterization of the provirus integration site in the target cell. For example, a tRNA amber suppressor sequence may be included in the construct. An insulator sequence from e.g., chicken 3-globin may also be included in the viral genome construct. This element reduces the chance of silencing an integrated provirus in the target cell due to methylation and heterochromatinization effects. In addition, the insulator may shield the internal enhancer, promoter and exogenous gene from positive or negative positional effects from surrounding DNA at the integration site on the chromosome. In addition, the vector genome may contain one or more genetic elements designed to enhance expression of the gene of interest. For example, a woodchuck hepatitis virus responsive element (WRE) may be placed into the construct (Zufferey et al., J. Virol.74:3668-3681 (1999); Deglon et al., Hum. Gene Ther.11:179-190 (2000), each of which is incorporated herein). The viral vector is constructed in a plasmid form that can be transfected into a packaging or producer cell line. The plasmid generally comprises sequences useful for replication of the plasmid in bacteria. Such plasmids are well known and can be selected for a particular use using routine techniques known in the art. In addition, vectors that include a prokaryotic origin of replication may also include a gene whose expression confers a detectable or selectable marker such as a drug resistance. Typical bacterial drug resistance products are those that confer resistance to ampicillin or tetracycline. Plasmids containing one or more of the components described herein are readily constructed using standard techniques well known in the art. For analysis to confirm correct sequences in plasmids constructed, the plasmid may be replicated in E. coli, purified, and analyzed by restriction endonuclease digestion or its DNA sequence determined by conventional methods. Vectors constructed for transient expression in mammalian cells can also be used. Transient expression involves the use of an expression vector that is able to replicate efficiently in a host cell, such that the host cell accumulates many copies of the expression vector and, in turn, synthesizes high levels of the polypeptide encoded by the Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 antigen-specific polynucleotide in the expression vector. Other vectors and methods suitable for adaptation to the expression of polypeptides are well known in the art and can be readily adapted to the specific circumstances. The sequence or gene of interest is not limited in any way and includes any nucleic acid that one of ordinary skill desires to have integrated, transcribed, and expressed in the target cell. The product can be a protein or a nucleic acid. A sequence or gene of interest may encode a therapeutic protein, apoptotic protein, chimeric antigen receptor, cell surface receptor, antibody, antibody fragment, siRNA, shRNA, antigen, cytokine, microRNA, CRISPR ((clustered, regularly interspaced, short palindromic repeat)) / CAS element(s) (for example CAS9 and / or guide RNAs, in particular for specific gene disruption or correction), other nuclease system, such as Zink Finger Nucleases, S / MAR (Scaffold / Matrix Attachment Region)—episomes, ligand and / or receptor. Examples of a sequence or gene of interest include globin gene, hematopoietic growth factor gene (for example erythropoietin (EPO) gene), interleukin gene (especially Interleukin-1, Interleukin-2, Interleukin-3, Interleukin-6 or Interleukin-12 gene), colony- stimulating factor gene (such as granulocyte colony-stimulating factor gene, granulocyte / macrophage colony-stimulating factor gene or stem-cell colony-stimulating factor gene), the platelet-specific integrin allbβ gene, multidrug resistance gene, the gp91 or gp 47 genes, which are defective in patients with chronic granulomatous disease (CGD), antiviral gene rendering cells resistant to infections with pathogens (such as human immunodeficiency virus), gene coding for blood coagulation factors VIII or IX which are mutated in hemophilia's, gene encoding a ligand involved in T cell-mediated immune responses (such as T cell antigen receptors, chimeric antigen receptor (CARs), B cell antigen receptors (immunoglobulins, neutralizing antibodies against HIV, Hepatitis C, Hepatitis B and / or other infectious diseases), the interleukin receptor common y chain gene, TNF gene, gamma interferon gene, CTLA4 gene, genes expressed in tumor cells such as Melana, MAGE genes (such as MAGE-1, MAGE- 2, MAGE-3), BAGE genes, GAGE genes (such as GAGE-1 and GAGE-2), LAGE-1 genes, NY-ESO-1 genes, P198 gene, P1A gene, or gp100 gene. Therapeutic Applications and Kits In yet another aspect, the present disclosure relates to the use of the above- described formulations (See, Section 2) in combination with lentiviral vector particles or lentiviral vectors (including pseudotyped lentiviral vector particles or pseudotyped lentiviral Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 vectors) (See, Section 3) in treating a subject (e.g., a human), specifically, in immune therapy gene therapy and / or vaccination. Gene therapy is a therapy that uses one or more gene(s) for treatment, which can, for example, be obtained by delivering in a target cell a gene of interest and / or correcting a gene(s) of interest at the endogenous site in vivo. In gene therapy, a nucleic acid comprising the gene(s) of interest is delivered into the cells of a patient, the expression of the protein(s) encoded by gene(s) of interest and / or the correction of the gene(s) of interest thereby allowing preventing and / or treating a disease. The formulations described herein when used in combination with a lentiviral vector particle allow for efficient transduction in vivo and thus overcome some of the difficulties with gene therapy known in the art. One or more gene(s) of interest may be present in the RNA molecule comprised in the lentiviral vector described herein and the correction of one or more gene(s) of interest may be carried out by the CRISPR / CAS system. Immune therapy, also called immunotherapy, is a therapy based on modulating the activity of the immune system (for example, stimulation or inhibition) to prevent and / or treat a disease. In the present disclosure, immunotherapy involves modulating the activity of only specific target cells, by using a combination of the formulations and lentiviral vector particles or lentiviral vectors described herein, and optionally selectively transducing said target cells (e.g., immune cells). For example, the lentiviral vector may be used to activate B cells, such as make them differentiate in plasma cells, and optionally transduced them with a nucleic acid encoding an ectopic antibody against an infectious agent (for example against HIV, HCV or HBC). Immune therapy also comprises T cell therapy. In T cell therapy, T cells might in addition to being modulated for their function be more permissive to gene transfer, for example for the T cell receptor (CAR) gene transfer. Adoptive T cell therapy is a therapy wherein T cells are transfused to a subject in need thereof. In other aspects, vaccination consists in displaying at the surface of the lentiviral vector particle or lentiviral vector specific viral epitopes that will be targeted to and activate at the same time the antigen presenting cells (for example macrophages) that will subsequently present the epitopes to the immune system (T and B cells). Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 In other aspects, the use of the formulations described herein in combination with lentiviral vector particles or lentiviral vectors can be used to modulate the activity of target cells and optionally selectively transduces target cells. In yet further aspects, the use of the formulations described herein in combination with lentiviral vector particles or lentiviral vectors can be used to prevent and / or treat a disease. Examples of diseases include, for example, an immune disease (for example an auto- immune disease), cancer, genetic disease, allergic disease, inflammatory disease, infectious disease (in particular bacteria and / or virus infection), metabolic disease, neurological disease (such as neural dystrophy, Alzheimer disease, Parkinson disease, Huntington disease), muscular disease, or any combination thereof. In yet another aspect, the formulations described herein in combination with lentiviral vector particles or lentiviral vectors containing a sequence or gene of interest can be used to improve DC (Dendritic Cell) vaccine, for example, by co-displaying DC cell specific ligand (such as CD11b) and GM-SCF (Granulocyte-Macrophage Colony-Stimulating Factor) on the surface of the vector, for protein or gene transfer. In yet another aspect, the formulations described herein in combination with lentiviral vector particles or lentiviral vectors can be used to enhance selective gene delivery into resting B lymphocytes, for example in B cell-based gene therapy, such as immunotherapy that allows the B cells to produce neutralizing antibodies against infectious agent(s) or allows B cell secretion of recombinant proteins that are tolerated by the immune system since B cell can act as tolerogenic cells. Moreover, displaying one or more cytokines on the surface of the lentiviral vector particle or lentiviral vector may induce the T cell subset differentiating into phenotypes like TSCM or TCM, which might persist long term in vivo. In yet another aspect, the present disclosure may be used for in vivo expansion of (autologous) anti-cancer natural killer cells, for cancer therapy. In another aspect, the formulations described herein in combination with lentiviral vector particles or lentiviral vectors can used to induce apoptosis of a defined cell subset by co-displaying an apoptosis ligand and a tumor or immune cell specific targeting domain. The lentiviral vector particle or lentiviral vector described may be provided in the form of a pharmaceutical composition and can be packaged together or separately with the formulations described herein. In some aspects, the formulations described herein are included in a kit along with instructions for use. