Methods for treatment of age-related macular degeneration

Abstract

Methods are disclosed for treating or reducing the risk of developing age-related macular degeneration (AMD) in a subject. These methods can include selecting a subject having, or at risk of developing, the AMD and administering to the subject an effective amount of an agent that inhibits HERV-K. An agent that inhibits HERV-K includes, but is not limited to, an antibody, an inhibitory RNA molecule, an anti-retroviral agent, a CRISPR / Cas13 system targeting HERV-K, as well as angiogenin. A CRISPR / Cas13 system targeting HERV-K is also provided. These methods also can include selecting a subject having, or at risk of developing, the AMD and administering to the subject an effective amount of an agent that increases ANG activity.

Description

METHODS FOR TREATMENT OF AGE-RELATED MACULAR DEGENERATION CROSS REFERENCE TO RELATED APPLICATIONS This claims the benefit of U.S. Provisional Application No.63 / 453,006, filed March 17, 2023, which is incorporated by reference herein in its entirety. FIELD OF THE DISCLOSURE This relates to the field of retinal disease, specifically to the inhibition of human endogenous retrovirus K (HERV-K), and / or increasing angiogenin (ANG) activity, for the treatment of age-related macular degeneration (AMD). SEQUENCE LISTING The Sequence Listing is submitted as an XML file in the form of the file named “Sequence.xml” (88,776 bytes), which was created on March 14, 2024, which is incorporated by reference herein. BACKGROUND Age-related macular degeneration (AMD) is a major cause of blindness worldwide (reviewed in Lim et al., The Lancet 379 (9827): 1728-1738, 2012 and Mitchell et al., The Lancet 392 (10153): 1147-1159, 2018). There is an aging population in many countries, and thus more than 20% of the world population may have AMD. Advanced AMD, including neovascular age-related macular degeneration (wet) and geographic atrophy (late, dry), is associated with substantial, progressive visual impairment. Major risk factors include cigarette smoking, nutritional factors, cardiovascular diseases, and genetic markers, including genes regulating complement, lipid, angiogenic, and extracellular matrix pathways. More than 50 genetic susceptibility loci have been identified, including the CFH and ARMS2 genes. Accurate diagnosis of AMD uses both clinical examination and vision testing, including retinal photography, angiography, and optical coherence tomography. Dietary anti-oxidant supplementation has been shown to slow progression of the disease, but not eliminate it. Current treatments for neovascular age- related macular degeneration include intraocular injections of anti-VEGF agents. Evidence suggests that the three commonly used anti-VEGF therapies, ranibizumab, aflibercept, and bevacizumab, have similar efficacy. However, a need remains for additional agents that can be used to treat AMD and that reduce the risk of developing AMD. SUMMARY OF THE DISCLOSURE Methods are disclosed for treating or reducing the risk of developing age-related macular degeneration (AMD) in a subject. In some aspects, these methods include selecting a subject having, or at risk of developing, the AMD; and administering to the subject an effective amount of an agent that inhibits HERV-K, for example administration to the eye. An agent that inhibits HERV-K can reduce a) the amountof human endogenous retrovirus (HERV)-K; b) of an mRNA encoding a HERV-K proteins, c) translation of the HERV-K mRNA; d) the amount HERV-K proteins in the subject; e) inhibit activity of HERV-K mRNA and / or proteins, or any combination of a)-e). Exemplary agents include, but are not limited to, antibodies, inhibitory RNA molecules, inhibitory peptides, anti-retroviral agents and CRISPR / Cas13 systems targeting HERV-K. In some aspects, the agent that inhibits HERV-K is angiogenin or an agent that increases angiogenin expression and / or activity (such as a viral vector expressing ANG). In some aspects, angiogenin expression and / or activity is increased in the eye, such as RPE cells of the eye, by at least 50%, at least 100%, at least 200%, at least 500%, or more. Also provided are CRISPR / Cas13 systems and ribonucleoprotein (RNP) complexes for targeting HERV-K, as well as isolated cells containing such. In further aspects, methods are provided for treating or reducing the risk of developing age-related macular degeneration (AMD) in a subject that include selecting a subject having, or at risk of developing, the AMD; and administering to the subject an effective amount of an agent that increases angiogenin (ANG) activity. The foregoing and other features of the disclosure will become more apparent from the following detailed description of several aspects which proceeds with reference to the accompanying figures. BRIEF DESCRIPTION OF THE FIGURES FIG.1A is a set of digital images showing induced pluripotent stem (iPSC)-derived retinal pigment epithelium (iRPE) cells treated with complement incompetent human serum (CIHS, left images) or complement competent human serum (CCHS, right images). CC-HS triggers formation of subRPE deposits (drusen) as shown by change in APOE immunostaining from the apical membrane of iRPE (side views) to basolateral membrane. TW = transwell membrane on which iRPE cells are grown. FIG.1B is a graph showing transepithelial resistance (TER) of iRPE monolayers after CIHS (grey bar) and CCHS (white bar) treatments. FIG.2 is a schematic diagram of the genomic structure of retroviruses: endogenous retroviruses containing two long terminal repeats (5’ and 3’LTRs) flanking the internal coding sequence of the three basic retroviral genes (Gag, Pol, and Env). GAG=glycosaminoglycan, POL=polymerase, ENV=envelope. FIGS.3A and 3B are graphs showing RNAseq analysis of CC-HS treated iRPE transcriptome revealed genomic loci that show differential elevation of the mRNA of HERV-K. A) Bioinformatics analysis of RNAseq data identified the differentially expressed HERV-K in human serum treated iPSC-RPE. 5% CCHS was added to both apical and basal media of iRPE grown on trans-well for 48 hours, and HERV- K RNA levels from LTR and ORF containing HERV-K loci (~80), which is displayed as scaled depth values (signal reads) was normalized to length of transcripts. B) Scaled depth values of the top 16 differentially expressed HERV-K loci in human genome in CCHS treated samples compared to control, which is complement incompetent human serum (5% CIHS). Each graph shows the exact location of the endogenousretrovirus locus. Chromosome number is the first number and then the position is shown in base pair. Genome ID of the location is shown in FIGS.4A and 4B are graphs showing sustained low-level CCHS uniquely elevated mRNA of HERV-K components in iRPE. A) Representative images of RNA seq data, which was viewed by the Integrative Genomics Viewer, shows the aligned reads of the differentially expressed HERV-K loci. Only the reads of HERV-K, not the ones for HERV-P, were increased by the CCHS. B) Quantitative reverse transcriptase polymerase chain reaction (qRT-PCR) quantification of HERV-K components GAG, ENV, POL, in 0.1% CCHS-treated iRPE, shows specifically increases of HERV-K ENV and GAG, not the HERV R in cultured iRPE. CCHS (5%) were added to fully differentiated monolayer of iRPE for 2 days, 4 days, and 6 days. Data are calculated as fold change (CCHS / CHIS). MEAN ± SEM. N=3, p<0.05 is considered statistically significant. Symbol indicates individual iRPE donor. Star shows statistically significant data. FIG.5. shows digital images of iPRE cells. Sustained low-level complement competent human serum (CCHS) elevates HERV-K ENV level in iRPE Immunofluorescent detection of increases of HERV-K ENV protein in CCHS (0.1%) treated iRPE 4 and 6 days after the treatment. Confocal laser microscopic images of IF signals (HERV-K, phalloidin, and DAPI are shown), scale bar 20uM. FIG.6 shows digital images of the localization of HERV-K expression in iRPE cells using RNAscope. Increased HERV-K (ENV) mRNA was detected in both CCHS treated iRPE and in eyes of AMD patients. Top left: PPIB (Peptidylprolyl Isomerase B) mRNA probe is included as a positive control and validate the detection procedure. HERV-K was detected specifically in CCHS treated iRPE after 48 hours exposure, (left, bottom), other than in the cells which was treated with CIHS under the same condition (left, Middle). Cross section of eyes obtained from human AMD patient (90 years old, right panel) was subjected to HERV-K RNA detection by RNASCOPE™. The data shows HERV-K RNA was present in RPE and choroid of human patient, and absent in age matched control eye. FIGS.7A-7B are graphs showing reduced CCHS-induced secretion of proinflammatory cytokines upon treatment with anti-viral drug or TLR inhibitors. iRPE grown on transwells were pretreated with antiviral drug (Tenofovir, 20uM), TLR3 / dsRNA complex inhibitor (10uM) or TLR4 inhibitor TAK-242 (5uM) overnight, followed by incubation with CIHS (5%) or CCHS (5%) for 48hours. Apical and basal media were collected and were analyzed by the Multiplex Luminex assay to detect IL-6, IL-8 IL-18, IL-1β and IFN β. Levels of IL-18, IL-1β and IFN β are below detection range. CCHS induced increases of (A) IL-8 and (B) IL-6 were reduced by these inhibitors for two biological replicates. The results show an anti- viral as preventative for dry AMD, and combination therapy with anti-VEGF for wet AMD, can be used as pills and topical eye drops. FIGS.8A and 8B show lipid staining iRPE treated with CCHS and / or TLR inhibitors. TLR inhibitors reduce CCHS- induced lipid accumulations. A) iRPE was pretreated with TLR3 or TLR4 inhibitor and CCHS. The iRPE was stained with BODIPY® fluorescent dye (stains for lipids that accumulate under the RPE) (10uM) or DAPI (stains DNA) .and images captured with laser scanning confocal microscope (40X). B) Quantification of fluorescent signals. Data are the representative of 2 biological replicates.FIGS.9A-9C show the generation the lentiviral construct to express HERV-K ENV. A) Schematic diagram illustrates the HERV-K ENV expression cassette of the lentiviral construct. B) Detection of HERV-K ENV protein in IPSC. AMDCD cells were transduced with HERV-K ENV lentiviral construct (MOI 1). 48 hours later, and total protein lysate was analyzed by Western blot against HERV-K ENV using GAPDH as a loading control. The data shows an increase in HERV-K ENV protein in the over expressing cell. C) Live imaging of mcherry fluorescent signal shows amount of transduced lentivirus coordinates with the levels of protein expression in fully differentiated iRPE at 14 days after transduction. iRPE was transduced with the lentivirus (MOI – multiplicity of infection - 0.5 or 3) containing 5%RPE media supplemented with 5ug / ml polybrone for 16 hours. The media was replaced with fresh media and continuously incubated for additional 14 days. Media was refreshed every other day. FIGS.10A-10C show that HERV-K ENV is sufficient in inducing RPE degeneration, resembling AMD phenotype. HERV-K-ENV, expressed via lentiviral transduction, reduces TER and induces lipid accumulation in iRPE. A) Transepithelial resistance (TER), measured by using EVOM, was decreased by HERV-K ENV overexpression. B) Images of immunostaining of HERV-K ENV (Top panel) and staining with Alexa 488-conjugated BODIPY® fluorescent dye (bottom panel), taken under laser scanning confocal microscopy (LSM980) using 40X objective. C) Quantification of HERV-KENV (top graph) and BODIPY® fluorescent dye (bottom graph) in HERV-K overexpressing iRPE. Four images were captured per sample. Signals were quantified with Image J according to an established method and normalized to the number of cells in the view. The data are MEAN± SEM of signal count per cell of three biological replicates. ****P<0.0001, ***P<0.005; ** p<0.05. FIGS.11A-11C are graphs showing that CCHS progressively decreased mRNA and secreted angiogenin (ANG) in iRPE. A) CCHS (5%) were added to fully differentiated monolayer of iRPE for 48hours. Total RNA was subjected to RNAseq analysis. Data show CCHS specifically decreased mRNA levels of ANG, not that of DICER. Data are calculated as fold change (CCHS / CHIS). MEAN ± SEM. N=3, p<0.05 is considered statistically significant. Symbols indicate iRPE donor cells. B) mRNA levels of ANG were progressively decreased by CCHS treatments. CCHS (0.1%) was added to both apical and basal media of iRPE for 2 days, 4 days, and 6 days and refreshed daily. Total RNA was analyzed for ANG and Dicer expression by qRT-PCR using CIHS treated cells as a control. N=3, p<0.05. C) CCHS (0.1%) decreased the secretion of ANG into the iRPE media. CCHS or CIHS was added to the iRPE media similarly as described in B). Apical and basal media were collected separately at 2 days, 4 days and 6 days. Amount of ANG were quantified by QUANTIKINE® ELISA kit. Data are MEAN ± SEM of secretion activities. N=3, p<0.05 is considered statistically significant. FIG.12 are digital images showing that CCHS progressively decreases intracellular angiogenin (ANG) in iRPE. CCHS (0.1%) decreased intracellular ANG in iRPE. IPRE were treated with CCHS or CIHS (5%) for 48 hours. Total protein lysate was analyzed by Western Blot (top) for the expression ANG. In a parallel experiment, cells were fixed in 4%PFA for 20 mins and stained with antibodies against human ANG. Expression of ANG (bottom) were visualized by immunofluorescent signal, cell boarded with ZO-1)and nuclei with DAPI. scale bar: 20µM. FIGS.13A-13B are graphs showing that decreases HERV-K specific ANG targets-transfer RNA fragments (tRFs) in iRPE. A) CCHS specifically decreased tRFs, which control HERV-K levels in iRPE. CCHS (CIHS as a control) was added to fully differentiated iRPE for 3hr, 24hr and 48hrs. Total RNA was extracted and subjected to adaptor mediated tRF RT-qPCR to detect either tRFs that are specifically binds to HERV-K (3”tiR088 (LysCTT(n)), 3006B--LysTTT, tRF-33002A pro-AGG, tRF-33016 / 18 / 22B LysCTT(n) or the ones do not bind (3009B Leu TAA) shown in (B). FIGS.14A-14B show a gene therapy strategy (A) to reduce HERV-K levels in CC-HS treated iRPE cells. HERV-K is made from multiple loci within the genome and these loci have slight sequence variations. Therefore, to develop a gene therapy for HERV-K RNA made from most of these different loci of HERV-K is targeted. Cas13 is a nuclease that can target RNA using a complementary guide sequence. Using bioinformatics analysis, three guide sequences (SEQ ID NOs: 1-3) (B) were identified in HERV-K that were used to target HERV-K expression in RPE cells. These sequences were designed against the GAG part of HERV-K mRNA because that is the start of the RNA. Degradation of the start of RNA leads to degradation of the remainder of the RNA. FIGS.15A-15C. Sequences showed complementarity across multiple HERV-K loci and also showed good consensuses for CAS13Rx based targeting. The genomic distribution of three guides used is shown in the Table. SEQ ID NOS: 1-3 are shown bold and underlined. The consensus sequences for gRNA1 (SEQ ID NO: 18), gRNA2(SEQ ID NOs: 34 and 51), and gRNA3 (SEQ ID NO: 59) are shown. The various alignments to the genome are shown for gRNA1 (SEQ ID NOs: 19-33), gRNA2(SEQ ID NOs: 35- 50 & 52-58), and gRNA3 (SEQ ID NO: 60-75). FIGS.16A-16B show the induction of Cas13Rx expression using doxycycline. (A) is a Western blot showing HA-tagged Cas13Rx overexpressed using a lentivirus construct. High expression of HA-tagged Cas13Rx is seen at multiplicity of infection (MOI) of 1.0. (B) is a digital image showing HA-tag-Cas13Rx enzyme expression in iRPE cells at MOI of 1.0 of the lentivirus vector. FIGS.17A-17E. Cas13Rx mediated HERV K knock down reverses complement-induced lipid accumulation. (A) To overexpress Cas13Rx in iRPE cells were transduced with lentivirus expressing a HA- tagged CAS13Rx under the control of a doxycycline inducible promoter. Seven days of doxycycline treatment induced the expression of CAS13Rx (FIGS.16A-16B). At this stage, iRPE cells were transduced with another lentiviral construct that expresses one of the three guide RNAs along or together and the control guide RNA. Another 7 days was allowed for guide RNAs to be expressed at high levels and then treated cells with CC-HS. Four days after CC-HS or CI-HS treatment, HERV-K levels were measured in cells and monolayer TER and BODIPY® levels were measured in cells. (B) Shows a TER graph of CIHS (grey bars) and CCHS (black bars) treated samples that were transduced with a scrambled guide RNA (NEG) or no guide RNA (Cas13Rx) or guide RNA #2 (Fig.15). Only guide RNA#2 is able to rescue TER downregulated by CCHS treatment (C) Top panel: shows digital images of CIHS or CCHS treated iRPE, transduced either with a scrambled control (NEG) or guideRNA#2. CCHS induced increase in HERV-Kexpression (compare CIHS NEG samples with CCHS NEG samples) is downregulated by guide RNA 2 against HERV-K. Bottom panel: shows digital of CIHS or CCHS treated iRPE, transduced either with a scrambled control (NEG) or guideRNA#2. CCHS induced increase in lipid deposits (measured as BODIPY® signal) in CCHS is downregulated by guide RNA 2 against HERV-K. (D) Quantification of HERV-K levels seen in FIG.17C top panel shows guide RNA#2 is able to downregulate HERV-K levels in CCHS treated iRPE cells. (E) Quantification of BODIPY® levels seen in FIG.17C bottom panel shows guide RNA#2 is able to downregulate BODIPY® in CCHS treated iRPE cells. FIG.18. Cas13Rx mediated HERV K knock down reverses complement-induced lipid accumulation by all three guides selected in FIG.15. Digital images of CCHS treated AMD patient 1-iRPE, transduced either with a scrambled control (NEG) or three guide RNAs #1, 2, 3 alone or in combination. CCHS induced increase in lipid deposits (measured as BODIPY® signal). BODIPY® signal is downregulated by all three guides against HERV-K when transduced with CCHS treated cells. Left graph shows quantification of digital imaging data. FIG.19. Cas13Rx mediated HERV K knock down reverses complement-induced lipid accumulation by guides selected in FIG.15 (example shown for two guides). Digital images of CCHS treated AMD patient 2-iRPE, transduced either with a scrambled control (NEG) or two guide RNAs #1, 2. CCHS induced increase in lipid deposits (measured as BODIPY® signal). BODIPY® signal is downregulated by guides against HERV-K when transduced with CCHS treated cells. CIHs treatment is a negative control for the study. Left graph shows quantification of digital imaging data. FIG.20. Schematic diagram of method for testing the role of exogenously expressed angiogenin (ANG) in protection of CCHS-induced iRPE injury. FIG.21. A bar graph showing ANG overexpression by lentivirus. FIG.22. A digital image showing that ANG prevented the CCHS-induced HERVK increase. FIG.23. A digital image showing that ANG reduced the CCHS-induced lipid accumulation. FIG.24. A bar graph showing ANG overexpression prevents CCHS induced TER decrease in iRPE. FIGS.25A-25C. (A) Schematic illustrates the transgene domain structure in expression vector, where HERV-K ENV is under RPE specific human VMD2 promoter (also known as best1 promoter). (B) qPCR data of genotyping of six HERV-K ENV founder mice. (C) qRT-PCR identified two founder mice lines- founder1 and founder6 showing significantly higher expression of HERV-K ENV. These founder mice lines (1&6) were backcrossed to C57BL / 6J to generate pure to C57BL / 6. In induced pluripotent stem cell derived-RPE (iPSC-RPE), complement competent human serum (CC-HS) increased HERV-K ENV, coinciding with increased lipid accumulation, cytokine release and loss of epithelial cell morphology, mimicking pathogenic changes during early AMD (Sharma R, et.al., Nat Commun.2021 Dec 15;12(1):7293. doi: 10.1038 / s41467-021-27488-x.PMID: 34911940, 36550275). FIGS.26A-26H. HERV-K ENV overexpression induces lipid accumulation in transgenic RPE. (A-B) Immunostaining images show higher expression of HERV-K ENV in flat mounts of RPE isolated from 1–2-month-old transgenic mice eye (A) and quantification of the HERV-K ENV signal is shown in(B). (C-D) Immunostaining images show higher of HERV-K ENV in flat mounts of RPE isolated from 7–8-month-old transgenic eye (C) quantification data is shown in (D). (E- F) Immunostaining images show higher lipid droplets stained with BODIPY®, in HERV-K ENV over- expression mice aged 1–2-month (E) and corresponding quantification data show significant higher lipid droplet signal in homo HERV-K ENV mice (F). (G-H) Immunostaining images show higher lipid droplets stained with BODIPY®, in HERV-K ENV over-expression mice aged 7-8 months old (G) and corresponding quantification data shows significantly higher lipid droplet levels in homo HERV-K ENV mice (H). Four images per sample was captured under laser scanning according to an established method and normalized to size of imaging area in the view. The data is ratio of raw count obtained from transgenic RPE compared to wildtype RPE for n>3 biological replicates., **P<0.005; * p<0.05. FIGS.27A and 27B. Lipid droplets co-localize with HERV-K ENV protein in RPE of transgenic mice. (A) En-face view of images show the localization of HERV-K ENV (magenta) with lipid droplets (stained with BODIPY®, green) in 7–8-month-old transgenic mice compared to wild type mice. (B) 3D rendered images of panel A shows the sub-cellular localization of HERV-K ENV and lipid droplets. FIGS.28A and 28B. Appearance of hyperfluorescent spots in HERV-K ENV overexpressing eye. (A) Autofluorescence (AF) images of mice eyes aged 7-8-month wildtype+ / + (WT, left) and heterozygous HERV-K ENV tg / + (middle) or homozygous HERV-K ENV tg / tg transgenic mice (right) show increased autofluorescence deposits (arrows) in the transgenic mice compared to WT and heterozygotes. (B) Light microscopic images of H&E-stained 5 μm histological sections of WT, heterozygous and homozygous HERK-K ENV mice. The anatomic layers of the retina are labeled including the ganglion cell layer (GCL); inner plexiform layer (IPL); inner nuclear layer (INL); outer plexiform layer (OPL); outer nuclear layers (ONL); inner segment / outer segment layer (IS / OS) and the neighboring RPE and choroid. Blue arrows mark abnormal cells in the SRS among misaligned outer segments. FIGS 29A-29D. Appearance of subretinal cells and RPE intracellular vacuoles in HERV-K ENV overexpressing eye. (A-D) Transmission electron (TEM) micrograph images of the photoreceptor-RPE- choroid complex in the 7-8 month wildtype + / + (A) and heterozygous HERV-K ENV tg / + (B) or homozygous HERV-K ENV tg / tg transgenic mice (C,D), show lipid aggregates (white arrows, B ), an abnormal subretinal cell (horizontal black arrow, C), vacuoles (white arrow, C), and disrupted tight junctions (black arrowheads, D) in transgenic eye. FIGS.30A-30F. Combination of antiviral drugs exerted greater effect on blocking CCHS induced lipid accumulation effect. A) Flow chart of experimental process and assay. Mature iPSC-RPE grown on 96 cell culture wares were treated in triplicates with single drug or with combination drugs for 24 hours before the addition of Complement Competent Human Serum (CC-HS) (0.1%) and Complement Incompetent Human Serum (CI-HS) (0.1%) as control, cells with no treatment were also included for baseline comparison. B) The diagram outlines the application format of single drug and combination drug treatment and the plate map of the application. The tested drugs were: Metformin hydrochloride (3 mM); Darunavir (50 µM); L-745,870 trihydrochloride (6 uM, a highly potent and selective D4 dopamine receptorblocker), Tenofovir (10 µM, a nucleoside reverse inhibitors (NRTIs)). C) Combinations with antiviral drugs displayed greater rescue effect on HS induced lipid accumulation than single drugs only. Mature iRPE grown on 96 cell culture were treated in triplicates with single drug or in combination 24 hours before the addition of CC-HS with CI-HS. Cells were fixed and labeled with Alexa 488-conjugated BODIPY® fluorescent dye (10 µM) and ZO-1 Monoclonal Antibody Alexa FLUOR™ 594 (1:200), then imaged with ANDOR confocal scanning microscope (Oxford system, BC43). Four images were captured at random per each sample. The images were exported from each channel. The BODIPY® signals were quantified with Image J according to an established method and normalized to size of imaging area in the view. Raw counts of lipid deposits were obtained from 4 images per replicate, 3 replicates per sample group. ****P<0.0001; *** p<0.0005. Data was analyzed and plotted through PRISM. D) Images of the ZO-1 labeled cell border were subjected to REShAPE analysis to evaluate cell area, aspect ratio and hexagonality. Data was analyzed and plotted through R program. E-F) Combination with antiretroviral drugs inhibit CC-HS induced IL-8 and IL-6 release.100uL media was collected from each well of 96 well culture plate and diluted 50X before running Luminex-based multiplex human assay. Amount of IL-8 and IL-6 in media was analyzed by the Luminex based multiplex human cytokine assay protocol. Values of cytokine concentration for the triplicates of each sample are shown. FIGS.31A and 31B. Application of AAV8-shRNA HERV-K ENV as therapeutics to treat AMD, in vitro and in vivo studies. A) Schematic diagram illustrates the workflow of in Vitro experiments with iRPE to test the effect of AAV8-shRNA HERV-K ENV in rescuing the cell defects caused by anaphylatoxin (CC-HS). Either naïve iRPE or HERV-K ENV overexpressing iRPE are transduced with AAV HERV-K ENV or AAV control at MOI 104to 1054 days before the addition of CC-HS (0.1%) or control CIHS (0.1%). The anaphylatoxin containing media is refreshed daily for 3 days. Samples are collected at day 4 and corresponding assays will be performed to detect the rescuing effect. B) Schematic diagram of the procedures for determining the effect of AAV-shRNA HERV-K ENV in reversing HERV-K ENV caused RPE degeneration. SEQUENCES The nucleic and amino acid sequences listed in the accompanying sequence listing are shown using standard letter abbreviations for nucleotide bases, and one letter code for amino acids, as defined in 37 C.F.R.1.822. Only one strand of each nucleic acid sequence is shown, but the complementary strand is understood as included by any reference to the displayed strand. SEQ ID NOs: 1-3 are exemplary nucleic acid sequence of gRNA. SEQ ID NO: 4 is an exemplary nucleic acid sequence of HERV-K. SEQ ID NO: 5 is an exemplary nucleic acid sequence encoding a Cas13Rx. SEQ ID NO: 6 is an exemplary HERV-K Gag amino acid sequence (GENBANK® Accession No. AAL16779.1). SEQ ID NO: 7 is an exemplary HERV-K Gag amino acid sequence (GENBANK® Accession No. AAL60056.1).SEQ ID NO: 8 is an exemplary HERV-K Env amino acid sequence (GENBANK® Accession No. AAL16780.1). SEQ ID NO: 9 is an exemplary Cas13Rx protein (without the signal peptide) (GENBANK® Accession No. QMT62609.1). SEQ ID NO: 10 is an exemplary nucleic acid sequence encoding a Cas13Rx (GENBANK® Accession No. MN934322.1). SEQ ID NO: 11 is an exemplary amino acid sequence of human ANG. SEQ ID NOs: 12 and 13 are exemplary genomic DNA corresponding to tRNA fragments, tRNA- CTT and tRNA-TTT. SEQ ID NO: 14 is an exemplary nucleic acid sequence encoding human ANG. SEQ ID NOs: 15-16 are nucleic acid sequences of primers. SEQ ID NO: 17 is the nucleic acid sequence of a reporter. SEQ ID NO 18 is the consensus nucleic acid sequence for gRNA1. SEQ ID NOs 19-33 are the nucleic acid alignment sequences for gRNA1. SEQ ID NOs 34 & 51 are the consensus nucleic acid sequences for gRNA2. SEQ ID NOs: 35-50 & 52-58 are the nucleic acid alignment sequences for gRNA2. SEQ ID NO 59 is the consensus nucleic acid sequence for gRNA3. SEQ ID NOs 60-75 are the nucleic acid alignment sequences for gRNA3. DETAILED DESCRIPTION OF SEVERAL ASPECTS Human endogenous retroviruses (HERVs) and elements containing long terminal repeat-like sequences comprise up to 8% of the human genome, see U.S. Published Patent Application No. 2008 / 0019979A1. There are over 200 distinct groups and subgroups of HERVs. HERVs have lost infectivity due to mutations, and in general they are largely noninfectious retroviral remnants. However, open reading frames (ORFs) have been observed for ERV3, HERV-E 4-1, and HERV-K. The members of the HERV-K superfamily, which is characterized by the presence of primer binding sites for lysine tRNA, are the most biologically active. Only HERV-K seems to have the full complement of open reading frames typical of replication competent mammalian retroviruses. The K family contains a central open reading frame (cORF) and is comparable to HIV-1 Rev protein. HERV-K was originally identified by its homology to the mouse mammary tumor virus (MMTV), and is transcriptionally active in several human cancer tissues, including breast cancer tissues, as well as tumor cell lines, such as the human breast cancer cell line T47D and the teratocarcinoma cell line GH. HERV-K env mRNA is frequently expressed in human breast cancer and HERV-E mRNA is expressed in prostate cancer and ovarian cancer, see U.S. Published Patent Application No.2008 / 0019979A1, which discloses antibodies that specifically bind an HERV-K protein, see also U.S. Patent No.10,723,787 and U.S. Patent No.10,981,976. It is disclosed herein that HERV-K expression is associated with the AMD phenotype of human cells in the retinal pigment epithelium (RPE). Furthermore, inhibition of HERV-K transcription andtranslation, using inhibitory RNA molecules, peptides, anti-retroviral agents, and CRISPR / Cas13 or Cas 9 can reduce pathological phenotype of RPE cells. In addition, an agent that increases ANG activity prevented CCHS-induced HERVK increase, reduced CCHS-induced lipid accumulation, and prevented a CCHS induced TER decrease in RPE cells. Methods are disclosed for treating or reducing the risk of developing age-related macular degeneration (AMD) in a subject. These methods include selecting a subject having, or at risk of developing, AMD, and administering to the subject an effective amount of an agent that inhibits HERV-K. Also provided herein are CRISPR / Cas13 systems and RNPs which can be used in the methods for treating AMD. Methods are also disclosed for treating a subject having, or at risk of developing, the AMD, by administering to the subject an effective amount of an agent that increases ANG activity. I. Terms Unless otherwise noted, technical terms are used according to conventional usage. Definitions of many common terms in molecular biology may be found in Krebs et al. (eds.), Lewin’s genes XII, published by Jones & Bartlett Learning, 2017. As used herein, the singular forms “a,” “an,” and “the,” refer to both the singular as well as plural, unless the context indicates otherwise. For example, the term “a protein” includes single or plural proteins and can be considered equivalent to the phrase “at least one protein.” As used herein, the term “comprises” means “includes.” Unless otherwise indicated “about” indicates within five percent. It is further to be understood that any and all base sizes or amino acid sizes, and all molecular weight or molecular mass values, given for nucleic acids or polypeptides are approximate, and are provided for descriptive purposes, unless otherwise indicated. Although many methods and materials similar or equivalent to those described herein can be used, particular suitable methods and materials are described below. In case of conflict, the present specification, including explanations of terms, will control. In addition, the materials, methods, and examples are illustrative only and not intended to be limiting. To facilitate review of the various aspects, the following explanations of terms are provided: Administration: The introduction of a composition (such as one containing an agent that increases or decreases HERV-K transcription or translation) into a subject by a chosen route. Administration can be local or systemic. For example, if the route is intravenous, the composition is administered by introducing the composition into a vein of the subject. Similarly, if the route is intramuscular, the composition is administered by introducing the composition into a muscle of the subject. If the chosen route is oral, the composition is administered by ingesting the composition. Exemplary routes of administration of use in the methods disclosed herein include, but are not limited to, oral, injection (such as subcutaneous, intramuscular, intradermal, intraperitoneal, intraosseous, and intravenous), sublingual, rectal, transdermal (for example, topical), intranasal, vaginal, and inhalation routes. Administration can also be local, such as to the eye of a subject. In a specific aspect, administration is topical to the eye, such as via an eye drop solution. In a specific aspect, administration is intraocular, such as subretinal, direct retinal, suprachoroidal or intravitreal injection.As used herein, the term "co-administer" (or "co-administration") refers to administration of two or more agents within about 2 hours of each other, for example, as part of a clinical treatment regimen. In other aspects, "co-administer" refers to administration of two or more agents within 1 hour of each other. In other aspects, "co-administer" refers to administration of two or more agents within 30 minutes of each other. In other aspects, "co-administer" refers to administration of two or more agents within 15 minutes of each other. In other aspects, "co-administer" refers to administration of two or more agents at the same time, either as part of a single formulation or as multiple formulations that are administered by the same or different routes. A single “dose” refers to co-administration of agents at the same time. Age Related Macular Degeneration (AMD): AMD is caused by damage to the macula of the retina. Onset of AMD may be asymptomatic, but AMD gradually worsens over time and generally results in blurred or no vision in the center of the visual field in one or both eyes. It can be hard to recognize faces, drive, read, or perform other activities of daily life, and visual hallucinations may also occur. AMD typically occurs in older people, such as subjects about 50 years and older. Genetic factors and smoking can play a role. Diagnosis includes a complete eye exam, and severity can range from early, intermediate, and late types, in which the late type can further include "dry" and "wet" forms. Dry AMD (also called atrophic AMD) occurs over time, wherein macular tissue thins and breaks down. Symptoms can include visual distortions, reduced central vision in one or both eyes, a need for brighter light for reading or close work, increased difficulty adapting to low light levels, increased blurriness of printed words, decreased intensity or brightness of colors, and difficulty recognizing faces. Dry AMD is diagnosed by examining the back of the eye for drusen; testing for defects in the center of the vision (such as using an Amsler grid to identify whether straight lines in the grid to look faded, broken, or distorted, indicating the presence of dry AMD); fluorescein or indocyanine green angiography (examining for abnormal blood vessel or retinal changes); and / or optical coherence tomography (examining for retinal thinning, thickening, or swelling). Currently available treatments include rehabilitation for adapting to the loss of central vision (low vision rehabilitation) and implanting a telescopic lens. Wet AMD (also called advanced neovascular AMD) follows dry AMD and includes abnormal blood vessel growth as well as fluid build-up in the back of the eye, which can produce a bump in the macula, causing vision loss or distortion. In addition to the symptoms of dry AMD, wet AMD symptoms can also include a well-defined blurry spot or blind spot in the field of vision, general haziness in overall vision, and