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 In another aspect, the present disclosure relates to a method for treating a subject in need thereof comprising administering to the subject an effective amount of the formulation described herein and a therapeutically effective amount of a lentiviral vector particle or lentiviral vector described herein in the frame of an immune therapy, gene therapy and / or vaccination. In some aspects, the formulations described herein and the lentiviral vector particle are administered simultaneously at the same time as a single composition. In other aspects, the formulation and the lentiviral vector particle are administered separately and sequentially. For example, in some aspects, the formulation described herein can be administered prior to or after the administration of the lentiviral vector particle or lentiviral vector. In some aspects, the formulation is administered at least 1 minutes, at least 2 minutes, at least 3 minutes, at least 4 minutes, at least 5 minutes, at least 6 minutes, at least 7 minutes, at least 8 minutes, at least 9 minutes, at least 10 minutes, at least 15 minutes, at least 20 minutes, at least 25 minutes, at least 30 minutes, at least 40 minutes, at least 50 minutes, at least 60 minutes, at 1.5 hours, at least 2 hours, at least 3 hours, at least 4 hours, at least 5 hours, at least 6 hours, at least 7 hours, at least 8 hours, at least 9 hours, or at least 10 hours prior to the administration of the lentiviral vector particles or lentiviral vectors. In other aspects, the formulation is administered at least 1 minutes, at least 2 minutes, at least 3 minutes, at least 4 minutes, at least 5 minutes, at least 6 minutes, at least 7 minutes, at least 8 minutes, at least 9 minutes, at least 10 minutes, at least 15 minutes, at least 20 minutes, at least 25 minutes, at least 30 minutes, at least 40 minutes, at least 50 minutes, at least 60 minutes, at 1.5 hours, at least 2 hours, at least 3 hours, at least 4 hours, at least 5 hours, at least 6 hours, at least 7 hours, at least 8 hours, at least 9 hours, or at least 10 hours after the administration of the lentiviral vector particles or lentiviral vectors. In yet another aspect, the present disclosure relates to a method for treating a subject in need thereof comprising administering to a subject an effective amount of the formulation described herein and a therapeutically effective amount of a lentiviral vector particle or lentiviral vector as described herein, wherein said lentiviral vector particle or lentiviral vector selectively modulates the activity of target cells and optionally selectively transduces target cells. In some aspects, the formulations described herein and the lentiviral vector particle are administered simultaneously at the same time as a single composition. In other aspects, the formulation and the lentiviral vector particle are administered separately and sequentially. For example, in some aspects, the formulation described herein can be administered prior to or after the administration of the lentiviral vector particle or lentiviral vector. In some aspects, the formulation is administered at least 1 minutes, at least 2 minutes, Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 at least 3 minutes, at least 4 minutes, at least 5 minutes, at least 6 minutes, at least 7 minutes, at least 8 minutes, at least 9 minutes, at least 10 minutes, at least 15 minutes, at least 20 minutes, at least 25 minutes, at least 30 minutes, at least 40 minutes, at least 50 minutes, at least 60 minutes, at 1.5 hours, at least 2 hours, at least 3 hours, at least 4 hours, at least 5 hours, at least 6 hours, at least 7 hours, at least 8 hours, at least 9 hours, or at least 10 hours prior to the administration of the lentiviral vector particles or lentiviral vectors. In other aspects, the formulation is administered at least 1 minutes, at least 2 minutes, at least 3 minutes, at least 4 minutes, at least 5 minutes, at least 6 minutes, at least 7 minutes, at least 8 minutes, at least 9 minutes, at least 10 minutes, at least 15 minutes, at least 20 minutes, at least 25 minutes, at least 30 minutes, at least 40 minutes, at least 50 minutes, at least 60 minutes, at 1.5 hours, at least 2 hours, at least 3 hours, at least 4 hours, at least 5 hours, at least 6 hours, at least 7 hours, at least 8 hours, at least 9 hours, or at least 10 hours after the administration of the lentiviral vector particles or lentiviral vectors. In yet another aspect, the present disclosure relates to a method for preventing and / or treating a disease, comprising administering to a subject in need thereof an effective amount of a formulation described herein and a therapeutically effective amount of a lentiviral vector particle or lentiviral vector as described, wherein the disease is an immune disease (for example an auto-immune disease), cancer, genetic disease, allergic disease, inflammatory disease, infectious disease (in particular bacteria and / or virus infection), metabolic disease, neurological disease (such as neural dystrophy, Alzheimer disease, Parkinson disease, Huntington disease), muscular disease or any combination thereof. In some aspects, the formulations described herein and the lentiviral vector particle are administered simultaneously at the same time as a single composition. In other aspects, the formulation and the lentiviral vector particle are administered separately and sequentially and in any order. For example, in some aspects, the formulation described herein can be administered prior to or after the administration of the lentiviral vector particle or lentiviral vector. In some aspects, the formulation is administered at least 1 minutes, at least 2 minutes, at least 3 minutes, at least 4 minutes, at least 5 minutes, at least 6 minutes, at least 7 minutes, at least 8 minutes, at least 9 minutes, at least 10 minutes, at least 15 minutes, at least 20 minutes, at least 25 minutes, at least 30 minutes, at least 40 minutes, at least 50 minutes, at least 60 minutes, at 1.5 hours, at least 2 hours, at least 3 hours, at least 4 hours, at least 5 hours, at least 6 hours, at least 7 hours, at least 8 hours, at least 9 hours, or at least 10 hours prior to the administration of the lentiviral vector particles or lentiviral vectors. In other aspects, the formulation is administered at least 1 minutes, at least 2 minutes, at least 3 Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 minutes, at least 4 minutes, at least 5 minutes, at least 6 minutes, at least 7 minutes, at least 8 minutes, at least 9 minutes, at least 10 minutes, at least 15 minutes, at least 20 minutes, at least 25 minutes, at least 30 minutes, at least 40 minutes, at least 50 minutes, at least 60 minutes, at 1.5 hours, at least 2 hours, at least 3 hours, at least 4 hours, at least 5 hours, at least 6 hours, at least 7 hours, at least 8 hours, at least 9 hours, or at least 10 hours after the administration of the lentiviral vector particles or lentiviral vectors. Any suitable method of administration known from one skilled in the art may be used. The formulation and the lentiviral vector particle or lentiviral vector may be administered by the same or different routes. For example, the formulation and the lentiviral vector particle or lentiviral vector may be administered by the oral route, the parenteral route, the medullar route, in particular the intra-femur (such as in the bone marrow cavity) or humerus medullar route injection and / or local intra-tumor injection. Materials and Methods Cell Culture. SA13 cells, Isolated B cells, and PBMCs were cultured in IMDM with 10% Fetal Bovine Serum (FBS) at 37C and 5% CO2. LVMAX cells were cultured according to manufacturer’s specifications. B Cell Isolation from Peripheral Blood Mononuclear Cells. B cells were isolated from fresh PBMCs using the Dynabeads™ Untouched™ Human B Cells Kit using the manufacturers protocol. Following isolation, the B cells were cultured for 3 days in media supplemented with 55 uM 2-mercaptoethanol, 50 ng / mL IL-2, 50 ng / mL IL-10, 10 ng / mL IL- 15, 100 ng / mL soluble CD40 Ligand, and 1 ug / mL CpG oligodeoxynucleotide 2006. LV Pseudotyping Plasmids. The DNA encoding the LV pseudotyping proteins were produced similar to the plasmids described in (Bender et al. 2016, supra). Following initial cloning, blinding mutations described in (Bender et al.2016) were added. LV Production. Lentivirus were produced using the LVMAX lentivirus production cell line, and LVMAX chemical transfection kit. LV Purification. Lentivirus were purified using the following protocol: (1) At 48- 55 h post-transfection, LVMAX production cultures were transferred to 50 mL falcon tubes and were centrifuged (1,300 xg, 15 min). Supernatant from the cultures was collected and vacuum filtered using 0.45 uM 150 mL filter unit. (2) 10 mL of the filtered lentivirus supernatant was added into each pre-chilled 13.2 mL polypropylene Ultracentrifuge (UC) tube - six tubes total. (3) Slowly, 1.5 mL of cold sucrose cushion solution (25% sucrose, 2.5% HEPES (1M), 2.6% NaCl (5M)) was added directly to base of three UC tubes fully filled Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 containing 7.5 ml cold sucrose cushion solution. (4) UC tubes were transferred into the pre- chilled rotor buckets of the ultracentrifuge’s swinging-bucket rotor. (5) Lids were tightly screwed onto the rotor buckets and place onto pre-chilled rotor. (6) The vacuum on the pre- chilled ultracentrifuge was released. The rotor was carefully lowered into the ultracentrifuge. Any condensation from rotor chamber was wiped away. (7) Lentiviral supernatants were ultracentrifuged for 105 min at 91,000 × g, 4°C. (8) Rotor and buckets were removed. Contents of each UC tube were immediately poured into a waste container and then each tube was placed on ice. (9) A small pellet containing virus particles may be visible at the base of each tube. (10) 150 μl of cold cryoprotective solution (10% sucrose solution – made from diluting 25% sucrose solution in DI water) was added to each UC tube. UC tubes were placed in rack and rack was placed in refrigerator overnight. (11) 16 hours later, combine like lentivirus solutions and aliquot into PCR tubes for freezing. Place in -80C freezer for at least 2 hours before quantifying through qPCR. (12) Stored in at -80C until utilized. LV quantitation (qPCR). Lentiviral titers were determined from frozen (-80C) LV stock by using qPCR, using the Applied Biological Materials qPCR Lentivirus Titer Kit, following the manufacturers protocol. In Vitro Experimentation: SA13 and isolated B cell. Enhancer toxicity experiments were completed on SA13 cells across a range of concentrations for each enhancers. The cells were plated in 24 well, flat bottom plates at 100,000 cells / mL in experimental triplicates, confirmed by handheld cell counter. Cells were counted at 0, 12, 24, 48 and 72 hours. Effective values in combination were tested to determine enhancer combination effect on cell growth and cell viability, following the same protocol. For cell viability measurements, a life technologies Countess II was used with Invitrogen Trypan Blue Stain 0.4%, follow manufacturer’s use protocols.2 samples were taken from each experimental well (which were triplicates). Following toxicity experiments, experiments using all enhancer combinations with the CD20 targeting LVs were performed. The enhancer concentrations used in all experiments after the toxicity experiments were as follows: 5 ug / mL of Vectofusin-1, 150 ug / mL of Valproic Acid, 250 ug / mL of Poloxamer 407, 2 ug / mL of Rapamycin. For the isolated B cell experiments, B cells were isolated from fresh human PBMCs as described above. They were then incubated with the CD20 targeting LVs at an MOI of 1 - determined through qPCR tittering as described above – and the specific enhancers tested. The incubation occurred through spinoculation, at 34 C, 2400 RPM for 2.5 hours, with 20,000 B cells each. For the SA13 cells, an MOI of 4 was used to achieve appreciable levels of transduction in the no enhancer control group. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 Following spinoculation, the cells were washed 2x with cold, sterile PBS and media was replaced with fresh culture media without enhancers. Six days later, transduction efficiency was evaluated through GFP / RFP expression. For results, cells that were GFP+RFP+ were considered positive transduction events, an underreport due to the nature of 2A sequences. The data for GFP+% is reported in the supplemental figures. MFI was reported for GFP not RFP because of the lower RFP expression. A Dunett’s multiple comparisons test was performed for any statistical significance compared to no enhancer control. In Vitro Experimentation: PBMCs. In vitro experiments using fresh PBMCs were performed using 2 separate MOIs: a “Low MOI” representing an MOI of 1 based on B cells comprising 10% of the PBMC population, and a “High MOI” representing an MOI of 10. MOIs of 1 and 10 were chosen due to the MOI used on the isolated B cell population in FIG. 2, and expectations that transduction would be reduced in whole PBMCs versus isolated B cells. PBMCs from 3 donors were used for biological replicates. The experiment was set up in 2 separate 24 well, flat bottom, tissue culture treated plates, one for High MOI and the other for low. Each well contained 750,000 PBMCs in 800 uL of media, with the enhancers in their specified concentrations. The plates were spinoculated for 2.5 hours, 2400 RPM, 34 C. Following this, the wells were replated into a 96 well plate, washed with cold PBS, and media replaced with fresh media without enhancers. 4 days later, PBMCs were analyzed using flow cytometry. Flow Cytometry Quantitation: In Vitro. For in vitro flow cytometry labelling, CD20 Mouse Anti-Human Brilliant Violet 421 was used. Attune NxT was used to perform flow analysis. Used FCS Express 7 for computational work. Used Prism Graphpad for Statistical Analysis. In Vivo Experimentation. The in vivo experiments were set up using NSG mice, with 7 million live PBMCs per mouse. The MOIs in these experiments were standardized to the number of PBMCs, with an MOI of 0.3 used. Enhancer concentrations were determined based on the assumption of total distribution volume in the mouse as the total volume of blood, assumed to be 2 mL per mouse. The concentration of enhancers was the same as the concentrations used in previous experiments. On Day 0, 7 million live, fresh PBMCs from 3 different donors in 200ul total volume was injected intravenously. After 4 hours, the TEs and LVs were injected into the mice intravenously. Blood was harvested before injection as negative control. At Day 3, Day 7 and Day 14, blood was harvested for flow analysis. On day 15, blood was collected for final bloodwork and urinalysis. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 The in vivo study was conducted in 2 separate experiments. The first used 31 mice: 9 LV only, 3 negative controls with only PBMCs, 9 mice testing group 12, and 9 mice testing group 17, and 1 fully naïve mouse with no PBMCs. The second contained 10 mice: 3 LV only, 6 testing group 10, and 1 PBMC only. Both the first and second in vivo studies agreed with each other in terms of transduction rates of the LV only group. Separated out figures for each in vivo study are listed in the supplemental material. Each study was conducted identically. IUCAC protocol number 22-057. Flow Cytometry Quantitation: In Vivo.100 uL of blood was collected, processed, and the cells resuspended in 200 microliters FACS buffer. Attune NxT was used to perform flow analysis. Complete Bloodwork. The results of the complete bloodwork, performed on a ProCyte Dx, done on mice on Day 15 are described in FIG.6 and Example 5. Examples It will be readily apparent to those skilled in the art that other suitable modifications and adaptations of the methods of the present disclosure described herein are readily applicable and appreciable, and may be made using suitable equivalents without departing from the scope of the present disclosure or the aspects and embodiments disclosed herein. Having now described the present disclosure in detail, the same will be more clearly understood by reference to the following examples, which are merely intended only to illustrate some aspects and embodiments of the disclosure, and should not be viewed as limiting to the scope of the disclosure. The disclosures of all journal references, U.S. patents, and publications referred to herein are hereby incorporated by reference in their entireties. The present disclosure has multiple aspects, illustrated by the following non-limiting examples. Example 1 Toxicity of TEs in vitro. For each of the TEs, concentrations that can exert cellular stress or toxicity were identified, focusing on conditions that limited the growth of SA13 hybridoma cells over a 72-hour period, a more stringent criteria than concentrations that cause acute toxicity. Of the TEs tested, only P407 exhibited no effect on cell growth across all concentrations (FIG.1A). VF-1 significantly inhibited cell growth at >5 ug / mL (FIG.1B). By 48 hours, VPA slowed growth at all concentrations tested, with modest growth only observed at ≤150 ug / mL (FIG. 1C). Finally, rapamycin effectively inhibited cell growth at all concentrations tested. None of the TEs induced cell death or a reduction in cell counts, indicating their likely safe use with transient exposure. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 Informed by the TE screening, the specific concentration of each TE was determined to investigate further, individually and in combination. These included P407 at 250 ug / mL, VF-1 at 5 ug / mL, and VPA at 145 ug / mL, a concentration that facilitated enhanced transduction while not completely inhibiting cell growth. As Rapamycin essentially halted cell growth at all concentrations, 2 ug / mL was used for testing. The various TE combinations are listed in FIG. 1G. Example 2 TE-enhanced transduction of SA13 and primary B cells. The impact of including TEs on transduction was next evaluated, beginning with SA13 cells (FIGS.2A-2D). Over half of the TE combinations increased LV transduction of SA13 cells, as reflected by both an increase in mean fluorescence intensity (MFI) and the fraction of B cells that were positive for RFP. Among single TEs, only VF-1 markedly increased transduction of SA13 cells. Among combinations of 2 TEs, Group 10 (combination of P407 + VF-1) was the most potent at enhancing transduction. Groups 8, 9, and 12 enhanced transduction to a level similar to VF-1. Most of the 3 TE combinations demonstrated increases in both MFI and RFP+ cell fraction relative to no TE control (group 2), with the most potent combination (group 16 – VF-1, VPA, and Rapa) increasing the fraction of RFP+GFP+ cells by ~19 fold from ~1.5% to ~29%, and MFI increasing ~5.5 fold from ~1,800 to ~10,000. The “all” TE group (group 17) also saw similar increases, with ~ 30% of RFP+GFP+ cells and MFI increasing to ~9,300. Neither group 16 nor 17 were more potent than group 10 with only P407 and VF-1, which saw an increase of transduced cells to ~34% and MFI reaching ~12,800. The TEs in primary B cells isolated from human PBMCs were next tested. Similar trends of TE-enhanced transduction was noted, but the most potent TE combinations differed slightly. Among single TEs, VF-1 was again the only TE to appreciably enhance transduction compared to LV only control. Among the two TEs group, both Group 10 (P407 + VF-1) and Group 12 (VF-1 + VPA) saw improvement over LV only control, with ~29% and ~30% of cells transduced, respectively, and MFI reaching ~3400. Among groups with 3 TEs, Group 14 (VF-1, P407, Rapa) saw slightly greater transduction (cells transduced to ~32%) and MFI (to ~3700). The “All” TE group did not improve transduction further. While a number of combinations containing Rapa saw increased transduction, these groups also led to marked reductions in total cell counts (FIG. 1). For this reason, all two and three TE groups with Rapa were excluded from subsequent experiments on PBMCs and in vivo; rapamycin was only included in the four TE group. Among the 2 TE groups, many Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 exhibited potencies comparable to the 3 TE groups; Group 10 and Group 12 were advanced. Altogether, the following groups were advanced to the next study using whole PBMCs: 1 and 2 as controls, and 7, 10, 12, 13, and 17 as experimental groups. Example 3 TE-enhanced transduction of B cells in PBMCs. For in vivo transduction, B cells are specifically and efficiently transduced without first separating or activating the B cell populations. The direct addition of TE and LV combinations to whole PBMC populations was next evaluated (FIGS. 3A-3F). LVs were dosed at two LV to cell ratios (i.e. the ratio of the number of viral particles used to infect cells to the actual number of cells) with a multiplicity of infection (MOI) of ~1 and ~10 to total B cells assuming B cells comprised ~10% of the total PBMC population. The latter is equivalent to an MOI of ~1 based to total PBMC count. It was also noted that there were distinct populations of CD20+ cells in PBMCs: those expressing high levels of CD20, low but detectable levels of CD20, and non-detectable levels. Greater CD20 receptor expression was generally correlated to greater levels of transduction achieved: the CD20Highcell population saw rates of transduction that were 5-10 times higher than the CD20Lowpopulation, while the CD20Lowpopulation still saw rates of transduction about 20 times that of CD20- cells. For instance, Group 10 TEs coupled with LV at high MOI transduced ~20% of CD20High, ~2% of CD20Lowand ~0.1% of CD20- to express both GFP and RFP. The effect of TE on each of these cell populations was analyzed. Of the experimental groups tested, Groups 10, 12, and 17 performed the best: at low MOI, the fraction of transduced CD20Highcells increased from ~0.6% to ~3.3%, 1.8% and 6.1% respectively, while at high MOI the values increased from 3.1% to ~18%, ~12% and ~18%, respectively. MFI values achieved in CD20Highcells at high MOI also saw substantial increases, from ~550 with no TE control group, while to 3000, ~2000 and ~1700 for Groups 10, 12 and 17, respectively. The specificity of LV transduction was evaluated by analyzing the CD20- cell populations within the PBMCs (which represents up to 90% of the cells present). Not a single experimental data point showed more than 0.23% of the CD20- cells transduced. Additionally, there was virtually no difference in CD20- cell transduction across all experimental group, supported by the uniformity of the GFP MFI seen across all groups. Regardless of the TEs used, off target transduction was not increased, with the highest average off target transduction less than 0.1%. An on target: off target ratio of each condition was defined (FIG. 4). All TE combinations evaluated enhanced transduction of target cells without sacrificing the Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 specificity. No TE group exhibited lower on:off target ratios than the no TE control group; Group 17 at low MOI saw better specificity than no TE control. At high MOI, Group 12 afforded the best specificity. Based on these results, it was decided to advance Groups 10, 12 and 17 TEs into in vivo studies. Example 4 TE-enhanced transduction of B cells in vivo. To mimic clinical use where viruses are injected into individuals with circulating immune cells, human PBMCs were injected into NSG mice, followed by TE + LVs, LVs only, or PBS 4 hours later (FIGS. 5A-5D). Each experimental group included PBMCs from a minimum of 3 unique donors to account for biological variance. Blood was collected on Days 3, 7, and 14 to evaluate the fraction of circulating B cells transduced, and urinalysis and bloodwork on Day 15 for safety. Small differences in transduction were seen on day 3: while Group 2 saw an average of ~0.5% of CD20+ cells transduced, groups 10 and 17 saw ~ 1% of CD20+ cells transduced at this early timepoint. Greater difference emerged by day 7. Group 12 achieved the greatest transduction on Days 7 and 14, with 1.55% and 1.2% of the circulating B cells transduced representing a 3x and 2.5x improvement over group 2, and falling just short of statistical significance on day 14. Transduction mediated by group 10 TEs were also comparable to group 12. Incorporating rapamycin (group 17) did not appear to further enhance transduction. The TE and LV combination appears to preserve exceptional specificity of targeting: ~80% of all animals actually had no detectable GFP+ CD20- cells. An on target: off target ratio was not calculated. Antibody production by in vivo engineered B cells Mirroring the experimental procedure above, the levels of B cells transduced that could result in meaningful levels of protein production were examined. To do so, CD20- targeted NLV that encodes a neutralizing recombinant antibody against the RSV F protein in the form of scFv-Fc was used, and serum concentration of the secreted ScFv-Fc on days 3, 7, 14, and 26 was tracked via ELISA, as shown in FIG. 6. Low levels of the scFv-Fc antibody were detected across days 3-14, and by day 26 many of the mice exhibited micrograms / mL levels of ScFv-Fc in their serum (FIG. 6). In fact, both Group 7 (P407 + VPA) and Group 17 (all TE) possessed significantly higher levels of serum ScFv-Fc, with an average serum concentration >4 ug / mL, and the top performer >15 ug / mL (Figure 6). The level of scFv-Fc is ~1000-fold greater than the level of scFv-Fc observed in mice receiving CD20-targeted NLV Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 only. This underscores the inclusion of TEs in NLV formulations can dramatically increase protein production. Example 5 In vivo toxicity of TEs. Complete bloodwork and serum analysis was performed comparing the TE groups to naïve NSG mouse as well as published normal ranges for NSG mice (FIGS. 6A-6D). While Group 12 had a slight increase in level of ALT, the values were comparable to those from the PBS no virus control group, with each group having only 1 mouse above the normal ALT range. Multiple groups had ALT levels below the normal range, however the naïve control mouse also showed lower ALT. Groups 2, 10 and 12 all had slightly lower than normal AST levels. Group 12 also had levels of BUN slightly below the normal range – 12.7 vs. 15 mg / dL as the lower limit of normal. Beyond these, all other values fell within a normal range, and were comparable to the values collected in the naïve mouse. All mice had Urine Creatinine (UC) levels that were within the normal range of 0.2 – 0.6 mg / dL. Based on these data, it does not appear that the use of TEs elicited any kidney or liver toxicity. Example 6 TEs for Nipah-paramyxovirus-based LV In some cases, described herein are methods and compositions that may be particularly and surprisingly effective in enhancing transcription in vivo in paramyxovirus pseudotyped lentivirus (LV) and in particular in Nipah-paramyxovirus-based LV. For example, TE compositions including poloxymer P407 and peptide VF-1, either alone or in combination with other components (e.g., an HDAC inhibitor, a Blimp1 pathway blocker, rapamycin, etc.). In some cases the TE compositions may include poloxymer P407 and peptide LAH4, either alone or in combination with other components (e.g., an HDAC inhibitor, a Blimp1 pathway blocker, rapamycin, etc.). In some cases the TE compositions may include both LAH4 and VF-1 as well as poloxymer P407, either alone or in combination with other components (e.g., an HDAC inhibitor, a Blimp1 pathway blocker, rapamycin, etc.), including but not limited to VPA (valproic acid). Thus, in general, the methods and apparatuses may enhance transduction of a vector such as paramyxovirus pseudotyped lentivirus (LV) (and in particular in Nipah- paramyxovirus-based LV) that mediate transduction at the cell membrane level by using a cell penetrating peptide, such as VF-1 and / or LAH4 with P407 which may have beneficial Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 cell membrane level effects. Interestingly, other LVs that mediate transduction differently, such as LVs pseudotyped with Vesicular stomatitis virus glycoprotein G (VSV-G) do not see the high-levels of enhancement seen with LVs that mediate transduction through the cell membrane. Thus, in some cases LVs pseudotyped with surface proteins, so that their primary mechanism is by fusion with cell membrane (as opposed to more common delivery by endocytosis) such as pseudotyped lentivirus (LV) and in particular in Nipah-paramyxovirus- based LVs may be surprisingly effective in combination with TEs comprising a cell penetrating peptide, such as VF-1 and / or LAH4 with P407. For example, these compositions may include from about 0.1 µg / mL to about 100 µg / mL of at least one of VF-1 and / or LAH4 (e.g., from about 1 µg / mL to about 50 µg / mL, from about 1 µg / mL to about 30 µg / mL, from about 0.1 µg / mL to about 50 µg / mL, from about 0.1 µg / mL to about 25 µg / mL, from about 10 µg / mL to about 100 µg / mL, etc.) and from about 1 µg / mL to about 1000 µg / mL of poloxymer P407 surfactant (e.g., from about 1 µg / mL to about 800 µg / mL, from about 1 µg / mL to about 700 µg / mL, from about 1 µg / mL to about µg / mL, from about 10 µg / mL to about 1000 µg / mL, from about 10 µg / mL to about 800 µg / mL, from about 10 µg / mL to about 700 µg / mL, from about 10 µg / mL to about 500 µg / mL, from about 50 µg / mL to about 1000 µg / mL, from about 0.1 µg / mL to about 1000 µg / mL, from about 0.1 µg / mL to about 500 µg / mL, from about 0.1 µg / mL to about 250 µg / mL, etc.). In any of these examples, the surfactant (e.g., P407) may be in excess of the CPP (e.g., VF-1 and / or LAH4). For example, the amount of surfactant may be greater than 1.2x (e.g. greater than 1.5x, greater than 2x, greater than 2.5x, greater than 3x, greater than 3.5x, greater than 4x, greater than 4.5x, greater than 5x, greater than 10x, greater than 15x, greater than 20x, etc.) the amount of the CPP. In examples including VPA, VPA may be present in the TE from about 10 µg / mL to about 400 µg / mL (e.g., from about 20 µg / mL to about 400 µg / mL, from about 20 µg / mL to about 300 µg / mL, from about 20 µg / mL to about 200 µg / mL, from about 10 µg / mL to about 300 µg / mL, from about 10 µg / mL to about 200 µg / mL, etc.). The composition of the TE used may depend upon the cell type. For a TE composition for use with B cells and paramyxovirus pseudotyped lentivirus (LV) (and in particular in Nipah-paramyxovirus-based LV), may include P407 and VF-1 and / or LAH4. In some cases a TE composition for use with B-cells and paramyxovirus pseudotyped lentivirus (LV) (and in particular in Nipah-paramyxovirus-based LV)may include P407 without a CPP, such as P407 and valproic acis (VPA). In some cases either VPA or a CPP (and specifically VP-1 and / or LAH4) may be exclusive, such that either VPA or the CPP may be used with P407, particularly when used with B cells. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 For a TE composition for use with T cells and paramyxovirus pseudotyped lentivirus (LV) (and in particular in Nipah-paramyxovirus-based LV), may include P407 and VF-1 and / or LAH4, either exclusively or in combination with an HDAC inhibitor, a Blimp1 pathway blocker and / or an mTOR) inhibitor (e.g., rapamycin). While a number of ex vivo engineered T cells (e.g. CAR-T) have received FDA approval, with many more undergoing clinical development, there are far fewer efforts advancing engineered B cells into clinical study. This reality underscored both the difficulty in manufacturing large quantities of B cells ex vivo, and the inherent challenges associated with transducing B cells, both in vitro and in vivo. Most efforts attempt B cell manipulation in vitro through electroporation. Indeed, recent work using an optimized AAV system achieved transduction of ~0.5% total blood B cells but required both B cell activation from pre- immunization as well as very high viral titer (5E11 vg). The lack of suitable vector systems that can efficiently and specifically deliver target transgene into B cells has greatly limited potential B cell applications to date. The compositions and methods described herein may further optimize transduction enhancers (TEs) that may be particularly useful for Nipah-paramyxovirus-based LVs that may be of particular use. For example, the unique TEs described herein demonstrated markedly enhanced direct in vivo transduction of B cells with Nipah-paramyxovirus-based LVs, achieving thresholds that substantially exceed what have been previously reported. For instance, TEs including P407 and VF-1 and VPA increased B cell transduction by as much as 3x in vivo, inducing GFP expression in ~1.5% of all circulating B cells. Further, these TEs appeared to fully preserve the specificity of the LVs, require a relatively very low dose of virus (>5-log less than AAV), and does not require pre-activation of the B cells. The results from a study of in vivo ScFv-Fc secretion further validated the findings from the in vivo GFP expression experiments, and demonstrated how TE-mediated enhanced transduction can yield profound differences in secreted proteins in the circulation. These results underscore the promise of combining TEs with CD20-targeted LVs as a platform for direct in vivo reprogramming of B cells. Given the paucity of engineered B cells that have advanced into clinical development to date, there is limited direct evidence substantiating the minimum threshold of engineered B cells needed. Nevertheless, based on earlier studies utilizing a less potent AAV at MOI ~ 1,000,000, ~0.5% of circulating B cells transduced led to serum levels of a knocked-in mAb that were comparable to those achieved via infusion of B cells engineered ex vivo reaching low single digit ug / mL that were sufficient to protect against infection. By Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 day 26 in the in vivo ScFv-Fc secretion experiment, >2.5 ug / mL average serum concentration was achieved for 3 of the 4 TE groups despite the use of 100,000 lower MOI, a level likely to be sufficient to protect against infection. This is more than 12x the average of ~200 ng / mL in the No Enhancer LV only control group. Therefore, the level of transduced B cells achieved in the TE groups is highly likely be physiologically relevant. The TE compositions and method of use described herein may be used for in vivo use and / or in ex vivo CAR-T manufacturing, and may enhance in vitro transduction. The combinatorial screening of different TEs described herein allowed the identification of synergies that would be difficult or impossible to predict theoretically that confer effective transduction in vivo. The TEs described herein may be safely used in humans. For instance, P407 is in the Inactive Ingredient Database of the FDA and is used in the FDA-approved surgical gels and numerous ophthalmic products. VPA is a commonly used drug in patients with bipolar disorder and epilepsy, but at much higher doses than what was explored here. Rapamycin was initially discovered as a promising antifungal agent and is now ubiquitously used as a potent immunosuppressant and strong anticancer drug. As described herein, TE-treated mice had no toxicology markers that significantly deviated from naïve mice receiving PBS. Further, also described herein are in vivo use of TEs: when infused systemically along with the LV, they are already at the highest concentrations directly in the proximity of target cells (e.g. B cells in the blood). In turn, this