abrupt onset and rapid worsening of symptoms. Currently available treatments include medications directed to stopping the growth of new blood vessels, such as bevacizumab (AVASTIN®), ranibizumab (LUCENTIS®), and aflibercept (EYLEA®); photodynamic therapy; photocoagulation; and low vision rehabilitation. Agent: Any substance or any combination of substances that is useful for achieving an end or result; for example, a substance or combination of substances useful for treating AMD. Agents include proteins, nucleic acid molecules (such as gRNAs), compounds, small molecules, organic compounds, inorganic compounds, or other molecules of interest. An agent can include a therapeutic agent (such as ananti-retroviral agent), a diagnostic agent or a agent. Angiogenin (ANG): A protein, also as ribonuclease 5, that is stimulator of the formation of new blood vessels in vivo. ANG can hydrolyze cellular RNA, resulting in modulated levels of protein synthesis and interacts with DNA causing a promoter-like increase in the expression of ribosomal (r)RNA. ANG enhances rRNA transcription by binding to a CT-rich angiogenin binding element. ANG has a similar catalytic activity to RNase A, it preferentially binds on the 3' side of pyrimidines and follows a transphosphorylation / hydrolysis mechanism. Unlike RNase A, which has no base specificity, ANG usually cleaves the 3′-side of cytidylic or uridylic acid residues when the pyrimidine is followed by adenine, but not restrict to all the potential cleavage sites. ANG shows preferential cleavage of single-stranded RNA as the substrate, and cleaves tRNAs. Although ANG has been shown to bind DNA in vivo, it does not cleave DNA, see Sheng and Zu, Acta Biochimica et Biophysica Sinica 48: 3990-410, 2016. ANG overexpression selectively cleaves a subset of tRNAs, including tRNAGlu, tRNAGly, tRNALys, tRNAVal, tRNAHis, tRNAAsp, and tRNASeCto tRNA halves and tRF-5s that are 16–30 bases called tiRNAs Zu et al.mammals and birds. The term mammal includes both human and non-human mammals. Similarly, the term “subject” includes both human and veterinary subjects. Antibody: A polypeptide comprising at least a light chain or heavy chain immunoglobulin variable region which specifically recognizes and binds an epitope (e.g., an antigen, such as an HERV-K protein (for example, Gag, Pol, or Env, or fragment thereof). This includes intact immunoglobulins and the variants and portions of them well known in the art, such as Fab' fragments, F(ab)'2 fragments, single chain Fv proteins (“scFv”), and disulfide stabilized Fv proteins (“dsFv”). A 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. The term also includes genetically engineered forms such as chimeric antibodies (e.g., humanized murine antibodies), heteroconjugate antibodies (e.g., bispecific antibodies). See also, Pierce Catalog and Handbook, 1994-1995 (Pierce Chemical Co., Rockford, IL); Kuby, J., Immunology, 3rdEd., W.H. Freeman & Co., New York, 1997. Typically, an immunoglobulin has a heavy and light chain. 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 regionscontain a "framework" region interrupted by three regions, also called “complementarity- determining regions” or “CDRs”. The extent of region and CDRs has been defined (see, Kabat et al., Sequences of Proteins of Immunological Interest, U.S. Department of Health and Human Services, 1991, 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, serves to position and align the CDRs in three-dimensional space. 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 VL CDR1 is the CDR1 from the variable domain of the light chain of the antibody in which it is found. References to “VH” or “VH” refer to the variable region of an immunoglobulin heavy chain, including that of an Fv, scFv, dsFv or Fab. References to “VL” or “VL” refer to the variable region of an immunoglobulin light chain, including that of an Fv, scFv, dsFv or Fab. A “monoclonal antibody” is an antibody produced by a single clone of B-lymphocytes or by a cell into which the light and heavy chain genes of a single antibody have been transfected. Monoclonal antibodies are produced by methods known to those of skill in the art, for instance by making hybrid antibody-forming cells from a fusion of myeloma cells with immune spleen cells. Monoclonal antibodies include humanized monoclonal antibodies. A "humanized" immunoglobulin is an immunoglobulin including a human framework region and one or more CDRs from a non-human (such as a mouse, rat, or synthetic) immunoglobulin. The non-human immunoglobulin providing the CDRs is termed a “donor,” and the human immunoglobulin providing the framework is termed an “acceptor.” In one aspect, all the CDRs are from the donor immunoglobulin in a humanized immunoglobulin. Constant regions need not be present, but if they are, they must be substantially identical to human immunoglobulin constant regions, i.e., at least about 85-90%, such as about 95% or more identical. Hence, all parts of a humanized immunoglobulin, except possibly the CDRs, are substantially identical to corresponding parts of natural human immunoglobulin sequences. A “humanized antibody” is an antibody comprising a humanized light chain and a humanized heavy chain immunoglobulin. A humanized antibody binds to the same antigen as the donor antibody that provides the CDRs. The acceptor framework of a humanized immunoglobulin or antibody may have a limited number of substitutions by amino acids taken from the donor framework. Humanized or other monoclonal antibodies can have additional conservative amino acid substitutions which have substantially no effect on antigen binding or other immunoglobulin functions. Humanized immunoglobulins can be constructed by means of genetic engineering (e.g., see U.S. Patent No.5,585,089). Anti-retroviral agent: An agent that specifically reduces or inhibits, expression or replication activity of a retrovirus (or endogenous retrovirus viral elements in the human genome) in cells, or aretrovirus from infecting cells. Non-limiting of antiretroviral agents that are drugs, which can be used in the disclosed methods, include fusion (e.g., enfuvirtide), entry inhibitors (e.g., maraviroc), nucleoside and nucleotide reverse transcriptase inhibitors (e.g., lamivudine, zidovudine, abacavir, tenofovir, TAF, TDF, FTC), non-nucleoside reverse transcriptase inhibitors (NNRTI) (e.g. delavirdine, efavirenz, nevirapine, and other diarylpyrimidine (DAPY) derivatives), protease inhibitors (e.g., indinavir, ritonavir, darunavir, atazanavir), and integrase inhibitors (e.g., elvitegravir, raltegravir, dolutegravir). Anti-retroviral agents of use in the present methods are disclosed, for example, in Tyagi et al., Inhibition of human endogenous retrovirus-K by antiretroviral drugs, Retrovirology 14: 21 (13 pages), 2017, incorporated herein by reference. Anti-retroviral therapy (ART): A therapeutic treatment for inhibiting a retrovirus involving administration of at least one anti-retroviral agent (e.g., one, two, three or four anti-retroviral agents) to an individual (such as one infected with a retrovirus) during a course of treatment. One example of a regimen includes treatment with a combination of TAF, FTC, and EVG. In some examples, ART includes Highly Active Anti-Retroviral Therapy (HAART). Caspase (Cas): An enzyme that is that a cysteine-aspartic protease, cysteine aspartase or cysteine- dependent aspartate-directed protease. Caspases are a family of protease enzymes playing essential roles in programmed cell death. They are named caspases due to their specific cysteine protease activity, wherein a cysteine in its active site nucleophilically attacks and cleaves a target protein only after an aspartic acid residue. cDNA (complementary DNA): A piece of DNA lacking internal, non-coding segments (introns) and regulatory sequences that determine transcription. cDNA is synthesized in the laboratory by reverse transcription from messenger RNA extracted from cells. Cobicistat (COBI): 1,3-thiazol-5-ylmethyl (2R,5R)-(5-{[(2S)-2-[(methyl{[2-(propan-2-yl)-1,3- thiazol-4-yl]methyl}carbamoyl)amino]]-4-(morpholin-4-yl)butanamido}-1,6-diphenylhexan-2-yl)carbamate. Cobicistat is a cytochrome P4503A inhibitor that acts as pharmacokinetic enhancer to increase the effectiveness of HIV anti-retroviral drugs. It is used to increase the bioavailability of other anti-retroviral agents. Cobicistat is marketed as TYBOST® and is also known as GS-9350. Control: A reference standard. In some aspects, the control is a negative control sample obtained from a healthy patient (such as one without AMD), or a subject treated with a carrier, non-targeted nucleic acid sequences, scrambled nucleic acid / amino acid sequences or untreated cells from a healthy patient. In other aspects, the control is a positive control sample obtained from a patient that has been treated with an active agent. In still other aspects, the control is a historical control or standard reference value or range of values (such as a previously tested control sample, such as a group of patients with known prognosis or outcome, or group of samples that represent baseline or normal values). A difference between a test sample and a control can be an increase or conversely a decrease. The difference can be a qualitative difference or a quantitative difference, for example a statistically significant difference. In some examples, a difference is an increase or decrease, relative to a control, of at least about5%, such as at least about 10%, at least about at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at 80%, at least about 90%, at least about 100%, at least about 150%, at least about 200%, at least about 250%, at least about 300%, at least about 350%, at least about 400%, at least about 500%, or greater than 500%. CRISPR (Clustered Regularly InterSpaced Short Palindromic Repeats) / Cas (CRISPR-associated protein) Editing System: An engineered nuclease system based on a bacterial system that is used for genome engineering. It is based in part on the adaptive immune response of many bacteria and archaea. Such methods can be used to allow genetic material to be added, removed, or altered at particular locations, for example in a target DNA or RNA sequence (such as a La nucleic acid sequence). Thus, CRISPR / Cas systems can be used for nucleic acid targeting (such as DNA or RNA), for example to detect a target DNA or RNA, modify a target DNA or RNA at any desired location, or cut the target DNA or RNA at any desired location. Thus, such methods can be used to modify expression of a HERV-K Gag, Pol or Env, for example by introducing a mutation to silene expression, such as knocking out the La gene. In one example, the method edits DNA, such as a genome, and uses a Cas9 nuclease. Cas9 nuclease cleaves the DNA to generate blunt ends at the double-strand break at sites specified by a 20-nucleotide complementary strand sequence contained within the crRNA transcript. Thus, a CRISPR / Cas system can be engineered to create a double-strand break at a desired target in a genome of a cell, and harness the cell's endogenous mechanisms to repair the induced break by homology-directed repair (HDR) or nonhomologous end-joining (NHEJ). In another example, the method edits RNA, such as a an HERV-K Gag, Pol or Env RNA, and uses a Cas13 nuclease. Exemplary Cas13 nucleases (also referred to as CasM) include Cas13a, Cas13b, Cas13c, Cas13Rx, Cas13x, and Cas13y (see for example WO 2019 / 040664, US 11,293,011, and US 10,392,616). In some examples, a CRISPR array includes at least a DR-spacer-DR-spacer. This feature was used to identify the Cas13Rx protein family. In bacteria, the array is transcribed as one single transcript (containing multiple crRNA units), which is then processed by the Cas13Rx protein and other RNases into individual crRNAs. CRISPRs are often associated with cas genes that code for proteins related to CRISPRs (such as the Cas13Rx proteins). A CRISPR / Cas system can be used for RNA targeting, for example, to modify a target HEV-K RNA at any desired location. Degenerate variant: A polynucleotide encoding a peptide that includes a sequence that is degenerate as a result of the genetic code. There are 20 natural amino acids, most of which are specified by more than one codon. Therefore, all degenerate nucleotide sequences are included in this disclosure as long as the amino acid sequence of the polypeptide encoded by the nucleotide sequence is unchanged. Downregulated or knocked down: When used in reference to the expression of a molecule, such as a target RNA, refers to any process which results in a decrease in production of the target RNA, but in some examples not complete elimination of the target RNA product or target RNA function. In one example, downregulation or knock down does not result in complete elimination of detectable target RNA expression or target RNA activity. In some examples, the target RNA is a coding HERV-K RNA. In someexamples, the target RNA is non-coding HERV-K RNA. Downregulation or knock down includes any decrease in the target HERV-K RNA. In certain examples, detectable target HERV-K RNA in a cell or cell free system decreases by at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% (such as a decrease of 40% to 90%, 40% to 80% or 50% to 95%) as compared to a control (such an amount of target HERV-K RNA detected in a corresponding normal cell or sample). In one example, a control is a relative amount of expression in a cell that does not include Cas13 or guide RNA). Emtricitabine; 2'-deoxy-5-fluoro-3'thiacytidine (FTC). FTC is sold under the trade name EMTRIVA® (emtricitabine) formerly COVIRACIL®), is a nucleoside reverse transcriptase inhibitor (NRTI) used in the treatment of HIV infection in adults and children. Emtricitabine is also marketed in a fixed-dose combination with tenofovir disproxil fumerate (Viread) under the brand name TRUVADA®. A fixed-dose triple combination of emtricitabine, tenofovir and efavirenz (Sustiva, marketed by Bristol-Myers Squibb) was approved by the U.S. Food and Drug Administration (FDA) under the name ATRIPLA®. Emtricitabine makes up one fourth of the four drug (“Quad”) combination known as STRIBILD®. Expression Control Sequences: Nucleic acid sequences that regulate the expression of a heterologous nucleic acid sequence to which it is operatively linked. Expression control sequences are operatively linked to a nucleic acid sequence when the expression control sequences control and regulate the transcription and, as appropriate, translation of the nucleic acid sequence. Thus, expression control sequences can include appropriate promoters, enhancers, transcription terminators, a start codon (i.e., ATG) in front of a protein-encoding gene, splicing signal for introns, maintenance of the correct gene reading frame to permit proper translation of mRNA, and stop codons. The term “control sequences” includes, at a minimum, components whose presence can influence expression, and can also include additional components whose presence is advantageous, for example, leader sequences and fusion partner sequences. Expression control sequences can include a promoter. A promoter is a minimal sequence sufficient to direct transcription. Also included are those promoter elements which are sufficient to render promoter-dependent gene expression controllable for cell- type specific, tissue-specific, or inducible by external signals or agents; such elements may be located in the 5' or 3' regions of the gene. Both constitutive and inducible promoters are included (see e.g., Bitter et al., 1987, Methods in Enzymology 153, 516-544). For example, when cloning in bacterial systems, inducible promoters such as pL of bacteriophage lambda, plac, ptrp, ptac (ptrp-lac hybrid promoter) and the like can be used. In one aspect, when cloning in mammalian cell systems, promoters derived from the genome of mammalian cells (such as the metallothionein promoter) or from mammalian viruses (such as the retrovirus long terminal repeat; the adenovirus late promoter; the vaccinia virus 7.5K promoter) can be used. Promoters produced by recombinant DNA or synthetic techniques can also be used to provide for transcription of the nucleic acid sequences.Heterologous: Originating from a different source, so that the biological components are not found together in nature. The components may cells, genes, or regulatory regions, such as promoters. Although the heterologous components are not found together in nature, they can function together, such as when a promoter heterologous to a gene is operably linked to the gene. Host cells: Cells in which a vector can be propagated and its DNA expressed. The cell may be prokaryotic or eukaryotic. The cell can be mammalian, such as a human cell. The term also includes any progeny of the subject host cell. It is understood that all progeny may not be identical to the parental cell since there may be mutations that occur during replication. However, such progeny are included when the term “host cell” is used. In one example a host cell is a retinal cell. Human Endogenous Retrovirus (HERV): Endogenous viral elements in the human genome that closely resemble and can be derived from retroviruses, and make up about 8% of the genome. ERVs are a vertically inherited proviral sequences. ERVs lack most transposon functions, are typically not infectious and are often defective genomic remnants of the retroviral replication cycle. They are distinguished as germline provirus retroelements due to their integration and reverse-transcription into the nuclear genome of the host cell. There are over 200 distinct groups and subgroups of HERVs. Most HERVs have lost infectivity due to mutations, and in general they are largely noninfectious retroviral remnants. However, open reading frames (ORFs) have been observed for ERV3, HERV-E 4-1, and HERV-K. The members of the HERV-K superfamily, which is characterized by the presence of primer binding sites