should enhance transduction to the maximum extent possible over the short time frame that it typically takes for a paramyxoviral vector to bind and fuse with target cells. The large volume of distribution in the body, coupled with renal excretion, will result in relatively quick dilution to safe thresholds. This is in contrast to the ex vivo use of TEs where TEs may be maintained at their input concentrations long after the viral vector has successfully delivered the transgene. Thus, there is a sufficient large therapeutic and safety window to ensure the safe and effective use of TEs. Example 7 NLV + TE: a new efficient and targeted LV system. To enable in vivo CAR-B engineering, LV must be able to transduce circulating B cells in their native states. An LV mechanism of transduction relying on direct fusion of the LV at the plasma membrane level and Nipah-based LV (NLV) was focused on. B cells specificity was conferred by a single- chain antibody fragment (scFv) against CD20 grafted to the exposed C terminus of the G. To further improve the transduction efficiency in non-activated T cells, a library of transduction Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 enhancers (TE) was tested (FIG.8). Several TE combinations that markedly enhanced the transduction potencies of the NLV, reproducibly transducing >25% of the primary B cells were identified. The combination of VPA and vectofusin-1 (VF-1) for in vivo testing was elected, due to both the consistency of transduction, minimal off-targeting, and no observable toxicity. For every one off-target GFP+ cell detected in PBMC, >100 CD20+ B cells were transduced. Example 8 In vivo validation of targeted B cell transduction by LV+TE. As a proof-of- concept that TE can enhance transduction of circulating B cells in vivo, a pilot study was performed where NSG mice with human PBMCs injected 30 mins prior were given CD20- targeted NLV, with and without TE. Despite the fact that B cells represent a minority population within PBMC (there are far greater abundance of T cells), and without any antigen stimulation, ~0.6% of circulating B cells were transduced (GFP+) on Day 7 (FIG.9A). TE was used in achieving the observed level of transduction. Limited off-target transduction was demonstrated despite the greater abundance of CD3+ and CD14+ immune cells the PBMC (FIG.9B). Example 9 Evaluation of protection against RSV infection in NSG mice infused with human PBMC. RSV infections cause substantial pulmonary pathology in NSG mice infused with human PBMCs. PBMCs containing human B cells can be reprogrammed in vivo to secrete sufficient amounts of, e.g., MEDI-8897 to protect against RSV infection. An NLV systems as described herein may be used. The level of agent, e.g., MEDI-8897, in the serum over time, as well as quantify viral titers and pulmonary pathology may be assessed. In one example, RSV may be used as a proof-of-concept. MEDI-8897 is effective (~70% protection) in preventing RSV infections, unlike MEDI-8852 or other influenza- binding mAbs. A suitable mice model for HIV infection will require immunodeficient NOD / SCID / γc mice engrafted with human CD34+hematopoietic stem cells (hu-CD34 NSG) which is expensive. In contrast, the focus on assessing protection against RSV using a less expensive NSG mouse model may enable direct evaluation of in vivo transduction of circulating human B cells in a physiologically-relevant setting. RSV produces both high pulmonary viral titers and substantial pulmonary pathologies in NSG mice, making it highly suitable to assess the effectiveness of CAR-B mediated protection. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 In all mice studies, PBMCs (tail vein IV; 5×106PBMCs in 150 μL sterile PBS) may be first injected into mice, followed by different NLVs + TEs 30 minutes later. Then (1) PBMCs only, (2) NLV+TE encoding for non-specific integration of MEDI-8897, and (3) NLV+TE encoding for site-specific MEDI-8897 integration may be tested in one prophetic example. Infused human B cells may survive for >21 days in NSG mice. Thus, collection of serum may be sought weekly to assess MEDI-8897 levels over at least a 3 week duration (via RSV-F protein ELISA). The goal is to achieve >1 μg / mL MEDI-8897, which is >100-fold greater than its averaged IC50 against a broad panel of RSV A and B strains. Dose-finding studies were first performed (n=6 mice per group, 3M / 3F). Based on the concentrations of MEDI-8897 and fractions of transduced B cells detected, either the amount of viral titer to be dosed was adjusted or additional rounds of NLV+TE dosing if necessary may be performed. In an RSV challenge study, mice (n=16 mice per group, 8M / 8F) were injected with human PBMCs followed by NLV+TE as identified in the dose-finding studies, or PBMC only. One week later, the mice were challenged intranasally with replication-competent RSV (Viratree; 106PFU in 50 μL PBS per mouse). Weekly blood samples (~100 μL) were collected retro-orbitally to measure MEDI-8897 serum concentrations (ELISA). On Day 7 and 14 post viral inoculation, 8 animals per group may be sacrificed to assess viral load in both BALF (collected by intratracheal instillation and aspiration of 0.5 ml PBS) and lung tissue homogenates by qPCR and infectious viral titers. RSV titers may be quantified by standard plaque assays and expressed as the number of PFU per lung. In the repeat study, 4 animals for each time point were added, sacrificed on Day 7 and 14 to assess pulmonary pathology / inflammation of lung tissues by histology. Histologic sections may be used to determine: (i) the distribution of virus-infected epithelial cells by IHC and in situ hybridization (RNAScope); (ii) epithelial cell cytopathology and inflammation (morphometry) for ADE; and (iii) the mucin composition of mucus secretions (IHC). Immunodetection of virus infection will use antibodies against GFP, the specific viral antigen, and RNAScope. Airway inflammation are scored histologically on a scale of: 1 (none); 2 (minimal); 3 (moderate); and, 4 (severe). Finally, the numbers of epithelial cells (sloughed cells) from cytospins of BALF, and inflammatory cell counts for macrophages, neutrophils, eosinophils and lymphocytes (Cytospin) were quantified. Expected Findings: (i) it is anticipated that the use of TE leads to markedly greater transduction and correspondingly much greater CAR-B cells in the circulation and much higher serum levels of MEDI-8897; (ii) it is expected that NLV+TE afford effective protection against RSV infections. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 Statistical Considerations: Assuming 75% reduction in viral burden and typical variations observed with prior RSV animal studies, the proposed sample size (n=8 per group at each time point) enables evaluation of statistical significance at an α of 0.05 and power of at least 80%. Due to the need for animals for lung and nasal tissues for histology, it is anticipated that 12 animals per group at each time point are sufficient to differentiate interventions. All post-mortem data is assessed by one-way ANOVA with Tukey’s post-test. All clinical data is assessed by two-way ANOVA, and cumulative weight change is assessed by one-way ANOVA with Tukey’s post-test. To ensure reproducibility, at least 2 independent studies are conducted. Pitfalls & Alternative Strategies. Major problems are not expected in accomplishing the experiments, in successfully generating edited B cells that respond to antigen stimulation, or in performing a variety of RSV animal studies. If it is not possible to achieve high titers of MEDI-8897 with conventional IgG1-Fc, Fc with increased affinity to FcRn (e.g. YTE or LS mutations) will be engineered; the prolonged circulation is expected to further boost the steady state level of serum MEDI-8897. Delay of the start of the viral challenge is also possible to afford more time for secreted mAb to accumulate in the circulation. If substantial RSV infection is not observed in the control group (possibly due to presence of RSV-specific CD8+ T-cells in the PBMC), purified B cells will be injected into mice rather than whole PBMCs. Example 10 NLV + TE: a new efficient and targeted LV system. To enable in vivo CAR-T engineering, it is believed that LV can transduce T-cells without first stimulating / activating the T-cells. Despite the promising findings with mSindbis-LV in vivo, it was not possible to efficiently transduce resting T-cells present in PBMCs. Similar limitations were seen with VSV-G pseudotyped virus. A major reason is because T-cells (as well as B-cells) in the circulation (non-activated T-cells) do not readily undergo endocytosis. The mechanism of gene transfer with Sindbis and VSV-G involves endocytosis followed by endosomal escape. Thus, LV where the mechanism of transduction relies on direct fusion of the LV at the plasma membrane level, including both Measles virus (MLV) and Nipah virus (NLV) based LV was pursued. In both, T-cells specificity was conferred by a single-chain antibody fragment (scFv) against CD3 grafted to the exposed C terminus of the fusion protein. To improve the transduction efficiency in non-activated T cells, a library of transduction Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 enhancers (TE) was tested, and the combination of poloxamer 407 (P407) and vectofusin-1 (VF-1) was selected. CD3-targeted NLV and MLV was tested at different MOI (multiplicity of infection) in non-stimulated PBMCs, with and without P407 and VF-1 individually or in combination. Without TE, neither MLV nor NLV transduced appreciable population of non- activated PBMC (FIGS.11A-11C). However, the combination of P407+VF-1 markedly improved transduction of resting T-cells, particularly with NLV where an average of 2.5% and 6% of total T-cells were positive for GFP at MOI of 10 and 50, respectively (FIG.11C). Importantly, no obvious off-target effects with the combination of MLV / NLV with TE (we measured GFP expression in both CD3+ and CD3- cells in PBMC) were observed. In fact, the TE appeared to further reduce potential off-targeting at the highest MOI used, possibly by enabling more efficient transduction of CD3+ vs. CD3- cells. For every one off-target GFP+ cell detected in PBMC, >322 CD3+ T-cells were transduced. These results underscore the exceptional transduction efficiency and specificity with the TEs described herein, and also the importance of the use of TE (e.g., NLV on its own is inadequate). Example 11 In vitro characterization of CD19.CAR delivered by LV+TE. Whether NLV- CD3 can produce CAR-T cells expressing CD19-CAR was next evaluated. Comparable CAR expression (FIG.12A) as with an earlier GFP study (FIGS.12A-12B) was demonstrated. To test the activity of the CAR-T cells, a co-culture experiment with transduced non-activated PBMCs and human leukemia cell line BV-173 was performed. CD19.CAR delivered by NLV or Measles virus pseudotyped lentiviral vector (MLV) alone (i.e., without TE) resulted in minimal BV173 killing. In contrast, effective elimination of BV173 cells was achieved by otherwise unstimulated PBMCs receiving CD19.CAR delivered by either MLV or NLV (FIG. 12C) together with transduction enhancers (i.e., NLV+TE). Importantly, the data directly demonstrates that the specific TE cocktail for improving transduction is effective for two distinct paramyxovirus family, indicating it can broadly enhance transduction of viral vectors that mediate delivery by direct fusion with plasma membrane without endocytosis. Furthermore, these data demonstrate the feasibility of effective engineering of CD19.CAR T- cells directly from non-activated PBMCs. Furthermore, no significant toxicity of the LV system was shown with enhancers despite extensive incubation. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 Example 12 Characterization of in vivo engineered CD19.CAR-T cells. Unlike ex vivo engineered T cells, in vivo engineered CAR-T cells is expected to better mirror the physiologic T-cell responses in which a small number of antigen specific T cells can expand exponentially upon encountering the cognate antigen, as in vivo engineered T cells are less exhausted and can exploit their intact functional capacities. A single dose of the NLV + TE administered in vivo generated markedly more CAR.CD19-T cells than the NLV without enhancers (FIGS.15A), reaching ~7% of total T cells in blood. This modest number of CAR.CD19-T cells was nonetheless more than adequate to essentially eliminate the highly aggressive BV173 tumor (FIGS.15E, compared to FIGS.15B). Importantly, TE was essential in achieving the observed anti-tumor effect; in animals receiving the same dose of the NLV without enhancers (FIGS.15D), far less suppression of the tumor burden. Furthermore, whereas there was substantial tumor burden in the bone marrow and spleen in control animals, no detectable tumor burden in those organs was found in animals treated with NLV+TE (flow cytometry; data not shown due to space constraints). These results support the notion that a small number of in vivo engineered CAR-T cells can mediate highly effective therapy. Additional characterization of the in vivo engineered CAR-T shown in FIGS. 15A- 15E was performed. As the therapy eliminated all detectable signs of tumors, it was not possible to quantify the number of CAR-T cells in the tumor. Instead, it was possible to detect appreciable CAR-T among CD3+ T cells in both the spleen (FIG.13A) and bone marrow (FIG. 13B). Essentially no CAR expression above background was found among all CD3-negative cells in the blood (FIG.13C) and in spleen (FIG.13D). Preliminary phenotypic characterization of NLV+TE induced CAR-Ts was also performed. Appreciable levels of both CD4+ and CD8+ CAR-T cells in the blood (FIG. 13E), spleen (FIG. 13F) and bone marrow (data not shown) were found. Finally, among these in vivo engineered CAR+ T cells (CD3, CD4 and CD8), substantial T central memory (TCM; CD45RA-, CCR7+), T effector memory (TEM; CD45RA-, CCR7-), effector memory cells re-expressing CD45RA (TEMRA; CD45RA+, CCR7-), and naïve T cells (TNaïve; CD45RA+, CCR7+) were found (FIG. 14). Assessment CAR-T cells and off- targeting was be performed by qPCR, as well as evaluation of memory and extent of T cell exhaustion. Characterization of in vivo engineered B7-H3.CAR-T cells. As illustrated in FIG.17, NLV+TE can generate B7-H3.CAR-T that eradicates non-small cell lung cancer (NSCLC) cells. CAR activity was achieved by adding NLV encoding B7-H3.CAR, with and Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 without TE, to whole PBMCs (i.e., without any other activation) at a MOI of 10. The PBMCs were mixed with A549 cancer cells at PBMC:tumor cell ratio of 1:2 (assuming 50% T cells and 5% transduction, this is equivalent to an E:T ratio of 1:80). The number of tumor cells vs. T cells was quantified by flow cytometry 5 days later. As shown in FIG.21, TE dramatically improved B7-H3.CAR killing and virtually eliminated all A549 cells despite a very low ratio of E:T cells vs. typical ratios used in co-culture studies with ex vivo engineered CAR-Ts. Importantly, NLV alone and conventional VSV-G LV were both ineffective in generating active B7-H3.CAR-T cells when dosed to non-stimulated PBMC. Equally importantly, TE did not enhance VSV-G LV transduction of T cells, as reflected by the lack of B7-H3.CAR-T cells that were generated and thus lack of A549 killing in PBMCs receiving VSV-G LV together with TE. Together with earlier data (FIGS.12C) that demonstrates TE enhances NLV, this indicates that the enhancement effect is achieved only with viral vectors that achieve membrane fusion without endocytosis (notably, VSV-G pseudotyped LV requires endocytosis for delivery of its genetic cargo). NLV was then tested in a pilot study of metastatic human NSCLC. Whereas mice given PBMCs alone all died by Day 24, those given PBMCs then NLV+TE (MOI: 25) eliminated nearly all traces of NSCLC, as Shown in FIGS.18A-18C. NLV alone offered only limited protection: 2 of 5 mice died by Day 24. The difference in efficacy is consistent with a greater number of circulating B7-H3.CAR-T cells in the NLV+TE group (data not shown). The mice were rechallenged with the same NSCLC cells; those treated before with NLV+TE effectively eliminated all cancer cells from the rechallenge. These results are consistent with our earlier work with B7-H3.CAR-T against NSCLC. Thus, the examples shown in FIGS.18A-18BD illustrate the use of a TE (e.g., P407 and LV-1) to specifically enhance Nipah pseudotyped lentiviral vector (NLV) transduction of circulating CAR-T cells in an in vivo assay with NLV delivering the B7- H3.CAR gene to mice implanted with metastatic NSCLC. With this TE, NLV+TE mediated transduction to generate B7-H3.CAR-T cells in situ led to both smaller tumor volumes (as reflected by reduced tumor-associated bioluminescence (BLI)) but also improved survival in the animals compared to not just saline control but importantly also against NLV only control. This was true not just against the initial tumor but also against a subsequent rechallenge with NSCLC. An orthotopic NSCLC model also showed a clear distinction in anti-tumor activity of in situ engineered B7-H3.CAR-T based on NLV vs. NLV+TE. NLV alone did not generate sufficient CAR-T cells to eradicate the primary tumor, whereas the greater number Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 of B7-H3.CAR-T achieved with NLV+TE led to essentially complete eradication, as shown in FIGS.19A-19B. Altogether, these results underscore the ability to effectively transduce non-stimulated PBMCs and generate CAR-T in situ, even prior to rigorous optimization efforts, using the transduction enhancers described herein. The more effective suppression of NSCLC tumor growth was directly a consequence of greater number of CAR-T cells (as well as greater fraction of T cells that are B7-H3.CAR-positive) in the circulation, resulting in overall greater anti-tumor activity. The greater abundance of B7-H3.CAR-T cells in the NLV+TE group relative to NLV alone group was seen at the study end point, and in both the blood as well as the spleen. A possible reason to the enhanced killing of the NSCLC by B7-H3.CAR-T cells engineered from NLV+TE is that the improved transduction reduces the exhaustion of the T cells. At the time of sacrifice, consistently lower levels of Lag-3 were seen in the B7-H3.CAR-T cells from animals receiving NLV+TE than from animals receiving NLV alone. Example 13 NLV-generated B7-H3.CAR-Ts effectively killed human Panc-1 PDAC. Generation of functional B7-H3.CAR via the NLV was confirmed by performing a co-culture of transduced PBMCs with tumor cells. On Day 0, NLV (encoding the corresponding B7- H3.CAR with either the CD28 or 4-1BB endodomains) was added, with and without TE, to whole PBMCs (i.e. without any activation) at a MOI of 25. Then 4 days later, after changing media to remove residual TE, the PBMCs and Panc-1 PDAC cancer cells were mixed at PBMC:tumor cell ratio of 1:2 (assuming 50% T cells and 5% transduction, this was roughly equivalent to an E:T ratio of 1:80). Then, 5 days, later, the fraction of tumor cells vs. T cells was quantified by flow cytometry. As shown in FIGS.16A-16B, the presence of TE was able to improve the generation of B7-H3.CAR among the PBMCs leading to markedly lower fraction of tumor cells remaining. This reduction in Panc-1 cells despite a likely very low number of B7-H3.CAR-T cells was seen when compared to typical ratios used for assessing ex vivo engineered CAR-Ts. These results confirm that it is possible to generate the NLV necessary to test NLV+TE induced B7-H3.CAR-T vs. conventional CAR-T in (A) orthotopic TNBC patient-derived xenografts (PDX), and (B) orthotopic Panc-1 pancreatic ductal adenocarcinoma (PDAC). Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 Example 14 In vivo validation of targeted transduction by LV+TE. As a proof-of-concept that TE can be used in vivo, a pilot study where NSG mice with human PBMCs injected 30 mins prior were given CD20-targeted NLV, with and without TE was performed. Despite the fact that B-cells represent a minority population within PBMC (there are far greater abundance of T-cells than B-cells), and without any antigen stimulation, it was possible to transduce ~0.6% of all B-cells. TE was used in achieving the observed level of transduction. Limited off-target transduction despite the much greater abundance of CD3+ and CD14+ immune cells in PBMC was shown. These results underscore the potential of combining TE and CD3-targeted NLV for in vivo engineering of CAR-T cells. Example 15 Testing for possible TEs. A variety of possible compositions for transduction enhancers were examined and optimized. For example, table 2, below lists putative transduction enhancer components that were evaluated as described herein for use with paramyxovirus pseudotyped lentivirus (LV), such as Nipah-paramyxovirus-based LV. # Enhancer component Highest conc. Lowest conc. Highest non- (toxicity screen) (toxicity screen) toxic dose Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 As mentioned above, the methods and apparatuses described herein may be selected to specifically work with both B cell and T cells. In addition, these TEs may be selected and configured (e.g., have concentrations) that allow effective and efficient enhancement of paramyxovirus pseudotyped lentivirus (LV) and in particular in Nipah- paramyxovirus-based LV particles. Not all putative transduction enhancers work, including those shown in the table above, either alone or in combination. For example, Tubacin and L5257 heptadecanoyl appear to negatively impact the either VF-1 and P407 alone or in combination in both cell lines and PBMC. A toxicity screen was performed to determine the highest non-toxic concentration of potential transduction enhancers / components (TEs), listed in the table above. The toxicity screen was conducted on SUP-T1 cells. Fifteen enhancers were tested (listed in the table as #1-15), including cell-penetrating peptides (CPPs: LAH4, LEPTIN30, APOE, Vectofusin-1), HDAC inhibitors (MS-275, Tubacin, Valproic acid, SAHA, Panobinostat), mTOR inhibitors (Rapamycin, Metformin), and surfactants (L5257 heptadecanoyl, P407, P188, P403). Enhancers (e.g., components of enhancer formulations, such as CPPs) were initially tested at their highest soluble or known toxic concentration, followed by a 1:3 serial dilution to generate five concentrations in total. SUP-T1 cells were incubated with each concentration for 48 or 72 hours in a 48-well plate format (550 µL per well, including cells and enhancer). Cell viability was assessed using the Millipore Scepter 3.0 Handheld Automated Cell Counter (cell number as a proxy for viability). The highest concentration that did not significantly reduce cell viability was selected as the non-toxic dose for each enhancer and used in subsequent transduction experiments. Lentiviral Transduction For transduction, a lentiviral vector (LV) pseudotyped with truncated Nipah F and CD3-targeted G proteins was used, carrying a GFP reporter gene under control of the E1a promoter. SUP-T1 or PBMC cells were seeded in a 96-well U-bottom plate at a density of 5 × 10⁴ cells per well in a total volume of 200 µL. Enhancer combinations were added to the lentivirus and incubated for 10 minutes at room temperature before adding the mixture to cells (MOI=15, based on qPCR titration). Following transduction, cells were incubated at 37°C, and the media was refreshed after 24 hours. Flow cytometry was performed on day 5 post-transduction to assess GFP expression, with GFP-positive cells indicating successful transduction. A live / dead stain was used to assess cell viability. For some PBMC experiments, anti-CD4 and anti-CD8 antibodies were included to identify and analyze T-cell populations. Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 A Design of Experiments (DOE) approach was used to screen combinations of the 15 TEs in SUP-T1 cells for optimal enhancement of lentiviral transduction. The DOE was designed using JMP Custom DOE software, with a total of 45 experimental runs, allowing up to 4 enhancers per condition to streamline the screening process. This is schematically illustrated in FIG.20A. Enhancers (or components of enhancers) were tested at their highest non-toxic dose as determined in the toxicity screen. Each experimental run featured different combinations of TEs, and the DOE design was optimized to assess individual and interactive effects of each TE. A secondary DOE screen was conducted to refine the concentrations of the top five enhancers identified in the initial screen, testing high, medium, and low doses of each. This secondary screen was aimed at determining the optimal combination and concentration of TEs for maximizing transduction efficiency. FIGS.20B-20D show a SUP-T1-Based DOE Screening Strategy for Optimal Transduction Enhancer (TE) Cocktail Selection for CD3-Targeted Nipah Lentiviral Vector (NLV). To identify the most effective transduction enhancers (TEs) for CD3-targeted Nipah Lentiviral Vectors (NLVs), a systematic Design of Experiments (DOE) screening approach in SUP-T1 cells. This two-tiered strategy initially tested 15 TEs at their highest non-toxic concentrations, followed by a second stage where the top 5 candidates were assessed at three dose levels. This approach ensured diversity by including enhancers from different categories (e.g., cell-penetrating peptides, surfactants, and small molecules) while narrowing down the most promising candidates for optimization. Transduction efficiency was quantified as the percentage of GFP-positive cells (%GFP+), revealing that several TEs significantly enhanced transduction. FIG.20B highlights the individual contributions of each TE, showing that some candidates consistently performed better, even in combination. FIG.20C narrows the focus to the top 5 TEs, showing their performance at varying concentrations, with TE #13 selected over TE #14 for further analysis due to their similar effects. Statistical analysis (FIG.20D) revealed that LAH4 (TE #1), P407 (TE #13), and VF-1 (TE #4) significantly improved transduction efficiency, forming the basis of a refined TE cocktail for subsequent optimization. FIGS.21A-21D illustrate PBMC-Based DOE Screening Strategy to Identify Optimal TE Cocktail for CD3-Targeted NLV in Primary Immune Cells. To confirm findings in a more physiologically relevant system, the same DOE methodology was applied to primary peripheral blood mononuclear cells (PBMCs), as shown in FIG.21A. PBMCs, representing a mixed population of immune cells, provided a more complex context for evaluating transduction efficiency. FIG.21B shows the transduction rates (%GFP+) for the Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 15 TEs tested in combinations of three to four per condition, revealing trends similar to those seen in SUP-T1 cells, with several TEs significantly enhancing transduction. The individual contributions of each TE in PBMCs are displayed in FIG.21B, confirming that certain enhancers were the top contributors to transduction efficiency, including P407 (TE #13) and LAH4 (TE #1), which were identified as the most potent in PBMCs. Interestingly, TE #4 did not show the same significant enhancement as it did in SUP-T1 cells. FIGS.21C and 21D reinforce these findings, showing clear statistical significance for the top enhancers. The successful validation of these TEs in PBMCs strengthens the translational potential of the LAH4, P407, and VF-1 cocktail, highlighting their applicability not only in cell lines but also in primary human immune cells. Notably, despite the fact that at these concentrations TE#1 did not appear as promising, it was advanced into the final screen across a wider range of concentrations. FIGS.22A-22B illustrate final Characterization of NLV Transduction in CD3+ T Cells in PBMCs with Varying Concentrations of VF-1 + P407 or LAH4 + P407, with and without Metformin. Building on the findings from the SUP-T1 and PBMC screens, the functional impact of the optimized TE cocktails on CD3+ T cell transduction in PBMCs was further characterized, focusing on CD4+ and CD8+ T cell subsets. FIG.22A and 22B show data on transduction rates for these subsets using varying concentrations of the VF-1 + P407 or LAH4 + P407 cocktails, with and without metformin, a potential adjunct enhancer. Both VF-1 + P407 and LAH4 + P407 exhibited similar success across CD4+ and CD8+ subsets, with VF-1 + P407 showing higher transduction rates overall. The addition of metformin did not significantly boost transduction in either subset, suggesting it does not enhance the effect of the TEs. These results highlight the similar efficacy of the TE cocktails across diverse T cell populations, with VF-1 + P407 emerging as the most promising candidate for optimizing NLV transduction in CD3+ T cells. FIG.22c is a table showing the various TE formulation compositions with example concentrations. FIG.23 improved CD19 CAR-T Cell Generation and Anti-Cancer Efficacy with P407 + VF-1 TE Cocktail. The functional implications of the P407 + VF-1 TE cocktail was evaluated on the generation and anti-cancer efficacy of CD19-targeted CAR-T cells. FIGS. 23A-23B shows data on the cytotoxicity of CAR-T cells generated with the P407 + VF-1 cocktail, assessing their ability to kill Daudi cancer cells at two time points: 2 and 4 days post-transduction. The results demonstrate a significant improvement in both CAR-T cell generation and their cancer-killing ability, with cytotoxicity notably higher at 4 days, suggesting that the P407 + VF-1 cocktail not only enhances initial transduction but also Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 supports the expansion and sustained functionality of CAR-T cells. This increase in anti- cancer activity over time underscores the therapeutic potential of the P407 + VF-1 cocktail, highlighting its ability to generate potent CAR-T cells with robust anti-cancer effects, making it a promising candidate for clinical applications targeting CD19-expressing cancers. The toxicity screen of the 15 components of transduction enhancers (TEs) at five concentrations in SUP-T1 cells revealed dose-dependent inhibition of cell number growth (a highly sensitive proxy for toxicity) for several enhancers. Poloxamers, particularly P407 and P188, showed no toxicity at the highest concentration tested (200 µg / mL), while some peptides and HDAC inhibitors exhibited increased toxicity at lower doses. These results provided essential information on safe dosing ranges, which were used to guide the selection of concentrations for subsequent transduction screens. FIGS.24A-24E illustrate GFP and Toxicity Results from SUP-T1 DOE Screen. The initial DOE screen in SUP-T1 cells demonstrated that combinations containing LAH4, P407, and VF-1 significantly increased GFP expression while maintaining low toxicity. JMP analysis confirmed the positive impact of these TEs. GFP expression was directly correlated with enhanced transduction efficiency, and the low toxicity levels across conditions ensured the safety of these combinations. FIGS.25A-25D shows: GFP and Toxicity Results from PBMC DOE Screen. In the PBMC DOE screen, TEs such as P407, LAH4, and VF-1, both individually and in combination, led to significant increases in GFP expression with minimal toxicity. JMP analysis identified that combinations like VF-1 with Metformin and VF-1 with P407 had substantial transduction-enhancing effects. These results were pivotal in confirming safe and effective TE conditions for primary T-cell transduction in PBMCs. FIGS.26A-26C illustrate the CD4+ and CD8+ T-cell Transduction Phenotype in PBMCs. Post-transduction analysis of PBMCs revealed that TE treatments did not alter overall CD4+ or CD8+ cell proportions, indicating that the transduction process specifically targeted CD3+ T-cells without affecting other immune subsets. As shown in FIGS.26A-26C, GFP expression confirmed efficient transduction, ensuring the specificity and safety of the TE combinations in targeting T-cells. The methods described herein may be used in vivo to treat a patient, and / or in vitro. As mentioned, FIGS.23A-23B show the results of the addition of a TE formulation of P407 and VF-1 (with an excess of P407) markedly improved the generation of CD19.CAR-T cells resulting in more effective killing of Daudi cancer cells. Similar results were seen when screening various TE combinations, as shown in FIGS.24A-24E, for SUP-T1 cells, and in Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 FIGS.25A-25E for PBMCs, with the greatest effect consistently seen in TEs including both VF-1 and P (TE 13). Example 16 In any of the TE compositions described herein, the cell penetrating peptide (CPP) may be an LAH4 peptide. However, the end-cap modification on the LAH4 peptide may have a surprising and profound effect on the transduction efficiency, as illustrated in FIG.27. For example, end-cap modifications may impact LAH4's ability to enhance transduction in SUP- T1 cells. As shown in FIG.27, the amide end-cap (LAH4-A) disrupts LAH4’s transduction- enhancing function, resulting in low transduction efficiency regardless of the presence of P407. Conversely, the carboxyl end-cap (LAH4-C) recovers LAH4’s ability to facilitate transduction, suggesting that the end-cap's chemical nature plays a critical role in maintaining the peptide’s functionality. This highlights the sensitivity of LAH4’s transduction capacity to structural modifications at the terminal end, with the carboxyl group evidently preserving or supporting its activity more effectively than the amide. Thus, in any of the methods and apparatuses described herein the CPP may comprise an LAH4 peptide, but may be restricted to essentially just LAH4-C and / or VF-1 peptide, but may substantially or completely exclude the LAH4-A form. All publications and patent applications mentioned in this specification are herein incorporated by reference in their entirety to the same extent as if each individual publication or patent application was specifically and individually indicated to be incorporated by reference. Furthermore, it should be appreciated that all combinations of the foregoing concepts and additional concepts discussed in greater detail below (provided such concepts are not mutually inconsistent) are contemplated as being part of the inventive subject matter disclosed herein and may be used to achieve the benefits described herein.