for lysine tRNA, are the most biologically active. HERV-K seems to have the full complement of open reading frames typical of replication competent mammalian retroviruses. The K family contains a central open reading frame (cORF) and is comparable to HIV-1 Rev protein. HERV-K is transcribed during embryogenesis from the eight cell stage up to the stem cell derivation. HERV-K also is transcriptionally active in several human cancer tissues, including breast cancer tissues, as well as tumor cell lines, such as the human breast cancer cell line T47D and the teratocarcinoma cell line GH, see U.S. Published Patent Application No.2008 / 0019979A1. Inhibiting or treating a disease: Inhibiting a disease, such as, but not limited to, AMD, refers to inhibiting the full development of a disease. In several examples, inhibiting a disease refers to lessening symptoms of the particular disease. “Treatment” refers to a therapeutic intervention that ameliorates a sign or symptom of a disease or pathological condition related to the disease. Treatment can be measured using success or indicia of success in the attenuation or amelioration of an injury, pathology or condition, including any objective or subjective parameter such as abatement, remission, diminishing of symptoms or making the condition more tolerable to the patient, slowing in the rate of degeneration or decline, making the final point of degeneration less debilitating, improving a subject’s physical state. The treatment may be assessed by objective or subjective parameters; including the results of a physical examination or tests, such as vision tests. Inhibitory nucleic acid molecules: Includes inhibitory RNA and DNA molecules, such as an antisense oligonucleotide, a siRNA, a microRNA (miRNA), a shRNA or a ribozyme. Any type of antisensecompound that specifically targets and regulates of a nucleic acid encoding Gag, Pol or Env of HERV-K is contemplated for use. An antisense is one which specifically hybridizes with and modulates expression of a Gag, Pol or Env nucleic acid molecule. These compounds can be introduced as single-stranded, double-stranded, circular, branched or hairpin compounds and can contain structural elements such as internal or terminal bulges or loops. Double-stranded antisense compounds can be two strands hybridized to form double-stranded compounds or a single strand with sufficient self- complementarity to allow for hybridization and formation of a fully or partially double-stranded compound. In some examples, an antisense oligonucleotide is a single stranded antisense compound, such that when the antisense oligonucleotide hybridizes to a mRNA encoding Gag, Pol or Env protein and the resulting duplex is recognized by RNaseH, resulting in cleavage of the mRNA. In some examples, a miRNA is a single- stranded RNA molecule, such as about 21-23 nucleotides in length that is at least partially complementary to an mRNA molecule that regulates gene expression through an RNAi pathway. In further examples, a shRNA is an RNA oligonucleotide that forms a tight hairpin, which is cleaved into siRNA. siRNA molecules are generally about 15-40 nucleotides in length, such as 20-25 nucleotides in length, and may have a 0 to 5 nucleotide overhang on the 3' or 5’ end, or may be blunt ended. Generally, one strand of a siRNA is at least partially complementary to a nucleic acid molecule encoding Gag, Pol or Env. Antisense compounds specifically targeting a Gag, Pol or Env gene can be prepared by designing compounds that are complementary to a target nucleotide sequence, such as an mRNA sequence. Antisense compounds need not be 100% complementary to the nucleic acid molecule encoding Gag, Pol or Env to specifically hybridize and regulate expression of the target. For example, the antisense compound, or antisense strand of the compound if a double-stranded compound, can be at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 99% or 100% complementary to a nucleic acid molecule encoding Gag, Pol or Env. Methods of screening antisense compounds for specificity are known (see, for example, U.S. Inhibitory peptide: A blocking peptide competitively inhibits protein-protein interaction by mimicking one of their binding domains, or “binding epitopes.” The term mimicking epitope, or “mimotope,” and refers to a peptide macromolecule that reproduced, or “mimicked,” the epitope structure that elicits the same specific antibody response as the intact macromolecule from which it was derived. The term includes peptides that competitively interrupt protein-protein interactions by binding to one of the partner’s binding domains, including those that interfere with protein-protein interactions. Isolated: An “isolated” biological component (such as a nucleic acid molecule or protein or organelle) has been substantially separated or purified away from other biological components in the cell of the organism in which the component naturally occurs, i.e., other chromosomal and extra-chromosomal DNA and RNA, proteins and organelles. Nucleic acids and proteins that have been “isolated” include nucleic acids and proteins purified by standard purification methods. The term also embraces nucleic acids and proteins prepared by recombinant expression in a host cell as well as chemically synthesized nucleic acids and proteins.Label: A detectable compound or that is conjugated directly or indirectly to another molecule to facilitate detection of that molecule. non-limiting examples of labels include fluorescent tags, enzymatic linkages, and radioactive isotopes. Mammal: This term includes both human and non-human mammals. Similarly, the term “subject” includes both human and veterinary subjects. Modulate: To alter in a statistically significant manner. Modulation can be an increase or a decrease. One of skill in the art can identify an appropriate assay to determine a statistically significant increase or decrease in a parameter. These include, but are not limited to, a student’s t-test or a paired ratio t test. Nucleic acid molecule: A polymer composed of nucleotide units (ribonucleotides, deoxyribonucleotides, related naturally occurring structural variants, and synthetic non-naturally occurring analogs thereof) linked via phosphodiester bonds, related naturally occurring structural variants, and synthetic non-naturally occurring analogs thereof. Thus, the term includes nucleotide polymers in which the nucleotides and the linkages between them include non-naturally occurring synthetic analogs, such as, for example and without limitation, phosphorothioates, phosphoramidates, methyl phosphonates, chiral-methyl phosphonates, 2-O-methyl ribonucleotides, peptide-nucleic acids (PNAs), and the like. Such polynucleotides can be synthesized, for example, using an automated DNA synthesizer. The term “oligonucleotide” typically refers to short polynucleotides, generally no greater than about 50 nucleotides. It will be understood that when a nucleotide sequence is represented by a DNA sequence (i.e., A, T, G, C), this also includes an RNA sequence (i.e., A, U, G, C) in which “U” replaces “T.” Conventional notation is used herein to describe nucleotide sequences: the left-hand end of a single- stranded nucleotide sequence is the 5'-end; the left-hand direction of a double-stranded nucleotide sequence is referred to as the 5'-direction. The direction of 5' to 3' addition of nucleotides to nascent RNA transcripts is referred to as the transcription direction. The DNA strand having the same sequence as an mRNA is referred to as the “coding strand;” sequences on the DNA strand having the same sequence as an mRNA transcribed from that DNA and which are located 5' to the 5'-end of the RNA transcript are referred to as “upstream sequences;” sequences on the DNA strand having the same sequence as the RNA and which are 3' to the 3' end of the coding RNA transcript are referred to as “downstream sequences.” “cDNA” refers to a DNA that is complementary or identical to an mRNA, in either single stranded or double stranded form. “Encoding” refers to the inherent property of specific sequences of nucleotides in a polynucleotide, such as a gene, a cDNA, or an mRNA, to serve as templates for synthesis of other polymers and macromolecules in biological processes having either a defined sequence of nucleotides (i.e., rRNA, tRNA and mRNA) or a defined sequence of amino acids and the biological properties resulting therefrom. Thus, a gene encodes a protein if transcription and translation of mRNA produced by that gene produces the protein in a cell or other biological system. Both the coding strand, the nucleotide sequence of which is identical to the mRNA sequence and is usually provided in sequence listings, and non-coding strand, used as thetemplate for transcription, of a gene or cDNA can be referred to as encoding the protein or other product of that gene or cDNA. Unless otherwise specified, a sequence encoding an amino acid sequence" includes all nucleotide sequences that are degenerate versions of each other and that encode the same amino acid sequence. Nucleotide sequences that encode proteins and RNA may include introns. “Recombinant nucleic acid” refers to a nucleic acid having nucleotide sequences that are not naturally joined together. This includes nucleic acid vectors comprising an amplified or assembled nucleic acid which can be used to transform a suitable host cell. A host cell that comprises the recombinant nucleic acid is referred to as a “recombinant host cell.” The gene is then expressed in the recombinant host cell to produce, such as a “recombinant polypeptide.” A recombinant nucleic acid may serve a non-coding function (such as a promoter, origin of replication, ribosome-binding site, etc.) as well. A first sequence is an “antisense” with respect to a second sequence if a polynucleotide whose sequence is the first sequence specifically hybridizes with a polynucleotide whose sequence is the second sequence. Terms used to describe sequence relationships between two or more nucleotide sequences or amino acid sequences include “reference sequence,” “selected from,” “comparison window,” “identical,” “percentage of sequence identity,” “substantially identical,” “complementary,” and “substantially complementary.” For sequence comparison of nucleic acid sequences, typically one sequence acts as a reference sequence, to which test sequences are compared. When using a sequence comparison algorithm, test and reference sequences are entered into a computer, subsequence coordinates are designated, if necessary, and sequence algorithm program parameters are designated. Default program parameters are used. Methods of alignment of sequences for comparison are well known in the art. Optimal alignment of sequences for comparison can be conducted, for example, by the local homology algorithm of Smith & Waterman, Adv. Appl. Math.2:482, 1981, by the homology alignment algorithm of Needleman & Wunsch, J. Mol. Biol. 48:443, 1970, by the search for similarity method of Pearson & Lipman, Proc. Nat’l. Acad. Sci. USA 85:2444, 1988, by computerized implementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group, 575 Science Dr., Madison, WI), or by manual alignment and visual inspection (see for example, Current Protocols in Molecular Biology (Ausubel et al., eds 1995 supplement)). Nucleoside analog reverse-transcriptase inhibitors (NRTIs): The initial class of antiretroviral drugs that was developed. In order to be incorporated into the viral DNA, NRTIs must be activated in the cell by the addition of phosphate groups to their deoxyribose moiety, to form NRTI triphosphates. This phosphorylation step is carried out by cellular kinase enzymes. NRTIs include zidovudine, didanosine, zalcitabine, stavudine, lamivudine, abacavir, and emtricitabine (also called FTC). Nucleotide analog reverse-transcriptase inhibitors (NtRTIs): NTARTIs and NtRTIs are nucleotide analogues of cytidine, guanosine, thymidine, and adenosine that are of use in treatment of HIV infections. For example, tenofovir (and its related prodrugs) is an NtRTI adenosine analogue.Open reading frame (ORF): A series of nucleotide triplets (codons) coding for amino acids without any internal termination codons. These sequences are usually translatable into a protein. Operably linked: A first nucleic acid sequence is operably linked with a second nucleic acid sequence when the first nucleic acid sequence is placed in a functional relationship with the second nucleic acid sequence. For instance, a promoter is operably linked to a coding sequence if the promoter affects the transcription or expression of the coding sequence, such as a sequence that encodes a polypeptide. Generally, operably linked DNA sequences are contiguous and, where necessary to join two protein-coding regions, in the same reading frame. Pharmaceutically acceptable carriers: The pharmaceutically acceptable carriers of use are conventional. Remington’s Pharmaceutical Sciences, by E. W. Martin, Mack Publishing Co., Easton, PA, 15th Edition (1975), describes compositions and formulations suitable for pharmaceutical delivery of the therapeutic agents herein disclosed. In general, the nature of the carrier will depend on the particular mode of administration being employed. For instance, parenteral formulations usually comprise injectable fluids that include pharmaceutically and physiologically acceptable fluids such as water, physiological saline, balanced salt solutions, aqueous dextrose, glycerol or the like as a vehicle. For solid compositions (such as powder, pill, tablet, or capsule forms), conventional non-toxic solid carriers can include, for example, pharmaceutical grades of mannitol, lactose, starch, or magnesium stearate. In addition to biologically neutral carriers, pharmaceutical compositions to be administered can contain minor amounts of non-toxic auxiliary substances, such as wetting or emulsifying agents, preservatives, and pH buffering agents and the like, for example sodium acetate or sorbitan monolaurate. Pharmacoenhancer: A substance that increases the bioavailability and bioefficacy of active substances with which they are combined without having any activity of their own at the dose used. These agents are also known as “bioenhancers.” Increased bioavailability means increased levels of an agent, such as in the blood. Increased bioefficacy means the increased effectiveness of the drug due to, at least in part, to increased bioavailability. COBI is a pharmacoenhancer. Polypeptide: Any chain of amino acids, regardless of length or post-translational modification (e.g., glycosylation or phosphorylation). With regard to polypeptides and proteins, the word “about” indicates integer amounts. Thus, in one example, a polypeptide “about” 29 amino acids in length is from 28 to 30 amino acids in length. Thus, a polypeptide “about” a specified number of residues can be one amino acid shorter or one amino acid longer than the specified number. A fusion polypeptide includes the amino acid sequence of a first polypeptide and a second different polypeptide (for example, a heterologous polypeptide), and can be synthesized as a single amino acid sequence. A recombinant polypeptide has an amino acid sequence that is not naturally occurring or that is made by two otherwise separated segments of an amino acid sequence.Promoter: An array of nucleic acid control which direct transcription of a nucleic acid. A promoter includes necessary nucleic acid sequences near the start site of transcription, such as, in the case of a polymerase II type promoter, a TATA element. A promoter also optionally includes distal enhancer or repressor elements which can be located as much as several thousand base pairs from the start site of transcription. A promoter can be a constitutively active promoter (i.e., a promoter that is constitutively in an active / "ON" state), an inducible promoter (i.e., a promoter whose state, active / "ON" or inactive / "OFF", is controlled by an external stimulus, e.g., the presence of a particular temperature, compound, or protein.), a spatially restricted promoter (e.g., tissue specific promoter, cell type specific promoter, etc.), or it may be a temporally restricted promoter (i.e., the promoter is in the "ON" state or "OFF" state during specific stages of embryonic development or during specific stages of a biological process). RPE specific promoters can be used to drive expression specifically in the RPE. Some examples include promoters for genes like DCT (ID#1638), tyrosinase (ID#7299), VMD2 (ID #7439), RPE65 (ID#6121). Promoters specific for choroid can also be used, examples include Carbonic Anhydrase 4 (ID# 762), PLVAP (ID# 83483). Photoreceptor specific promoter examples include – Rhodopsin (ID# 6010), NR2E3 (ID# 10002) and NRL (ID# 4901). Purified: The term “purified” does not require absolute purity; rather, it is intended as a relative term. Thus, for example, a purified protein preparation is one in which the protein referred to is purer than the protein in its natural environment within a cell. For example, a preparation of a protein is purified such that the protein represents at least 50% of the total protein content of the preparation. Similarly, a purified nucleic acid molecule preparation is one in which the nucleic acid molecule is purer than in an environment including a complex mixture. A purified population of nucleic acids or proteins is greater than about 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% pure, or free other nucleic acids or proteins, respectively. RNA Editing: A type of genetic engineering in which an RNA molecule (or ribonucleotides of the RNA) is inserted, deleted or replaced in the genome of an organism using engineered nucleases (such as Cas13Rx proteins), which create site-specific strand breaks at desired locations in the RNA. The induced breaks are repaired resulting in targeted mutations or repairs. The CRISPR / Cas methods disclosed herein, such as those that use a Cas13Rx protein and a gRNA specific for HERV-K, can be used to edit the sequence of one or more target HERV-K RNAs. Sequence identity: The similarity between amino acid sequences is expressed in terms of the similarity between the sequences, otherwise referred to as sequence identity. Sequence identity is frequently measured in terms of percentage identity (or similarity or homology); the higher the percentage, the more similar the two sequences are. Homologs or variants of a polypeptide will possess a relatively high degree of sequence identity when aligned using standard methods. Methods of alignment of sequences for comparison are known t. Various programs and alignment algorithms are described in: Smith and Waterman, Adv. Appl. Math.2:482, 1981; Needleman and Wunsch, 1970, J Mol Biol 48, 443-453; Higgins and Sharp, 1988, Gene 73, 237-244; Higgins and Sharp, 1989, CABIOS 5, 151-153; Corpet et al., 1988, Nucleic Acids Research 16, 10881-10890; and Pearson and Lipman,1988, Proc Natl Acad Sci USA 85, 2444-2448. Altschul et al., 1994, Nature Genet 6, 119-129, presents a detailed consideration of sequence alignment and homology calculations. The NCBI Basic Local Alignment Search Tool (BLAST) (Altschul et al., 1990, J Mol Biol 215, 403- 410) is available from several sources, including the National Center for Biotechnology Information (NCBI, Bethesda, MD) and on the internet, for use in connection with the sequence analysis programs blastp, blastn, blastx, tblastn and tblastx. A description of how to determine sequence identity using this program is available on the NCBI website on the internet. Homologs and variants of a polypeptide are typically characterized by possession of at least 75%, for example at least 80%, sequence identity counted over the full length alignment with the amino acid sequence of a polypeptide using the NCBI Blast 2.0, gapped blastp set to default parameters. For comparisons of amino acid sequences of greater than about 30 amino acids, the Blast 2 sequences function is employed using the default BLOSUM62 matrix set to default parameters, (gap existence cost of 11, and a per residue gap cost of 1). When aligning short peptides (fewer than around 30 amino acids), the alignment should be performed using the Blast 2 sequences function, employing the PAM30 matrix set to default parameters (open gap 9, extension gap 1 penalties). Proteins with even greater similarity to the reference sequences will show increasing percentage identities when assessed by this method, such as at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or at least 99% sequence identity. When less than the entire sequence is being compared for sequence identity, homologs and variants will typically possess at least 80% sequence identity over short windows of 10-20 amino acids, and can possess sequence identities of at least 85% or at least 90% or 95% depending on their similarity to the reference sequence. Methods for determining sequence identity over such short windows are available at the NCBI website on the internet. These sequence identity ranges are provided for guidance only; it is entirely possible that strongly significant homologs could be obtained that fall outside of the ranges provided. Thus, in some examples, variants of a polypeptide or nucleic acid sequence are typically characterized by possession of at least about 75%, for example, at least about 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity counted over the full length alignment with the amino acid or nucleotide sequence of interest. Sequences with even greater similarity to the reference sequences will show increasing percentage identities when assessed by this method, such as at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or at least 99% sequence identity. When less than the entire sequence is being compared for sequence identity, homologs and variants will typically possess at least 80% sequence identity over short windows of 10-20 amino acids (or 30-60 nucleotides), and may possess sequence identities of at least 85% or at least 90% or 95% depending on their similarity to the reference sequence. Methods for determining sequence identity over such short windows are available at the NCBI website on the internet. As used herein, reference to “at least 90% identity” (or similar language) refers to “at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or even 100% identity” to a specified reference sequence.Subject: Living multi-cellular vertebrate a category that includes human and non- human mammals, such as non-human primates, rats, dogs, cats, horses, cows and pigs. In a specific aspect, a subject is a human. In an additional aspect, a subject is selected that has AMD. Tenofovir Prodrugs: Tenofovir (9-R-[(2-phosphonomethoxy)propyl]adenine), an acyclic nucleotide analog of dAMP, is a potent in vitro and in vivo inhibitor of human immunodeficiency virus type 1 (HIV-1) replication. Tenofovir is sequentially phosphorylated in the cell by AMP kinase and nucleoside diphosphate kinase to the active species, tenofovir diphosphate, which acts as a competitive inhibitor of HIV-1 reverse transcriptase that terminates the growing viral DNA chain. Tenofovir disoproxil fumarate (TDF) is an oral prodrug of tenofovir, marketed as VIREAD®, that has received marketing authorization in many countries as a once-daily tablet (300 mg) in combination with other antiretroviral agents for the treatment of HIV-1 infection. U.S. Patent No.7,390,791 and U.S. Pat. No.7,803,788, both incorporated herein by reference, disclose prodrugs of phosphonate nucleotide analogs that are also useful in therapy. 9-[(R)-2-[[(S)-[[(S)-1- (isopropoxycarbonyl)ethyl]amino] phenoxyphosphinyl]-methoxy]propyl]adenine 16 is an isopropylalaninyl phenyl ester prodrug of tenofovir. Tenofovir alafenamide (TAF) is also known as GS-7340. TAF has been marketed under the name VEMLIDY®. The hemifumarate form of TAF is also of use in the methods disclosed herein. TAF exhibits potent anti-HIV activity 500- to 1000-fold enhanced activity relative to tenofovir against HIV-1 in T cells, activated peripheral blood mononuclear lymphocytes (PBMCs), and macrophages. TAF also has enhanced ability to deliver and increase the accumulation of the parent tenofovir into PBMCs and other lymphatic tissues in vivo. TAF can be prepared as described in U.S. Pat. No. 7,390,791, incorporated herein by reference. FTC / TAF / EVG / COBI, also called GENVOYA® (which contains 150 mg EVG, 150 mg COBI, 200 mg FTC, and 10 mg TAF) is approved for the treatment of an existing HIV infections in subjects. EVG, FTC and TAF have been shown to suppress viral reproduction. Cobicistat increases the effectiveness of the combination, such as by inhibiting the liver and gut wall enzymes that metabolize EVG. The use of FTC / TAF / EVG / COBI for treatment of an existing HIV infection is disclosed, for example, in U.S. Patent Publication U.S.2015 / 0105350 entitled “Combination Therapy Comprising Tenofovir Alafenamide Hemifumarate and Cobicistat for Use in the Treatment of Viral Infections,” which is incorporated herein by reference. A FTC / TAF / EVG / COBI combination drug is manufactured, and is commercially available from, Gilead Sciences. Therapeutically effective amount: A quantity of a composition or a cell to achieve a desired effect in a subject being treated. For instance, this can be the amount necessary to inhibit vision loss and / or retinal degeneration. When administered to a subject, a dosage will generally be used that will achieve target tissue concentrations that has been shown to achieve an in vitro effect. A therapeutically effective amount may vary depending upon one or more of: the subject and disease condition being treated, the weight and age of the subject, the severity of the AMD, the manner of administration and the like, which can readily be determined by one of ordinary skill in the art. Thebeneficial therapeutic effect can include enablement of diagnostic determinations; amelioration of the AMD symptoms, improvement of vision, or delay in reducing or preventing the onset of AMD symptoms. In one aspect, an “effective amount” is an amount sufficient to reduce symptoms of AMD, for example by at least 10%, at least 20%, at least 50%, at least 70%, or at least 90% (as compared to no administration of the therapeutic agent), or that delays onset or progression. The term also applies to a dose that will allow for expression of a Cas13 and / or gRNA herein, and that allows for targeting (e.g., detection or modification) of a target HERV-K RNA. Transfer (t)RNA: An adaptor molecule composed of RNA, typically 76 to 90 nucleotides in length, that carries an amino acid to the ribosome. Complementation of a 3-nucleotide codon in a mRNA by the anti-codon in the tRNA results is protein synthesis. In the human genome there are 497 nuclear genes encoding cytoplasmic tRNA molecules. Cytoplasmic tRNA genes can be grouped into 49 families according to their anticodon features. Shorter molecules are produced after cleavage of mature tRNAs. When cleaved by ANG, the molecules have a characteristically unusual cyclic phosphate at their 3’ end and a hydroxyl group at the 5’ end, and play a role in RNA interference, specifically in the suppression of retroviruses and retrotransposons that use tRNA as a primer for replication. These molecules are called tiRNA or tRFs (see below) (see Schorn and Martienssen, Trends Cell Biol.28(10): 793-906, 2018). tRNA-derived stress-induced RNAs (tiRNAs) or tRNA fragments (tRFs): A class of small noncoding RNAs produced through specific cleavage of tRNA by endonucleases. tRNA-derived fragments are classified into two major types: tRNA halves (also known as tiRNAs) and smaller tRNA fragments, based on their enzyme cleavage site. tiRNAs, as an important subtype of tRNA-derived fragments, are generated by angiogenin, see Tao et al., J Cell Physiol.235:683–690, 2020. Unit dosage form: A physically discrete unit, such as a capsule, tablet, or solution, that is suitable as a unitary dosage for a human patient, each unit containing a predetermined quantity of one or more active ingredient(s) calculated to produce a therapeutic effect, in association with at least one pharmaceutically acceptable diluent or carrier, or combination thereof. Unit dosage formulations contain a daily dose or an appropriate fraction thereof, of the active ingredient(s). tRNA-derived fragments (or tRFs) are short molecules that emerge after cleavage of the mature tRNAs or the precursor transcript. Up Regulation and Knock-In: When used in reference to the expression of a molecule, such as a target, “up regulation” refers to any process which results in an increase in production of an RNA of interest. In one example, upregulation increases detectable RNA expression or RNA activity. A “knock-in” is an increase in expression due to the introduction of a nucleic acid molecule encoding a protein of interest, such as ANG, tRNA, or a tRNA fragment. Upregulation includes any detectable increase in the RNA. In certain examples, detectable RNA in a cell or cell free system increases by at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% (such as a decrease of 40% to 90%, 40% to 80% or 50% to 95%) as compared to a control (such an amount of ANG RNA detected in a corresponding non-treated cell or sample).Vector: A nucleic acid molecule as introduced into a host cell, thereby producing a transformed host cell. A vector may include nucleic acid sequences that permit it to replicate in a host cell, such as an origin of replication. A vector may also include one or more selectable marker gene and other genetic elements known in the art. Vectors include plasmid vectors, including plasmids for expression in gram- negative and gram-positive bacterial cell. Exemplary vectors include those for expression in E. coli and Salmonella. Vectors also include viral vectors, such as, but are not limited to, retrovirus, lentiviral, adeno- associated virus (AAV), orthopox, avipox, fowlpox, capripox, suipox, adenoviral, herpes virus, alpha virus, baculovirus, Sindbis virus, vaccinia virus and poliovirus vectors. Vectors also include vectors for expression in yeast cells or mammalian cells. In some aspects, the vector is a lentivirus (such as an integration-deficient lentiviral vector) or adeno-associated viral (AAV) vector. Certain vectors are capable of directing the expression of genes to which they are operatively-linked. Such vectors are referred to herein as "expression vectors." Common expression vectors are often in the form of plasmids. Recombinant expression vectors can comprise a nucleic acid provided herein (such as a guide RNA (which can be expressed from an RNA sequence or a RNA sequence), nucleic acid encoding a Cas13Rx protein) in a form suitable for expression of the nucleic acid in a host cell, which means that the recombinant expression vectors include one or more regulatory elements, which may be selected on the basis of the host cells to be used for expression, that is operatively-linked to the nucleic acid sequence to be expressed. Within a recombinant expression vector, "operably linked" is intended to mean that the nucleotide sequence of interest is linked to the regulatory element(s) in a manner that allows for expression of the nucleotide sequence (e.g., in an in vitro transcription / translation system or in a host cell when the vector is introduced into the host cell). It will be appreciated by those skilled in the art that the design of the expression vector can depend on such factors as the choice of the host cell to be transformed, the level of expression desired, etc. A vector can be introduced into host cells to thereby produce transcripts, proteins, or peptides, including fusion proteins or peptides, encoded by nucleic acids as described herein (e.g., clustered regularly interspersed short palindromic repeats (CRISPR) transcripts, proteins, enzymes, mutant forms thereof, fusion proteins thereof, etc.). Virus: Microscopic infectious organism that reproduces inside living cells. A virus consists essentially of a core of a single nucleic acid surrounded by a protein coat and has the ability to replicate only inside a living cell. “Viral replication” is the production of additional virus by the occurrence of at least one viral life cycle. “Retroviruses” are RNA viruses wherein the viral genome is RNA. When a host cell is infected with a retrovirus, the genomic RNA is reverse transcribed into a DNA intermediate which is integrated very efficiently into the chromosomal DNA of infected cells. The integrated DNA intermediate is referred to as a provirus. A wild-type retrovirus genome encodes a polymerase, glycosaminoglycan, and an envelope protein. The term "lentivirus" is used in its conventional sense to describe a genus of viruses containing reverse transcriptase. The lentiviruses include the “immunodeficiency viruses” which include humanimmunodeficiency virus (HIV) type 1 and type 2 I and HIV-II), simian immunodeficiency virus (SIV), and feline immunodeficiency virus (FIV). II. Agents that Inhibit HERV-K Methods are disclosed herein for treating AMD in a subject, and for reducing the risk of developing AMD. In some aspects, the method can reduce retinal degeneration, and / or halt vision loss or improve vision, for example by at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 75%, at least 90%, at least 95%, at least 100%, at least 200%, or even at least 500%. These methods use one or more agents that reduce or inhibit HERV-K activity, for example by at least 20%, at least 30%, at least 40%, at least 50%, at least 75%, at least 90%, at least 95%, or 100%. In some aspects, 100% inhibition of HERV-K activity is not required for the disclosed methods of treating AMD. An agent that treats, or reduces the risk of AMD in a subject can reduce one or more of a) the amount of human endogenous retrovirus (HERV)-K, b) production of an mRNA encoding a HERV-K protein, c) translation of the mRNA; d) the amount of an HERV-K protein in the subject ; e) inhibit activity of HERV-K mRNA and / or proteins, or any combination of a, b, c, d, and e. Exemplary agents are disclosed below, and can be used in any combination. In some aspects, an agent that inhibits HERV-K reduces the amount of HERV-K in a subject, such as locally in the retina of the subject. In other aspects, the agent is administered systemically. Suitable agents are discussed in more detail below. In addition, the treatments listed below can be used in any combination. In sone aspects, an anti-retroviral agent is administered in combination with CRISPR / Cas13 system. In some aspects, the treatment reduces the amount of, activity of proteins, and / or reduces virus mRNA. Inhibitory peptides are of use. Inhibitory peptides are also disclosed, for example, in Hoffman et al., J. Virol.94(23) e01682-20, 2000, incorporated herein by reference. Inhibitory peptides are also available for HIV (see Egerer et al., Mol. Ther.19(7):1236-1244, 2011), and other retroviruses (see Kotler et al., PNAS 85:4185-4189, 1988). In one aspect, the agent that inhibits KERV-K is ANG, such as a vector expressing ANG. A. Antibodies and Antigen Binding Fragments Thereof In some aspects, the agent is an antibody or an antigen binding fragment thereof, that specifically binds an HERV-K protein, such as, but not limited to, a monoclonal antibody that specifically binds Gag, Pol or Env of HERV-K. An exemplary complete nucleic acid sequence for HERV-K is: TGTGGGGAAAAGCAACAGAGGTCAGATTGTTACTGTGTCTGTATAGAAAGAAGTAGACATAGGAGACTCCATTTTGT TCTGTACTAAGAAAAATTATTCTGCCTTGAGATGCTGTTAATCTATGACCTTACCCCCAACCCCGTGCTCTCTGAAACA TGTGCTGTGTCAAACTCAGGGTTAAATGGATTAAGGGCGGTGCAAGATGTGCTTTGTTAAACAGATGCTTGAAGGCAGCATGCTCATTAAGAGTCATCACCACTCCCTAATCTCAAGTACCCAGGGACACAAAAACTGCGGAAGGCTGCAGGGGCCTCTGCCTAGGAAAGCCAGGTATTGTCCAAGGTTTCTCCCCATGTGAGAGTCTGAAATATGGCCTCGTGGGAAGGGAA AGACCTGACCGTCCCCCAGCCCGACACCCATAAAGGGTCTGTGCTGAGGAGGATTAGTATAAGAGGAAAGCATGCCT