Claims

Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 CLAIMS What is claimed is:

1. A formulation for use in enhancing transduction of a paramyxovirus pseudotyped lentivirus vector particle into a target cell, the formulation comprising: a cell penetrating peptide (CPP) comprising at least one of: vectofusion-1 or LAH4-C; and a poloxamer 407, wherein the poloxamer 407 has a concentration that is greater than 5-fold a concentration of the CPP.

2. The formulation of claim 1, wherein the CPP comprises vectorfusion-1.

3. The formulation of claim1, wherein the CPP comprises LAH4-C.

4. The formulation of claim 1, wherein the CPP comprises less than 0.1% of LAH4-A.

5. The formulation of claim 1, wherein the concentration of the poloxamer 407 is greater than 10-fold to the concentration of the CPP.

6. The formulation of claim 1, further comprising the paramyxovirus pseudotyped lentivirus vector particle.

7. A method of enhancing transduction of a paramyxovirus pseudotyped lentivirus vector particle into a target cell, the method comprising: transducing the target cell with the paramyxovirus pseudotyped lentivirus vector particle containing one or more genes of interest and a formulation comprising a poloxamer 407 and a cell penetrating peptide (CPP) comprising at least one of: vectofusion-1 or LAH4-C, wherein a concentration of the poloxamer 407 has a concentration that is greater than 5-fold a concentration of the CPP.

8. The method of claim 7, wherein transducing the target cell comprises transducing in vivo within a subject.

9. The method of claim 7, wherein the paramyxovirus pseudotyped lentivirus vector particle comprises one or more glycoproteins from a Nipah-paramyxovirus-based lentivirus vector particle.

10. The method of claim 7, wherein the target cell is a B cell.Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 11. The method of claim 7, wherein the target cell is a T cell.

12. The method of claim 7, wherein the paramyxovirus pseudotyped lentivirus vector particle contains one or more glycoproteins from one or more of: a Nipah virus, a Hendra virus, a measles virus, a Tupaia paramyxovirus, a Newcastle disease virus, a parainfluenza virus, a Sendai virus, a Baboon endogenous retrovirus, RD114 feline endogenous virus, primate type D retroviruses, a Gibbon-ape leukemia virus, a murine stem cell virus, a MERS virus, or any combinations thereof.

13. The method of claim 7, wherein the CPP comprises vectorfusion-1.

14. The method of claim 7, wherein the CPP comprises LAH4-C.

15. The method of claim 7, wherein the CPP comprises less than 0.1% of LAH4-A.

16. The method of claim 7, wherein the concentration of the poloxamer 407 is greater than 10-fold to the concentration of the CPP.

17. A formulation for use in enhancing transduction of a paramyxovirus pseudotyped lentivirus vector particle into a target cell, the formulation comprising: a cell penetrating peptide (CPP) comprising vectofusion-1; and a poloxamer 407, wherein a concentration of the poloxamer 407 has a concentration that is greater than 5-fold a concentration of the CPP.

18. The formulation of claim 17, wherein the CPP comprises less than 0.1% of LAH4-A.

19. The formulation of claim 17, wherein the concentration of the poloxamer 407 is greater than 20-fold to the concentration of the CPP.

20. A method of enhancing transduction of a paramyxovirus pseudotyped lentivirus vector particle into a target T cell or B cell, the method comprising: transducing the target cell with the paramyxovirus pseudotyped lentivirus vector particle containing one or more genes of interest and a formulation comprising a cell penetrating peptide (CPP) comprising vectofusion-1, and a poloxamer 407, wherein the poloxamer 407 has a concentration that is greater than 5-fold a concentration of the CPP.Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 21. The method of claim 20, wherein transducing the target cell comprises transducing in vivo within a subject.

22. The method of claim 20, wherein the paramyxovirus pseudotyped lentivirus vector particle comprises a Nipah-paramyxovirus-based lentivirus vector particle.

23. The method of claim 20, wherein the target cell is a B cell.

24. The method of claim 20, wherein the target cell is a T cell.

25. The method of claim 20, wherein the paramyxovirus pseudotyped lentivirus vector particle contains a glycoprotein from one or more of: a Nipah virus, a Hendra virus, a measles virus, a Tupaia paramyxovirus, a Newcastle disease virus, a parainfluenza virus, a Sendai virus, a Baboon endogenous retrovirus, RD114 feline endogenous virus, primate type D retroviruses, a Gibbon-ape leukemia virus, a murine stem cell virus, a MERS virus, or any combinations thereof.

26. The method of claim 20, wherein the concentration of the poloxamer 407 is greater than 10-fold to the concentration of the CPP.

27. A formulation for use in enhancing the transduction of a lentiviral vector particle into a target cell, the formulation comprising: a. at least one cell penetrating peptide (CPP); and b. at least one of: (i) a HDAC inhibitor; (ii) a Blimp1 pathway blocker; or (iii) a surfactant, wherein the surfactant is a natural surfactant or a poloxamer.

28. The formulation of claim 27, wherein the formulation further comprises at one mammalian target of rapamycin (mTOR) inhibitor.

29. The formulation of claim 27 or claim 28, wherein the CPP is vectofusion-1, LAH4, LEPTIN30, APOE or any combinations thereof.

30. The formulation of claim 29, wherein the CPP is vectofusion-1.

31. The formulation of any of claims 27-30, wherein the HDAC inhibitor is valproic acid, trichostatin A, suberuylanilide hydroxamic acid, PXD101, oxamflatin, LAW824, LBH589, pyroxamide, SK-7041, SK-7068, tubacin, MS-275 depsipeptide, trapoxin A, apicidin, CHAPs, or any combinations thereof.Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 32. The formulation of claim 31, wherein the HDAC inhibitor is valproic acid.

33. The formulation of any of claims 27-32, wherein the Blimp1 pathway blocker is a Blimp1 siRNA or a Blimp1 shRNA.

34. The formulation of any of claims 27-33, wherein the surfactant is a natural surfactant.

35. The formulation of claim 34, wherein the natural surfactant is derived from a mammal, plant, microorganism or any combinations thereof.

36. The formulation of any of claims 27-35, wherein the surfactant is a poloxamer.

37. The formulation of claim 36, wherein the poloxamer is poloxamer 407.

38. The formulation of any of claims 27-37, wherein the formulation comprises (a) a CPP and a HDAC inhibitor; (b) a CPP and a Blimp1 pathway blocker; (c) a CPP and a surfactant, wherein the surfactant is a natural surfactant or a poloxamer; (d) a CPP, a HDAC inhibitor and a Blimp1 pathway blocker; (e) a CPP, a HDAC inhibitor and a surfactant, wherein the surfactant is a natural surfactant or a poloxamer; (f) a CPP, a Blimp1 pathway blocker and a surfactant, wherein the surfactant is a natural surfactant or a poloxamer; (g) a CPP and a mTOR inhibitor; (h) a CPP a HDAC inhibitor, and a mTOR inhibitor; (i) a CPP, a Blimp1 pathway blocker, and a mTOR inhibitor; (j) a CPP, a surfactant, and a mTOR inhibitor, wherein the surfactant is a natural surfactant or a poloxamer; (k) a CPP, a HDAC inhibitor, a Blimp1 pathway blocker, and a mTOR inhibitor; (l) a CPP, a HDAC inhibitor, a surfactant and a mTOR inhibitor, wherein the surfactant is a natural surfactant or a poloxamer; (m) a CPP, a Blimp1 pathway blocker, and a surfactant, wherein the surfactant is a natural surfactant or a poloxamer; or (n), a CPP, a HDAC inhibitor, a Blimp1 pathway blocker, a surfactant, a mTOR inhibitor, wherein the surfactant is a natural surfactant or a poloxamer.

39. The formulation of claim 27 or claim 38, wherein the mTOR inhibitor is rapamycin.

40. A method for transducing a target cell with a lentiviral vector particle, the method comprising the step of: transducing a target cell with a lentiviral vector particle containing one or more genes of interest and the formulation of any of claims 27-39.

41. The method of claim 40, wherein the method is performed in vivo in a subject.Client Ref. No.24-0030 Atty. Docket No. UNC2-42478.101 42. The method of claim 40 or claim 41, wherein the lentiviral vector particle is a pseudotyped lentiviral vector particle.

43. The method of any of claims 39-41, wherein the method further comprises transducing the target cell with the lentiviral vector particle followed by transducing the target cell with the formulation after the transduction with the lentiviral vector particle.

44. The method of any of claims 39-41, wherein the method further comprises transducing the target cell with the formulation followed by transducing the target cell with the lentiviral vector particle after the transduction with the formulation.

45. The method of any of claims 39-44, wherein the target cell is a B-cell.

46. The method of any of claims 39-45, wherein the pseudotyped lentiviral vector particle contains one or more glycoproteins from one or more of: a Nipah virus, a Hendra virus, a measles virus, a Tupaia paramyxovirus, a Newcastle disease virus, a parainfluenza virus, a Sendai virus, a Baboon endogenous retrovirus, RD114 feline endogenous virus, primate type D retroviruses, a Gibbon-ape leukemia virus, a murine stem cell virus, a MERS virus, or any combinations thereof.

47. The method of claim 46, wherein the pseudotyped lentiviral vector particle contains a glycoprotein from a Nipah virus.

48. The method of claim 47, wherein the pseudotyped lentiviral vector particle contains a G and / or an F protein from the Nipah virus.

49. The method of claim 47, wherein the glycoprotein from the Nipah virus contains one or more mutations, deletions, substitutions or combinations thereof.

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