CTTGCAGTTGAGACAAGAGGAAGGCATCTGTTTCCCACCCATCCCTGGGCAATGGAATGTCTCGGTATAAAACCCGAT TGTACGTTCCACCTACTGAGATAGGGAGAAACCACCTTAGGGCTGGAGGTGGGACATGCAGGCAGCAATACTGCTTT GTAAAGCATTGAGATGTTTATGTGTATGCATATCTAAAAGCACAGCATTTAATCCTTTACCTTGTCTATGATGCAAAGACCTTTGTTCACGTGTTTGTCTGCTCACCCTCTCCCCACTATTGTCTTGTGACCCTGACACATCTCCCTCTCAGAGAAAC GGCCCCCTTATTTCTTTCTCTATACTTTGTCTCTGTGTCTTTTTCTTTTCCAAGTCTCTCATTGCACCTTACGAGAAACAC CCACAGGTGTGGAGGGGCAACCCACCCCTTCATCTGGTGCCCAACGTGGAGGCTTTTCTCTGGGGTGAAGGTACACTCGAGCGTGGTCATTGAGGACAAGTCGACAAGAGATCCCGAGTACATCTACAGTCAGCCTTACGGTAAGCTTGTGCACTCGGAAGAAGCTAGGGTGACAATGGGGCAAACTAAAACTAAAAGTAAATATGCCTCTTATCTTAGCTTCATTAAAATT CTTTTAAAAAGAGGGGGAGTTAGAGTATCCACCAAAAATCTAATCAAGCTATTTCAAACAACAGAACAATTTTGCCC ATGGTTTCCAGAACAAGGAAATTTAGATCTAGAAGATTGGAAAAGAATTGGTAAGGAACTAAAACAAGCAGGTAGG AAGGGTAATATCATTCCACTTACAGTATGGAATGATTGGCCCATTATTAAAGCAGCTTTAGAACCATTTCAAACAGAA GATAGCGTTTCAGTTTCTGATGCCCCTGGAAGCTGTATAATAGATTGTAATGAAAAGACAAGGAAAAAATCCCAGAA GGAAACGGAAACTTTACATTGCGAATATGTAGCAGAGCCGTTAATGGCTCAGTCAACGCAAAATGTTGACTATAATC AATTACAGGAGGTGATATATCCTGAAACATTAAAATTAGAAGGAAAAGGTCCAGAATTAGTGGGGCCATTAGAGTCT AAACCACGAGGGCCAAGTCCTCTTTCAGCAGGTCAGGTGACCGTAACATTACAACCTCAAGCGCAGGTTAGAGAAAA TAAGACCCAACTGCCAGTAGCTTATCAATACTGGCCACCGGCCGAACTTCAGTATCGGCCACCCCCAGAAAGTCAGTA TGGATATCTAGGAATGCCACCAGCACCACAGGACAGGGAGCCATACCCTCAGCCGCCCACTAGGAGACAATGCTATG GCACCACCTAGTAGGCAGGGTAGTGAATTACATGAAATTATTGAGAAGTCAAGAAAGGAAGGAGATACTGAGGCGT GGCAATTCCCAGTAACGTTAGAACCGATGCCACCTGGAGAAGGAGCCCAAGAGGGAGAGCCTCTCACAGTTGAGGCC AGATAAAGGTCTTTTTAGATAAAAATGCTAAAAGATATGAAAGAGGGAGTAAAACAGTATGGACCCAACTCCCCTTA TATGAGGACATTATTAGATTCCATTGCTCATGGACATAGACTCATTCCTTATGATTGGGAGATTCTGGCAAAATCATCTCTCTCACCCTCTCAATTTTTACAATTTAAGACTTGGTGAATTGATGGGGCACAAGAACAGGTCCGAAGAAATAGGGCTGCCAATCCTCCAGTTAACATAGATGCAGATCAACTATTAGGAACAGGTCAAAATTGGAGCACTATTAGTCAACAAGC ATTAATGCAAAATGAGGCCATTGAGCAAGTTAGAGCTATCTGCCTTAGAGCCTGGGAAAAAATCCAAGACCCAGGAA GCGCCTGCTCCACATTTAATACAGTAAGACAAGGTTCAAAAGAGCCCTACCCTGATTTTGTGGCAAGGCTCCAAGATG TTGCTCAAAAGTCAATTGCCAATGAAAAAGCCCGTAAGGTCATAGTGGAGTTGATGGCATACGAAAACGCCAATCCT GAGTGTCAATCAGCCATTAAGCCATTAAAAGGAAAGGTTCCCGCAGGATCAGATGTAATCTCAGAGTATGTAAAAGC CCGTGATGGAATTGGAGGAGCTACGCATAAAGCTATGCTTATGGCCCAAGCAATAACAGGAGTTGTTTTAGGAGGAC AAGTTAGAACATTTGGAGGAAAATGTTATAATTGTGGTCAAAATGGTCATTTAAAAAAGAATTGCCCAGTCTTAAATA AACAGAATATAACTATTCAAGCTACTACAACAACAGGTAGAGAGCCACCTGACTTATGTCCAAGATGTAAAAAAGGA AAACATTGGGCTAGTCAATGTCATTCTAAATTTGATAAAAATGGGCAATCATTGTCGGGAAACTACCAAAAGGGCTAGTCAATGTCGTTCCAAATTTGATAAAAATGGGCAACCATTGTCGGGAAACTAGCAAAGGGGCCAGCCTCAGGCCCTGCAACAAACTGGGGCATTCCCAATTCAGCCCTTTGTTCCTCAGGGTTTTCAGGGACAACAACCCCCACTGTCCCAAGTA CCTCAGGGAATAAGCCAGTTACCACAGTACAACAATTGTCCCCCGCCACAAGTGGCAGTGCAGCAGTAGATTTATGT ACTATACAAGCAGTCTCTCTGCTTCCAGGGGAGCCCCCACAAAAAATCCCCACAGGAGTATATGGCCCGCTGCCTGAG GAGACTGTAGGACTAATCTTGGGAAGATCACGTCTAAATCTAAAAGGAGTTCAAATTCATACTGGTGTGGTTGATTCA GACTATAAAGGTGAAATTCAATTGGTTATTAGCTCTTCAATTCCTTGGAGTGCCAGTCCAGGAGACAGGATTGCTCGA TTATTACTCCTGCCATATATTAAGGTTGGAAATAGTGAAATAAAAAGAACAGGAGGGTTTGGAAGCACTGATCCGAC AGGAAAGGCTGCATATTGGGCAAGTCAGGTCTCAGAGAACAGACCTGTGTGTAAGGCCGTTATTCAAGGAAAACAGC TTGAAGGATTGGTAGACACTGGAGCAGATGTCTCTATCATTGCTTTAAATCAGTGGCCAAAAAATTGGCCTAAACAAA AGGCTGTTACAGGACTTGTCGGCGTAGGCACAGCCTCAGAAGTGTATCAAAGTACTGAGATTTTACATTGCTTAGGGCCACATAATCAAGAAAGTACTGTTCAGCCAATGATCACTTCAATTCCTCTTAATCTGTGGGGTCGAGATTTGTTACAACAATGGGGTGCGGAAATCACCATGACCGCTACATTATATAGCCCCATGAGTCAAAAAATTATGACCAAGATGGGATAT ATACCAGGAAAGGGACTAGGAAAAAATGAAGATGGCATTAAAGTTCCAATTGAGGCTAAAATAAATCACGGAAGAG AAGGAACAGGGTATCCTTTTTAGGGGTGACCACTGTAGAGCCTCCTAAACCCATACCGTTAACTTGGAAAACAGAAA AACTGGTGTGGGTAAATCAGTGGCCACTACCAAAACAAAAACTGGAGGCTTTACATTTATTAGCAAATGAACAGTTA GAAAAGGGACATATTGAGCCTTCATTCTCGCCTTGGAATTCTCCTGTGTTTGTAATTCAGAAGAAATCCAGCAAATGG CGTATGTTAACTGACTTAAGGGCTGTAAATGCCGTAATTCAACCCATGGGGCCTCTCCAACCTGGGTTGCCCTCTCCA GCCATGATCCCAAAAGATTGGCCTTTAATTATAATTGATCTAAAGGACTGCTTTTTTACCATCCCTCTGGCAGAGCAG GATTGTGAAAAATTTGCCTTTACTATACCAGCCATAAATAATAAAGAACCAGCCACCAGGTTTCAGTGGAAAGTGTTA CCTCAGGGAATGCTTAATAGTCCAACTCTTTGTCAGACTTTTGTAGGTCGAGCTCTTCAACCAGTTAGAGACAAGTTTT CAGACTGTTATATTATTCATTATTTTGATGATATTTTATGTGCTGCAGAAACGAAAGATAAATTAATTGACTGTTATAC ATTTCTGCAAGCAGAGGTTGCCAATGCAGGACTGGCAATAGCATCTGATAAGATCCAAACCTCTACTCCTTTTCATTA TTTAGGGATGCAGATAGAAAATAGAAAAATTAAGCCACAAAAAATAGAAATAAGAAAAGACACATTAAAAACACTA AATGATTTTCAAAAATTGCTGGGAGATATTAATTGGATTCGGCCAACTCTAGGCATTCCTACTTATGCCATGTCAAATT TGTTCTCTATCTTAAGAGGAGACTCAGACTTAAATAGTAAAAGAATGTTAACCCCAGAGGCAACAAAAGAAATTAAATTAGTGGAAGAAAAAATTCAGTCAGCGCAAATAAATAGAATAGATCCCTTAGCCCCACTCCAACTTTTGATTTTTGCCACTGCCCATTCTCCAACAGGCATCATTATTCAAAATACTGATCTTGTGGAGTGGTCATTCCTTCCTCACAGTACAGTTAAGACTTTTACATTGTACTTGGATCAAATAGCTACTTTAATTGGTCCGACAAGATTACGAATAATAAAATTATGTGGAA TTGGTCTTGCTAATTTTGTGGGAATTATTGATAATCATTACCCAAAAACAAAAATCTTCCAGTTCTTAAAATTGACTAC TTGGATTCTACCTAAAATTACCAGACGTGAACCTTTAGAAAATGCTCTAACAGTATTTACTGATGGTTCCAGCAATGGAAAAGTGGCTTACACAGGGCCAAAAGAACGAGTAATCAAAACTCCATATCAATCGGCTCAAAGAGCAGAGTTGGTTGCAGTCATTACAGTGTTACAAGATTTTGATCAACCTATCAATATTATATCGGATTCTGCATATGTAGTACAGGCTACAA GGGATGTTGAGACAGCTCTAATTAAATATAGCATGGACGATCAGTTAAACCAGCTATTCAATTTATTACAACAAACTG TAAGAAAAAGAAACTTCCCATTTTATATTACTCATATTCGAGCACACACTAATTTACCAGGGCCTTTGACTAAAGCAA ATGAACAAGCTGACTTACTGGTATCATCTGCATTCATAAAAGCACAAGAACTTCATGCTTTGACTCATGTAAATGCAG CAGGATTAAAAAACAAATTTGATGTCACATGGAAACAGGCAAAAGATATTGTACAACATTGCACCCAGTGTCAAGTC TTAGACCTGCCCACTCAAGAGGCAGGAGTTAACCCAGAGGTCTGTGTCCTAATGCATTATGGCAAATGGATGTCACAC ATGTACCTTCATTTGGGAAGATTATCATATGTTCATGTAACAGTTGATACTTATTCACATTTCATGTGTGCAACTTGCC AAACAGGAGAAAGTACTTCCCATGTTAAAAAACATTTATTGTCTTGTTTTGCTGTAATGGGAGTTCCAGAAAAAATCA AAACTGACAATGGACCAGGATATTGTAGTAAAGCTTTCCAAAAATTCTTAAGTCAGTGGAAAATTTCACATACAACA GGAATTCCTTATAATTCCCAAGGACAGGCCATAGTTGAAAGAACTAATAGAACACTCAAAACTCAATTAGTTAAACA AAAAGAAGGGGGAGACAGTAAGGAGTGTACCACTCCTCAGATGCAACTTAATCTAGCACTCTATACTTTAAATTTTTT AAACATTTATAGAAATCAGACTACTACTTCTGCAGAACATCTTACTGGTAAAAAGAACAGCCCACATGAAGGAAAAC TAATTTAGCGGAAAGATAATTAAAATAAGACATGGGAAATAGGGAAGCTGATAACGTGGGGGAGAGGTTTTGCTTGT GTTTCACCAGGAGAAAATCAGCTTCCTGTTTGGATACCCACTAGACATTTGAAGTTCTACAATGAACCCATCAGAGATGCAAAGAAAAGCGCCTCCACGGAGATGGTAACACCAGTCACATGGATGGATAATCCTATAGAAGTATATGTTAATGATAGTGTATGGGTACCTGGCCCCACAGATGATCGCTGCCCTGCCAAACCTGAGGAAGAAGGGATGATGATAAATATTT CCATTGGGTATCATTATCCTCCTATTTGCCTAGGGAGAGCACCAGGATGTTTAATGCCTGCAGTCCAAAATTGGTTGGT AGAAGTACCTACTGTCAGTCCTAACAGTAGATTCACTTATCACATGGTAAGCGGGATGTCACTCAGGCCACGGGTAAA TTGTTTACAAGACTTTTCTTATCAAAGATCATTAAAATTTAGACCTAAAGGGAAAACTTGCCCCAAGGAAATTCCTAA AGGATCAAAGAATACAGAAGTTTTAGTTTGGGAAGAATGTGTGGCCAATAGTGTGGTGATATTACAAAACAATGAAT TCGGAACTATTATAGATTGGGCACCTCGAGGTCAATTCTACCACAATTGCTCAGGACAAACTCAGTCGTGTCCAAGTG CACAAGTGAGTCCAGCTGTCGATAGCGACTTAACAGAAAGTCTAGACAAACATAAGCATAAAAAATTACAGTCTTTC TACCTTTGGGAATGGGAAGAAAAAGGAATCTCTACCCCAAGACCAAAAATAATAAGTCCTGTTTCTGGTCCTGAACAT CCAGAATTGTGGAGGCTTACTGTGGCCTCACACCACATTAGAATTTGGTCTGGAAATCAAACTTTAGAAACAAGATATCGTAAGCCATTTTATACTATCGACCTAAATTCCATTCTAACGGTTCCTTTACAAAGTTGCGTAAAGCCCCCTTATATGCTAGTTGTAGGAAATATAGTTATTAAACCAGCCTCCCAAACTATAACCTGTGAAAATTGTAGATTGTTTACTTGCATTG ATTCAACTTTTAATTGGCAGCACCGTATTCTGCTGGTGAGAGCAAGAGAAGGCATGTGGATCCCTGTGTCCACGGACC GACCGTGGGAGGCCTCGCCATCCATCCATATTTTGACTGAAATATTAAAAGGCGTTTTAAATAGATCCAAAAGATTCA TTTTTACTTTAATTGCAGTGATTATGGGATTAATTGCAGTCACAGCTACGGCTGCTGTGGCAGGAGTTGCATTGCACTC TTCTGTTCAGTCAGTAAACTTTGTTAATTATTGGCAAAAGAATTCTACAAGATTGTGGAATTCACAATCTAGTATTGAT CAAAAATTGGCAAGTCAAATTAATGATCTTAGACAAACTGTCATTTGGATGGGAGACAGGCTCATGACCTTAGAACA TCATTTCCAGTTACAGTGTGACTGGAATACGTCAGATTTTTGTATTACACCCCAAATTTATAATGAGTCTGAGCATCAC TGGGACATGGTTAGACGCCATCTACAGGGAAGAGAAGATAATCTCACTTTAGACATTTCCAAATTAAAAGAACAAAT TTTCGAAGCATCAAAAGCCCATTTAAATTTGGTGCCAGGAACTGAGGCAATTGCAGGAGTTGCTGATGGCCTCGCAAATCTTAACCCTGTCACTTGGATTAAGACCATCAGAAGTACTATGATTATAAATCTCATATTAATCGTTGTGTGCCTGTTTTGTCTGTTGTTAGTCTGCAGGTGTACCCAACAGCTCCGAAGAGACAGTGACATCGAGAACGGGCCATGATGACGATG GCGGTTTTGTCGAAAAGAAAAGGGGGAAATGTGGGGAAAAGCAAGAGAGATGAGATTGTTACTGTGTCTGTATAGAA AGAAGTAGACATAGGAGACTCCATTTTGTTCTGTACTAAGAAAAATTCTTCTGCCTTGAGATGCTGTTAATCTATGAC CTTACCCCCAACCCCGTGCTCTCTGAAACATGTGCTGTGTCAAACTCTGGGTTAAATGGATTAAGGGTGGTGCAAGAT GTGCTTTGTTAAACAGATGCTTGAAGGCAGCATGCTCATTAAGAGTCATCACCACTCCCTAATCTCAAGTACCCAGGG ACACAAACACTGCGAAAGGCCGCAGGGACCTCTGCCTAGGAAAGCCAGGTATTGTCCAAGGTTTCTCCCCATGTGAG AGTCTGAAATATGGCCTCGTGGGAAGGGAAAGACCTGACCATCCCCCAGACCGACACCCGTAAAGGGTCTGTGCTGA GGAGGATTAGTATAAGAGGAAAGCATGCCTCTTGCAGTTGAGAGAAGAGGAAGACATCTGTTTCCTGCCCATCCCTG GGCAATGGAATGTCTCAGTATAAAACCCGATTGAACATTCCATCTACTGAGATAGGGAAAAACTGCCTTAGGGCTGG AGGTGGGACATGTGGCTTTACCTTGTCTATGATGCAAACACCTTTGTTCACGTGTTTGTCTGCTGACCCTCTCCCCACT ATTGTCTTGTGACCCTGACACATCCCCCTCTCGGAGAAACACCCACGAATGATCAATAAATACTAAGGGAACTCAGAG GCTGGCGGGATCCTCCATATGCTGAACGCTGGTTCCCCGGGCCCCCTTATTTCTTTCTCTATACTTTGTCTCTGTGTCTTTTTCTTTTCCAAGTCTCTCATTCCACCTTATGAGAAACACCCACAGGTGTGGAGGGGCAACCCACCCCTTCA(SEQ ID NO: 4)An exemplary HERV-K Gag amino acid (GenBank AAL16779.1) is: QAGRKGNIIPLTVWNDWPIIKAALEPFQTEDSVSVSDAPGSCIIDCNEKTRKKSQKETETLHCEYVAE PLMAQSTQNVDYNQLQEVIYPETLKLEGKGPELVGPLESKPRGPSPLSAGQVTVTLQPQAQVRENK TQLPVAYQYWPPAELQYRPPPESQYGYLGMPPAPQDREPYPQPPTRRQCYGTT(SEQ ID NO: 6) An exemplary HERV-K Pol amino acid sequence (GenBank AAL60056.1) is: MIPKDWPLIIIDLKDCFFTIPLAEQDCEKFAFTIPAINNKEPATRFQWKVLPQGMLNSPTLCQTFVGR ALQPVRDKFSDCYIIHYFDDILCAAETKDKLIDCYTFLQAEVANAGLAIASDKIQTSTPFHYLGMQIE NRKIKPQKIEIRKDTLKTLNDFQKLLGDINWIRPTLGIPTYAMSNLFSILRGDSDLNSKRMLTPEATK EIKLVEEKIQSAQINRIDPLAPLQLLIFATAHSPTGIIIQNTDLVEWSFLPHSTVKTFTLYLDQIATLIGP TRLRIIKLCGNDPDKIVVPLTKEQVRQAFINSGAWQIGLANFVGIIDNHYPKTKIFQFLKLTTWILPKI TRREPLENALTVFTDGSSNGKVAYTGPKERVIKTPYQSAQRAELVAVITVLQDFDQPINIISDSAYVV QATRDVETALIKYSMDDQLNQLFNLLQQTVRKRNFPFYITHIRAHTNLPGPLTKANEQADLLVSSAF IKAQELHALTHVNAAGLKNKFDVTWKQAKDIVQHCTQCQVLDLPTQEAGVNPEVCVLMHYGKW MSHMYLHLGRLSYVHVTVDTYSHFMCATCQTGESTSHVKKHLLSCFAVMGVPEKIKTDNGPGYC SKAFQKFLSQWKISHTTGIPYNSQGQAIVERTNRTLKTQLVKQKEGGDSKECTTPQMQLNLALYTL NFLNIYRNQTTTSAEHLTGKKNSPHEGKLI (SEQ ID NO: 7) An exemplary HERV-K Env amino acid sequence (GenBank AAL16780.1) is: MVTPVTWMDNPIEVYVNDSVWVPGPTDDRCPAKPEEEGMMINISIGYHYPPICLGRAPGCLMPAV QNWLVEVPTVSPNSRFTYHMVSGMSLRPRVNCLQDFSYQRSLKFRPKGKTCPKEIPKGSKNTEVLV WEECVANSVVILQNNEFGTIIDWAPRGQFYHNCSGQTQSCPSAQVSPAVDSDLTESLDKHKHKKLQ SFYLWEWEEKGISTPRPKIISPVSGPEHPELWRLTVASHHIRIWSGNQTLETRYRKPFYTIDLNSILTV PLQSCVKPPYMLVVGNIVIKPASQTITCENCRLFTCIDSTFNWQHRILLVRAREGMWIPVSTDRPWE ASPSIHILTEILKGVLNRSKRFIFTLIAVIMGLIAVTATAAVAGVALHSSVQSVNFVNYWQKNSTRLW NSQSSIDQKLASQINDLRQTVIWMGDRLMTLEHHFQLQCDWNTSDFCITPQIYNESEHHWDMVRR HLQGREDNLTLDISKLKEQIFEASKAHLNLVPGTEAIAGVADGLANLNPVTWIKTIRSTMIINLILIVV CLFCLLLVCRCTQQLRRDSDIENGP(SEQ ID NO: 8) Antibodies that specifically bind Gag, Pol or Env of HERV-K are available, see U.S. Published Patent Application No.2008 / 0019979A1, which discloses antibodies that specifically bind an HERV-K protein. Additional antibodies that bind HERV-K envelope protein are disclosed, for example, in U.S. Patent No.10,723,787 and U.S. Patent No.10,981,976, both incorporated herein by reference. In some aspects, and antibody, or antigen binding fragment thereof, that specifically binds Gag, Pol or Env or HERV-K is used in the disclosed methods. In some aspect, an antibody or antigen binding fragment is delivered locally to the eye. In other aspects, an antibody or antigen binding fragment is delivered systemically to the subject. In further aspects, a nucleic acid molecule encoding an antibody or antigen binding fragment is delivered locally to the eye or systemically to the subject. Antibodies to HERV-K envelope protein are commercially available from MyBioSource, Catalog number MBS602670 and MBS603725, and from United States Biological, Catalog number E2286-13-100ug and E2286-14-100ug. Antibodies to HERV-K envelope protein are commercially available from LSBio, catalog number LS-C65286-100, and from antibodies-online, catalog number ABIN472658. Antibodies that specifically bind and substantially reduce or inhibit Gag, Pol or Env activity (such as a reduction of at least 20%, at least 40%, at least 50%, at least 75%, at least 80%, at least 90%, at least 95%,at least 98% or even 100%) are of use in the methods disclosed herein. Antibodies include monoclonal antibodies, human antibodies, humanized antibodies, and immunoglobulin (Ig) fusion proteins. Fully human and humanized antibodies can also be produced using methods known to those of skill in the art. Polyclonal antagonistic antibodies can be prepared, such as by immunizing a suitable subject (such as a human subject or a veterinary subject) with an HERV-K Gag, Pol or Env protein. The anti-HERV-K Gag, Pol or Env antibody titer in the immunized subject can be monitored over time, such as with an enzyme linked immunosorbent assay (ELISA) using immobilized HERV-K Gag, Pol or Env or an epitope thereof. In one example, the antibody molecules that specifically bind HERV-K Gag, Pol or Env can be isolated from a mammal (such as from serum) and further purified, for example using protein A chromatography to isolate IgG antibodies. In some aspects, the antibody can also be selected using a functional assay, such as to detect inhibition of HERV-K function. Antibody-producing cells can be obtained from a subject, such as an immunized subject, and used to prepare monoclonal antibodies (see Kohler and Milstein Nature 256:49549, 1995; Brown et al., J. Immunol. 127:53946, 1981; Cole et al., Monoclonal Antibodies and Cancer Therapy, Alan R. Liss, Inc., pp.7796, 1985; Gefter, M. L. et al. (1977) Somatic Cell Genet.3:23136; Kenneth, R. H. in Monoclonal Antibodies: A New Dimension In Biological Analyses. Plenum Publishing Corp., New York, N.Y. (1980); Kozbor et al. Immunol. Today 4:72, 1983; Lerner, E. A. (1981) Yale J. Biol. Med.54:387402; Yeh et al., Proc. Natl. Acad. Sci.76:292731, 1976). In one example, an immortal cell line (typically a myeloma) is fused to lymphocytes (typically splenocytes) from a mammal immunized with HERV-K Gag, Pol or Env, and the culture supernatants of the resulting hybridoma cells are screened to identify a hybridoma producing a monoclonal antibody that specifically binds to the polypeptide of interest and inhibits a function of the polypeptide. In one aspect, to produce a hybridoma, an immortal cell line (such as a myeloma cell line) is derived from the same mammalian species as the lymphocytes. For example, murine hybridomas can be made by fusing lymphocytes from a mouse immunized with HERV-K Gag, Pol or Env, or an epitope thereof, with an immortalized mouse cell line. In one example, a mouse myeloma cell line is utilized that is sensitive to culture medium containing hypoxanthine, aminopterin and thymidine ("HAT medium"). Any of a number of myeloma cell lines can be used as a fusion partner, including, for example, P3-NS1 / 1-Ag4-1, P3-x63- Ag8.653 or Sp2 / O-Ag14 myeloma lines, which are available from the American Type Culture Collection (ATCC), Rockville, MD. HAT-sensitive mouse myeloma cells can be fused to mouse splenocytes using polyethylene glycol ("PEG"). Hybridoma cells resulting from the fusion are then selected using HAT medium, which kills unfused (and unproductively fused) myeloma cells. Hybridoma cells producing a monoclonal antibody of interest can be detected, for example, by screening the hybridoma culture supernatants for the production antibodies that bind a HERV-K Gag, Pol or Env, such as by using an immunological assay (such as an enzyme-linked immunosorbant assay (ELISA) or radioimmunoassay(RIA). As an alternative to preparing secreting hybridomas, a monoclonal antibody that specifically binds HERV-K Gag, Pol or Env can be identified and isolated by screening a recombinant combinatorial immunoglobulin library (such as an antibody phage display library) with HERV-K Gag, Pol or Env, or an epitope thereof, to isolate immunoglobulin library members that specifically bind the polypeptide. Library members can be selected that have particular activities, such as binding to HERV-K Gag, Pol or Env, or inhibiting HERV-K in an in vitro assay. Kits for generating and screening phage display libraries are commercially available (such as, but not limited to, Pharmacia and Stratagene). Examples of methods and reagents particularly amenable for use in generating and screening antibody display library can be found in, for example, U.S. Pat. No.5,223,409; PCT Publication No. WO 90 / 02809; PCT Publication No. WO 91 / 17271; PCT Publication No. WO 92 / 18619; PCT Publication WO 92 / 20791; PCT Publication No. WO 92 / 15679; PCT Publication No. WO 92 / 01047; PCT Publication WO 93 / 01288; PCT Publication No. WO 92 / 09690; Barbas et al., Proc. Natl. Acad. Sci. USA 88:79787982, 1991; Hoogenboom et al., Nucleic Acids Res.19:41334137, 1991. In one example the sequence of the specificity determining regions of each CDR is determined. Residues outside the SDR (specificity determining region, e.g., the non-ligand contacting sites) are substituted. For example, in any of the CDR sequences, at most one, two or three amino acids can be substituted. Chimeric antibodies, which include a framework region from one antibody and the CDRs from a different antibody, can be produced. For example, humanized antibodies can be produced. The antibody or antibody fragment can be a humanized immunoglobulin having CDRs from a donor monoclonal antibody that binds HERV-K Gag, Pol or Env, or an epitope thereof, and immunoglobulin and heavy and light chain variable region frameworks from human acceptor immunoglobulin heavy and light chain frameworks. Humanized monoclonal antibodies can be produced by transferring CDRs from heavy and light variable chains of the donor mouse immunoglobulin (that specifically binds HERV-K Gag, Pol or Env) into a human variable domain, and then substituting human residues in the framework regions when required to retain affinity. The use of antibody components derived from humanized monoclonal antibodies obviates potential problems associated with the immunogenicity of the constant regions of the donor antibody. Techniques for producing humanized monoclonal antibodies are described, for example, by Jones et al., Nature 321:522, 1986; Riechmann et al., Nature 332:323, 1988; Verhoeyen et al., Science 239:1534, 1988; Carter et al., Proc. Natl. Acad. Sci. U.S.A.89:4285, 1992; Sandhu, Crit. Rev. Biotech.12:437, 1992; and Singer et al., J. Immunol.150:2844, 1993. The antibody may be of any isotype, but in several aspects the antibody is an IgG, including but not limited to, IgG1, IgG2, IgG3 and IgG4. In one aspect, the sequence of the humanized immunoglobulin heavy chain variable region framework can be at least about 65% identical to the sequence of the donor immunoglobulin heavy chain variable region framework. Thus, the sequence of the humanized immunoglobulin heavy chain variable region framework can be at least about 75%, at least about 85%, at least about 99% or at least about 95%, identical to the sequence of the donor immunoglobulin heavy chain variable region framework. Humanframework regions, and mutations that can be made in humanized antibody framework regions (see, for example, in U.S. Patent No.5,585,089). Exemplary human antibodies are LEN and 21 / 28 CL. The sequences of the many human heavy and light chain frameworks are known. Generally, an antibody, such as a human or humanized antibody specifically binds to HERV-K Gag, Pol or Env, and / or an epitope thereof, with an affinity constant of at least 107M-1, such as at least 108M-1at least 5 X 108M-1or at least 109M-1. In several examples, the antibody specifically binds HERV-K Gag, Pol or Env , or an epitope thereof, with an affinity constant of at least 108M-1at least 5 X 108M-1or at least 109M-1. The antibody can be a fully human antibody. Antibodies, such as murine monoclonal antibodies, chimeric antibodies, and humanized antibodies, include full length molecules as well as fragments thereof, such as Fab, F(ab')2, and Fv which include a heavy chain and light chain variable region and are capable of binding specific epitope determinants. These antibody fragments retain some ability to selectively bind with their antigen or receptor. These fragments include: (1) Fab, the fragment which contains a monovalent antigen-binding fragment of an antibody molecule, can be produced by digestion of whole antibody with the enzyme papain to yield an intact light chain and a portion of one heavy chain; (2) Fab', the fragment of an antibody molecule can be obtained by treating whole antibody with pepsin, followed by reduction, to yield an intact light chain and a portion of the heavy chain; two Fab' fragments are obtained per antibody molecule; (3) (Fab')2, the fragment of the antibody that can be obtained by treating whole antibody with the enzyme pepsin without subsequent reduction; F(ab')2 is a dimer of two Fab' fragments held together by two disulfide bonds; (4) Fv, a genetically engineered fragment containing the variable region of the light chain and the variable region of the heavy chain expressed as two chains; and (5) Single chain antibody (such as scFv), defined as a genetically engineered molecule containing the variable region of the light chain, the variable region of the heavy chain, linked by a suitable polypeptide linker as a genetically fused single chain molecule. Methods of making these fragments are disclosed, for example, Harlow and Lane, Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory, New York, 1988. In several examples, the variable region includes the variable region of the light chain and the variable region of the heavy chain expressed as individual polypeptides. Fv antibodies are typically about 25 kDa and contain a complete antigen-binding site with three CDRs per each heavy chain and each light chain. To produce these antibodies, the VH and the VL can be expressed from two individual nucleic acid constructs in a host cell. If the VH and the VL are expressed non-contiguously, the chains of the Fv antibody are typically held together by noncovalent interactions. However, these chains tend to dissociate upon dilution, so methods have been developed to crosslink the chains through glutaraldehyde, intermolecular disulfides, or a peptide linker. Thus, in one example, the Fv can be a disulfide stabilized Fv (dsFv), wherein the heavy chain variable region and thelight chain variable region are chemically linked disulfide bonds. In an additional example, the Fv VHand VLchains connected by a peptide linker. These single-chain antigen binding proteins (scFv) are prepared by constructing a structural gene comprising DNA sequences encoding the VH and VL domains connected by an oligonucleotide. The structural gene is inserted into an expression vector, which is subsequently introduced into a host cell such as E. coli. The recombinant host cells synthesize a single polypeptide chain with a linker peptide bridging the two V domains. Methods for producing scFvs can be found, for example in Whitlow et al., Methods: a Companion to Methods in Enzymology, Vol.2, page 97, 1991; Bird et al., Science 242:423, 1988; U.S. Patent No.4,946,778; Pack et al., Bio / Technology 11:1271, 1993; and Sandhu, supra. Antibody fragments can be prepared by proteolytic hydrolysis of the antibody or by expression in E. coli of DNA encoding the fragment. Antibody fragments can be obtained by pepsin or papain digestion of whole antibodies by conventional methods. For example, antibody fragments can be produced by enzymatic cleavage of antibodies with pepsin to provide a 5S fragment denoted F(ab')2. This fragment can be further cleaved using a thiol reducing agent, and optionally a blocking group for the sulfhydryl groups resulting from cleavage of disulfide linkages, to produce 3.5S Fab' monovalent fragments. Alternatively, an enzymatic cleavage using pepsin produces two monovalent Fab' fragments and an Fc fragment directly (see U.S. Patent No.4,036,945 and U.S. Patent No.4,331,647, and references contained therein; Nisonhoff et al., Arch. Biochem. Biophys.89:230, 1960; Porter, Biochem. J.73:119, 1959; Edelman et al., Methods in Enzymology, Vol.1, page 422, Academic Press, 1967; and Coligan et al. at sections 2.8.1-2.8.10 and 2.10.1- 2.10.4). Other methods of cleaving antibodies, such as separation of heavy chains to form monovalent light- heavy chain fragments, further cleavage of fragments, or other enzymatic, chemical, or genetic techniques may also be used, so long as the fragments bind to the antigen that is recognized by the intact antibody. Any of the antigen binding fragments described herein are of use. Conservative variants of the antibodies can be produced. Such conservative variants employed in antibody fragments, such as dsFv fragments or in scFv fragments, will retain critical amino acid residues necessary for correct folding and stabilizing between the VH and the VL regions, and will retain the charge characteristics of the residues to preserve the low pI and low toxicity of the molecules. Amino acid substitutions (such as at most one, at most two, at most three, at most four, or at most five amino acid substitutions) can be made in the VHand the VLregions to increase yield. In some aspects, these substitutions are made in the framework regions, and are not made in the CDRs. A table of conservative amino acid substitutions is provided above. The amino acid sequence of an antibody of interest can be reviewed to locate one or more of the amino acids in a HERV-K Gag, Pol or Env sequence, identify a conservative substitution, and produce the conservative variant using molecular techniques. Effector molecules, such as detectable or therapeutic moieties can be linked to an antibody that specifically binds HERV-K Gag, Pol or Env, using any number of means. Both covalent and noncovalent attachment means may be used. The procedure for attaching an effector molecule to an antibody variesaccording to the chemical structure of the effector. typically contain a variety of functional groups; such as carboxylic acid (COOH), free NH2) or sulfhydryl (-SH) groups, which are available for reaction with a suitable functional group on an antibody to result in the binding of the effector molecule. Alternatively, the antibody is derivatized to expose or attach additional reactive functional groups. The derivatization may involve attachment of any number of linker molecules, such as those available from Pierce Chemical Company, Rockford, IL. The linker can be any molecule used to join the antibody to the effector molecule. The linker is capable of forming covalent bonds to both the antibody and to the effector molecule. Suitable linkers include, but are not limited to, straight or branched-chain carbon linkers, heterocyclic carbon linkers, or peptide linkers. Where the antibody and the effector molecule are polypeptides, the linkers may be joined to the constituent amino acids through their side groups (such as through a disulfide linkage to cysteine) or to the alpha carbon amino and carboxyl groups of the terminal amino acids. Nucleic acid sequences encoding the antibodies can be prepared, for example, cloning of appropriate sequences or by direct chemical synthesis by methods such as the phosphotriester method of Narang et al., Meth. Enzymol.68:90-99, 1979; the phosphodiester method of Brown et al., Meth. Enzymol.68:109-151, 1979; the diethylphosphoramidite method of Beaucage et al., Tetra. Lett.22:1859-1862, 1981; the solid phase phosphoramidite triester method described by Beaucage & Caruthers, Tetra. Letts.22(20):1859-1862, 1981, for example, using an automated synthesizer as described in, for example, Needham-VanDevanter et al., Nucl. Acids Res.12:6159-6168, 1984; and the solid support method of U.S. Patent No.4,458,066. Chemical synthesis produces a single stranded oligonucleotide. This can be converted into double stranded DNA by hybridization with a complementary sequence, or by polymerization with a DNA polymerase using the single strand as a template. Longer sequences may be obtained by the ligation of shorter sequences generated by chemical synthesis. Exemplary nucleic acids encoding sequences encoding an antibody that specifically binds HERV-K Gag, Pol or Env be prepared by cloning techniques. Examples of appropriate cloning and sequencing techniques, and instructions sufficient to direct persons of skill through many cloning exercises are found in Sambrook et al., supra, Berger and Kimmel (eds.), supra, and Ausubel, supra. Product information from manufacturers of biological reagents and experimental equipment also provide useful information. Such manufacturers include the SIGMA Chemical Company (Saint Louis, MO), R&D Systems (Minneapolis, MN), Pharmacia Amersham (Piscataway, NJ), CLONTECH Laboratories, Inc. (Palo Alto, CA), Chem Genes Corp., Aldrich Chemical Company (Milwaukee, WI), Glen Research, Inc., GIBCO BRL Life Technologies, Inc. (Gaithersburg, MD), Fluka Chemica-Biochemika Analytika (Fluka Chemie AG, Buchs, Switzerland), Invitrogen (San Diego, CA), and Applied Biosystems (Foster City, CA), as well as other commercial sources. Nucleic acids can also be prepared by amplification methods. Amplification methods include polymerase chain reaction (PCR), the ligase chain reaction (LCR), the transcription-based amplificationsystem (TAS), the self-sustained sequence (3SR). A wide variety of cloning methods, host cells, and in vitro amplification are known. In one example, an antibody of use is prepared by inserting the cDNA, which encodes a variable region from an antibody that specifically binds HERV-K Gag, Pol or Env, into a vector which comprises the cDNA encoding an effector molecule (EM). The insertion is made so that the variable region and the EM are read in frame so that one continuous polypeptide is produced. Thus, the encoded polypeptide contains a functional Fv region and a functional EM region. In one aspect, cDNA encoding a detectable marker (such as an enzyme) is ligated to a scFv so that the marker is located at the carboxyl terminus of the scFv. In another example, a detectable marker is located at the amino terminus of the scFv. In a further example, cDNA encoding a detectable marker is ligated to a heavy chain variable region of an antibody that specifically binds HERV-K Gag, Pol or Env, so that the marker is located at the carboxyl terminus of the heavy chain variable region. The heavy chain-variable region can subsequently be ligated to a light chain variable region of the antibody that specifically binds HERV-K Gag, Pol or Env using disulfide bonds. In a yet another example, cDNA encoding a marker is ligated to a light chain variable region of an antibody that binds HERV-K Gag, Pol or Env, so that the marker is located at the carboxyl terminus of the light chain variable region. The light chain-variable region can subsequently be ligated to a heavy chain variable region of the antibody that specifically binds HERV-K Gag, Pol or Env using disulfide bonds. Once the nucleic acids encoding the antibody or functional fragment thereof are isolated and cloned, the protein can be expressed in a recombinantly engineered cell such as bacteria, plant, yeast, insect and mammalian cells. One or more DNA sequences encoding the antibody or functional fragment thereof can be expressed in vitro by DNA transfer into a suitable host cell. The cell may be prokaryotic or eukaryotic. The term also includes any progeny of the subject host cell. It is understood that all progeny may not be identical to the parental cell since there may be mutations that occur during replication. Polynucleotide sequences encoding the antibody or functional fragment thereof (such as an scFV) can be operatively linked to expression control sequences. An expression control sequence operatively linked to a coding sequence is ligated such that expression of the coding sequence is achieved under conditions compatible with the expression control sequences. The expression control sequences include, but are not limited to appropriate promoters, enhancers, transcription terminators, a start codon (i.e., ATG) in front of a protein-encoding gene, splicing signal for introns, maintenance of the correct reading frame of that gene to permit proper translation of mRNA, and stop codons. RNA encoding the disclosed antibodies are also of use. The polynucleotide sequences encoding the antibody or functional fragment thereof can be inserted into an expression vector including, but not limited to a plasmid, virus or other vehicle that can be manipulated to allow insertion or incorporation of sequences and can be expressed in either prokaryotes or eukaryotes. Hosts can include microbial, yeast, insect and mammalian organisms. Methods of expressing DNA sequences having eukaryotic or viral sequences in prokaryotes can be used. Biologically functional viral and plasmid DNA vectors capable of expression and replication in a host can be used.Transformation of a host cell with recombinant DNA may be carried out. Where the host is prokaryotic, such as E. coli, competent cells are capable of DNA uptake can be prepared from cells harvested after exponential growth phase and subsequently treated by the CaCl2 method. Alternatively, MgCl2 can be used. Transformation can also be performed after forming a protoplast of the host cell if desired, or by electroporation. When the host is a eukaryote, such methods of transfection of DNA as calcium phosphate coprecipitates, mechanical procedures such as microinjection, electroporation, insertion of a plasmid encased in liposomes, or virus vectors, may be used. Eukaryotic cells can also be co-transformed with polynucleotide sequences encoding the antibody of functional fragment thereof and a second foreign DNA molecule encoding a selectable phenotype, such as the herpes simplex thymidine kinase gene. Another method is to use a eukaryotic viral vector, such as simian virus 40 (SV40) or bovine papilloma virus, to transiently infect or transform eukaryotic cells and express the protein (see for example, Eukaryotic Viral Vectors, Cold Spring Harbor Laboratory, Gluzman ed., 1982). Expression systems, such as plasmids and vectors, can be used to produce proteins in cells including higher eukaryotic cells such as the COS, CHO, HeLa and myeloma cell lines. Isolation and purification of a recombinantly expressed polypeptide can be performed, for example using preparative chromatography and immunological separations. Once expressed, the recombinant antibodies can be purified, or example using ammonium sulfate precipitation, affinity columns, column chromatography, and the like (see, generally, R. Scopes, Protein Purification, Springer-Verlag, N.Y., 1982). Substantially pure compositions of at least about 90 to 95% homogeneity are disclosed herein, and 98 to 99% or more homogeneity can be used for pharmaceutical purposes. Once purified, partially or to homogeneity as desired, if to be used therapeutically, the polypeptides should be substantially free of endotoxin. Methods for expression of single chain antibodies and / or refolding to an appropriate active form, including single chain antibodies, from bacteria such as E. coli have are applicable to the antibodies disclosed herein. See, Buchner et al., Anal. Biochem.205:263-270, 1992; Pluckthun, Biotechnology 9:545, 1991; Huse et al., Science 246:1275, 1989 and Ward et al., Nature 341:544, 1989. Often, functional heterologous proteins from E. coli or other bacteria are isolated from inclusion bodies and require solubilization using strong denaturants, and subsequent refolding. During the solubilization step, a reducing agent must be present to separate disulfide bonds. An exemplary buffer with a reducing agent is: 0.1 M Tris pH 8, 6 M guanidine, 2 mM EDTA, 0.3 M DTE (dithioerythritol). Reoxidation of the disulfide bonds can occur in the presence of low molecular weight thiol reagents in reduced and oxidized form, as described in Saxena et al., Biochemistry 9: 5015-5021, 1970, Buchner et al., supra. Renaturation is typically accomplished by dilution (for example, 100-fold) of the denatured and reduced protein into refolding buffer. An exemplary buffer is 0.1 M Tris, pH 8.0, 0.5 M L-arginine, 8 mMoxidized glutathione (GSSG), and 2 mM EDTA. As a modification to the two chain protocol, the heavy and light chain regions are separately solubilized and reduced and then combined in the refolding solution. An exemplary yield is obtained when these two proteins are mixed in a molar ratio such that a 5 fold molar excess of one protein over the other is not exceeded. It is desirable to add excess oxidized glutathione or other oxidizing low molecular weight compounds to the refolding solution after the redox-shuffling is completed. In addition to recombinant methods, the antibodies and functional fragments thereof that are disclosed herein can also be constructed in whole or in part using standard peptide synthesis. Solid phase synthesis of the polypeptides of less than about 50 amino acids in length can be accomplished by attaching the C-terminal amino acid of the sequence to an insoluble support followed by sequential addition of the remaining amino acids in the sequence. Techniques for solid phase synthesis are described by Barany & Merrifield, The Peptides: Analysis, Synthesis, Biology. Vol.2: Special Methods in Peptide Synthesis, Part A. pp. 3-284; Merrifield et al., J. Am. Chem. Soc.85:2149-2156, 1963, and Stewart et al., Solid Phase Peptide Synthesis, 2nd ed., Pierce Chem. Co., Rockford, Ill., 1984. Proteins of greater length may be synthesized by condensation of the amino and carboxyl termini of shorter fragments. Methods of forming peptide bonds by activation of a carboxyl terminal end (such as by the use of the coupling reagent N, N'- dicycylohexylcarbodimide) can be used. Pharmaceutical compositions for delivery of nucleic acid molecules encoding antibodies are disclosed below. B. Inhibitory Nucleic Acid Molecules An agent that inhibits HERV-K can be an inhibitory nucleic acid molecule. Inhibitory nucleic acids that decrease the expression and / or activity of HERV-K Gag, Pol or Env can also be used in the methods disclosed herein. In some examples, such inhibitor nucleic acid molecules decrease HERV-K Gag, Pol or Env expression or activity by at least 20%, at least 40%, at least 50%, at least 75%, at least 80%, at least 90%, at least 95%, at least 98% or even 100%. One aspect is an RNA interference (RNAi), such as, but not limited to, small inhibitory RNA (siRNA) or short hairpin RNA, which can be used for interference or inhibition of expression of a target. RNAs that specifically target HERV-K Gag, Pol or Env are commercially available, for example from Santa Cruz Biotechnology, Inc., ThermoFisher Scientific, and Sigma Aldrich. PCT Publication No. WO2017 / 059122 discloses the use of a polynucleotide sequence in the LTR of the HERV-K genome, wherein the polynucleotide sequence contains eight or more contiguous pyrimidine bases, to reduce HERV-K transcription There are ten (SEQ ID NOs: 1-10 of PCT Publication No. WO2017 / 059122) inhibitory mRNAs that are disclosed to be of use. Exemplary commercially available RNAi sequences specific for HERV-K Gag, Pol or Env that can be used with the disclosed methods include those that target any part of the HERV-K open reading frame. Generally, siRNAs are generated by the cleavage of relatively long double-stranded RNA molecules by Dicer or DCL enzymes (Zamore, Science, 296:1265-1269, 2002; Bernstein et al., Nature, 409:363-366, 2001). In animals and plants, siRNAs are assembled into RISC and guide the sequence specificribonucleolytic activity of RISC, thereby resulting in the cleavage of mRNAs or other RNA target molecules in the cytoplasm. In the nucleus, siRNAs also associated histone and DNA methylation, resulting in transcriptional silencing of individual genes or large chromatin domains. The present disclosure provides RNA suitable for interference or inhibition of expression of HERV- K Gag, Pol or Env. The RNA can also be used to inhibit the LTR, promoter, or enhancer of HERV-K. Other moieties that affect biding of transcription factor to the LTRs are also of use. In some aspect, inhibitory RNA includes double stranded RNA of about 19 to about 40 nucleotides with the sequence that is substantially identical to a portion of an mRNA or transcript of a target gene, such as HERV-K Gag, Pol or Env, or any regulatory sequence, such as the LTR, for which interference or inhibition of expression is desired. For purposes of this disclosure, a sequence of the RNA “substantially identical” to a specific portion of the mRNA or transcript of the target gene for which interference or inhibition of expression is desired differs by no more than about 30%, and in some aspects no more than about 10% or no more than 5% from the specific portion of the mRNA or transcript of the target gene. In particular aspects, the sequence of the RNA is exactly identical to a specific portion of the mRNA or transcript of the target gene (e.g., HERV-K Gag, Pol or Env transcripts. Target sequences are provided in FIG.15A-15B. Thus, siRNAs disclosed herein include double-stranded RNA of about 15 to about 40 nucleotides in length and a 3’ or 5’ overhang having a length of 0 to 5-nucleotides on each strand, wherein the sequence of the double stranded RNA is substantially identical to (see above) a portion of a mRNA or transcript of a nucleic acid encoding HERV-K Gag, Pol or Env. In particular examples, the double stranded RNA contains about 19 to about 25 nucleotides, for instance 20, 21, or 22 nucleotides substantially identical to a nucleic acid encoding HERV-K Gag, Pol or Env. In additional examples, the double stranded RNA contains about 19 to about 25 nucleotides 100% identical to a nucleic acid encoding HERV-K Gag, Pol or Env. It should be noted that in this context “about” refers to integer amounts only. In one example, “about” 20 nucleotides refers to a nucleotide of 19 to 21 nucleotides in length. Regarding the overhang on the double-stranded RNA, the length of the overhang is independent between the two strands, in that the length of one overhang is not dependent on the length of the overhang on other strand. In specific examples, the length of the 3’ or 5’ overhang is 0-nucleotide on at least one strand, and in some cases it is 0-nucleotide on both strands (thus, a blunt dsRNA). In other examples, the length of the 3’ or 5’ overhang is 1-nucleotide to 5-nucleotides on at least one strand. More particularly, in some examples the length of the 3’ or 5’ overhang is 2-nucleotides on at least one strand, or 2-nucleotides on both strands. In particular examples, the dsRNA molecule has 3’ overhangs of 2-nucleotides on both strands. Thus, in one particular aspect, the double-stranded RNA contains 20, 21, or 22 nucleotides, and the length of the 3’ overhang is 2-nucleotides on both strands. In aspects of the RNAs provided herein, the double-stranded RNA contains about 40-60% adenine+uracil (AU) and about 60-40% guanine+cytosine (GC). More particularly, in specific examples the double-stranded RNA contains about 50% AU and about50% GC. Also disclosed herein are RNAs that at least one modified ribonucleotide, for instance in the sense strand of the double-stranded RNA. In particular examples, the modified ribonucleotide is in the 3’ overhang of at least one strand, or more particularly in the 3’ overhang of the sense strand. It is contemplated that examples of modified ribonucleotides include ribonucleotides that include a detectable label (for instance, a fluorophore, such as rhodamine or FITC), a thiophosphate nucleotide analog, a deoxynucleotide (considered modified because the base molecule is ribonucleic acid), a 2’-fluorouracil, a 2’-aminouracil, a 2’-aminocytidine, a 4-thiouracil, a 5-bromouracil, a 5-iodouracil, a 5-(3- aminoallyl)-uracil, an inosine, or a 2’O-Me-nucleotide analog. Nucleotide analogs may also include modifications to the sugar portion of the nucleotides. For example, the 2' OH-group may be replaced by H, OR, R, F, Cl, Br, I, SH, SR, NH2, NHR, NR2, or COOR, wherein R is substituted or unsubstituted C.sub.l-C.sub.6 alkyl, alkenyl, alkynyl, aryl, etc. Other possible modifications include those described in U.S. Pat. Nos.5,858,988, and 6,291,438. A locked nucleic acid (LNA), often referred to as inaccessible RNA, is a modified RNA nucleotide. The ribose moiety of an LNA nucleotide is modified with an extra bridge connecting the 2' oxygen and 4' carbon. Antisense and ribozyme molecules for HERV-K Gag, Pol or Env are of use in the methods disclosed herein. Antisense nucleic acids are DNA or RNA molecules that are complementary to at least a portion of a specific mRNA molecule (Weintraub, Scientific American 262:40, 1990). In the cell, the antisense nucleic acids hybridize to the corresponding mRNA, forming a double-stranded molecule. The antisense nucleic acids interfere with the translation of the mRNA, since the cell will not translate an mRNA that is double- stranded. Antisense oligomers of about 15 nucleotides can be used, since they are easily synthesized and are less likely to cause problems than larger molecules when introduced into the target cell producing HERV-K Gag, Pol or Env (see, for example, Marcus-Sakura, Anal. Biochem.172:289, 1988). An antisense oligonucleotide can be, for example, about 5, 10, 15, 20, 25, 30, 35, 40, 45 or 50 nucleotides in length. An antisense nucleic acid can be constructed using chemical synthesis and enzymatic ligation reactions. For example, an antisense nucleic acid molecule can be chemically synthesized using naturally occurring nucleotides or variously modified nucleotides designed to increase the biological stability of the molecules or to increase the physical stability of the duplex formed between the antisense and sense nucleic acids, such as phosphorothioate derivatives and acridine substituted nucleotides can be used. Examples of modified nucleotides which can be used to generate the antisense nucleic acid include 5- fluorouracil, 5-bromouracil, 5-chlorouracil, 5-iodouracil, hypoxanthine, xantine, 4-acetylcytosine, 5- (carboxyhydroxylmethyl) uracil, 5-carboxymethylaminomethyl-2-thiouridin- e, 5- carboxymethylaminomethyluracil, dihydrouracil, beta-D-galactosylqueosine, inosine, amongst others. Use of an oligonucleotide to stall transcription is a triplex strategy where an oligonucleotide winds around double-helical DNA, forming a three-strand helix. Therefore, these triplex compounds can be designed to recognize a unique site on a chosen gene (Maher, et al., Antisense Res. and Dev.1(3):227, 1991; Helene, C., Anticancer Drug Design 6(6):569), 1991. This type of inhibitory oligonucleotide is also of usein the methods disclosed herein. Ribozymes, which are RNA molecules the ability to specifically cleave other single- stranded RNA in a manner analogous to DNA restriction endonucleases, are also of use. Through the modification of nucleotide sequences, which encode these RNAs, it is possible to engineer molecules that recognize specific nucleotide sequences in an RNA molecule and cleave it (Cech, J. Amer. Med. Assn. 260:3030, 1988). Because they are sequence-specific, only mRNAs with particular sequences are inactivated. There are two basic types of ribozymes namely, tetrahymena-type (Hasselhoff, Nature 334:585, 1988) and “hammerhead”-type. Tetrahymena-type ribozymes recognize sequences which are four bases in length, while “hammerhead”-type ribozymes recognize base sequences 11-18 bases in length. The longer the recognition sequence, the greater the likelihood that the sequence will occur exclusively in the target mRNA species. Consequently, hammerhead-type ribozymes are preferable to tetrahymena-type ribozymes for inactivating a specific mRNA species and 18-base recognition sequences are preferable to shorter recognition sequences. Various delivery systems can be used to administer the siRNAs and other inhibitory nucleic acid molecules as therapeutics. Such systems include, for example, encapsulation in liposomes, microparticles, microcapsules, nanoparticles, recombinant cells capable of expressing the therapeutic molecule(s) (see, e.g., Wu et al., J. Biol. Chem.262, 4429, 1987), construction of a therapeutic nucleic acid as part of a retroviral or other vector, and the like. Delivery of nucleic acid molecules is discussed below. C. CRISPR / Cas13 As disclosed in PCT Publication No. WO 2019 / 040664, incorporated herein by reference, Cas13 proteins (and coding sequences), and guide molecules (e.g., gRNA and coding sequences) can be used in a CRISPR / Cas system to target one or more RNA molecules, such as HERV-K. A CRISPR / Cas system for RNA targeting includes two general components: (1) a Cas13 protein or its coding sequence (whose expression can be driven by a promoter) and (2) a guide nucleic acid molecule, such as RNA (gRNA), which is specific for the target RNA (whose expression can also be driven by promoter). When introduced into cells for example (1) as Cas13 mRNA and gRNA, (2) as part of a single vector or plasmid or divided into multiple vectors or plasmids, (3) as separate Cas13 protein and guide molecules, or (4) as an RNP complex of the Cas13 protein and guide molecule, the guide molecule guides the Cas13 to the target RNA (such as HERV-K). In some aspects the Cas13 is Cas13a, Cas13b, Cas13c, Cas13Rx, Cas13x, or Cas13y. In a particular non-limiting example, the Cas13 is Cas13Rx. Exemplary Cas13 sequences are found in PCT Publication No. WO 2019 / 040664, US 11,293,011, and US 10,392,616, and are also provided below. In some examples, administration of a CRISPR / Cas system for HERV-K RNA targeting is into the eye. In some aspects, the Cas 13 is Cas13Rx. An exemplary nucleic acid sequence encoding Cas13Rx is: ATGAGCCCCAAGAAGAAGAGAAAGGTGGAGGCCAGCATCGAAAAAAAAAAGTCCTTCGCCAAGGGCATGGGCGTGA AGTCCACACTCGTGTCCGGCTCCAAAGTGTACATGACAACCTTCGCCGAAGGCAGCGACGCCAGGCTGGAAAAGATC GTGGAGGGCGACAGCATCAGGAGCGTGAATGAGGGCGAGGCCTTCAGCGCTGAAATGGCCGATAAAAACGCCGGCTATAAGATCGGCAACGCCAAATTCAGCCATCCTAAGGGCTACGCCGTGGTGGCTAACAACCCTCTGTATACAGGACCC TATTTGTATCCAGGTGATCCATAACATCCTGGACATTGAAAAAATCCTCGCCGAATACATTACCAACGCCGCCTACGC CGTCAACAATATCTCCGGCCTGGATAAGGACATTATTGGATTCGGCAAGTTCTCCACAGTGTATACCTACGACGAATTCAAAGACCCCGAGCACCATAGGGCCGCTTTCAACAATAACGATAAGCTCATCAACGCCATCAAGGCCCAGTATGACGAGTTCGACAACTTCCTCGATAACCCCAGACTCGGCTATTTCGGCCAGGCCTTTTTCAGCAAGGAGGGCAGAAATTACA TCATCAATTACGGCAACGAATGCTATGACATTCTGGCCCTCCTGAGCGGACTGGCGCACTGGGTGGTCGCTAACAACG AAGAAGAGTCCAGGATCTCCAGGACCTGGCTCTACAACCTCGATAAGAACCTCGACAACGAATACATCTCCACCCTC AACTACCTCTACGACAGGATCACCAATGAGCTGACCAACTCCTTCTCCAAGAACTCCGCCGCCAACGTGAACTATATT GCCGAAACTCTGGGAATCAACCCTGCCGAATTCGCCGAACAATATTTCAGATTCAGCATTATGAAAGAGCAGAAAAA CCTCGGATTCAATATCACCAAGCTCAGGGAAGTGATGCTGGACAGGAAGGATATGTCCGAGATCAGGAAAAATCATA AGGTGTTCGACTCCATCAGGACCAAGGTCTACACCATGATGGACTTTGTGATTTATAGGTATTACATCGAAGAGGATG CCAAGGTGGCTGCCGCCAATAAGTCCCTCCCCGATAATGAGAAGTCCCTGAGCGAGAAGGATATCTTTGTGATTAACC TGAGGGGCTCCTTCAACGACGACCAGAAGGATGCCCTCTACTACGATGAAGCTAATAGAATTTGGAGAAAGCTCGAA AATATCATGCACAACATCAAGGAATTTAGGGGAAACAAGACAAGAGAGTATAAGAAGAAGGACGCCCCTAGACTGC CCAGAATCCTGCCCGCTGGCCGTGATGTTTCCGCCTTCAGCAAACTCATGTATGCCCTGACCATGTTCCTGGATGGCA AGGAGATCAACGACCTCCTGACCACCCTGATTAATAAATTCGATAACATCCAGAGCTTCCTGAAGGTGATGCCTCTCA TCGGAGTCAACGCTAAGTTCGTGGAGGAATACGCCTTTTTCAAAGACTCCGCCAAGATCGCCGATGAGCTGAGGCTG ATCAAGTCCTTCGCTAGAATGGGAGAACCTATTGCCGATGCCAGGAGGGCCATGTATATCGACGCCATCCGTATTTTAGGAACCAACCTGTCCTATGATGAGCTCAAGGCCCTCGCCGACACCTTTTCCCTGGACGAGAACGGAAACAAGCTCAAGAAAGGCAAGCACGGCATGAGAAATTTCATTATTAATAACGTGATCAGCAATAAAAGGTTCCACTACCTGATCAGAT ACGGTGATCCTGCCCACCTCCATGAGATCGCCAAAAACGAGGCCGTGGTGAAGTTCGTGCTCGGCAGGATCGCTGAC ATCCAGAAAAAACAGGGCCAGAACGGCAAGAACCAGATCGACAGGTACTACGAAACTTGTATCGGAAAGGATAAGG GCAAGAGCGTGAGCGAAAAGGTGGACGCTCTCACAAAGATCATCACCGGAATGAACTACGACCAATTCGACAAGAA AAGGAGCGTCATTGAGGACACCGGCAGGGAAAACGCCGAGAGGGAGAAGTTTAAAAAGATCATCAGCCTGTACCTC ACCGTGATCTACCACATCCTCAAGAATATTGTCAATATCAACGCCAGGTACGTCATCGGATTCCATTGCGTCGAGCGT GATGCTCAACTGTACAAGGAGAAAGGCTACGACATCAATCTCAAGAAACTGGAAGAGAAGGGATTCAGCTCCGTCAC CAAGCTCTGCGCTGGCATTGATGAAACTGCCCCCGATAAGAGAAAGGACGTGGAAAAGGAGATGGCTGAAAGAGCC AAGGAGAGCATTGACAGCCTCGAGAGCGCCAACCCCAAGCTGTATGCCAATTACATCAAATACAGCGACGAGAAGAAAGCCGAGGAGTTCACCAGGCAGATTAACAGGGAGAAGGCCAAAACCGCCCTGAACGCCTACCTGAGGAACACCAAGTGGAATGTGATCATCAGGGAGGACCTCCTGAGAATTGACAACAAGACATGTACCCTGTTCGCAAACAAGGCCGTCG CCCTGGAAGTGGCCAGGTATGTCCACGCCTATATCAACGACATTGCCGAGGTCAATTCCTACTTCCAACTGTACCATT ACATCATGCAGAGAATTATCATGAATGAGAGGTACGAGAAAAGCAGCGGAAAGGTGTCCGAGTACTTCGACGCTGTG AATGACGAGAAGAAGTACAACGATAGGCTCCTGAAACTGCTGTGTGTGCCTTTCGGCTACTGTATCCCCAGGTTTAAG AACCTGAGCATCGAGGCCCTGTTCGATAGGAACGAGGCCGCCAAGTTCGACAAGGAGAAAAAGAAGGTGTCCGGCA ATTCCGGATCCGGA(SEQ ID NO: 5) (See Addgene, available on the internet, (.addgene.org / 138149 / sequences / 2771-5668) Another exemplary nucleic acid sequence encoding Cas13Rx is: atgatcgaaaagaagaagtcatttgcaaagggcatgggagtaaaatcaacacttgtatccggttcaaaggtatacatgacgacgttcgcagaaggaagcgat gccagacttgaaaagatcgttgaaggcgattctatcagatctgtcaacgaaggagaagcgttctcagctgaaatggctgataagaatgcaggctacaagatcg gtaacgcaaagttcagccacccaaagggctatgctgtagttgcaaacaaccccttatacaccggaccggtacagcaggatatgctcggtctgaaggaaacg cttgaaaagagatattttggagagtctgccgacggaaatgataatatctgtattcaggtcatccataatatcctcgatatcgaaaagatcctcgctgaatatataac caatgctgcttatgcggtaaacaatatttccggtcttgataaggatatcatcggttttggtaagttcagtacggtctatacttatgatgagttcaaggatcctgaacat cacagagcagctttcaacaataacgataagttaattaatgccatcaaggcacagtatgatgaatttgacaatttccttgataatcctcgtctcggctactttggaca ggcttttttcagtaaggaaggcagaaattacattatcaattacggcaacgagtgttatgatattcttgctttactcagcggattgcgtcactgggtagtacataataa tgaggaagaatcaaggatttcccgtacatggctttataatctcgacaagaatcttgacaacgaatatatctctactctcaattatctgtatgatagaattacaaacga attaacaaattccttctcaaagaatagtgcagccaacgtaaactatatcgctgaaacccttggtattaatcctgctgaatttgcagagcagtatttcagattcagtat catgaaggaacagaagaatctcggtttcaatattactaagctgagagaagtaatgcttgacagaaaggatatgtctgagatccgtaaaaatcataaggtctttga ttcaatccgtactaaggtctatactatgatggatttcgttatctacagatattacattgaagaggatgcaaaggttgctgctgccaacaagtctctgccggataacg aaaaaagcctcagtgaaaaggatatctttgttataaatctcagaggaagctttaacgatgatcagaaggatgccctttattatgatgaggccaatcgtatttggag aaagctcgaaaacattatgcacaatatcaaggaattcagaggcaataagacacgtgaatacaagaagaaggatgctccaagactccccagaattcttcctgcc ggaagggatgtttccgcgttctcaaagttgatgtacgctcttaccatgttccttgatggtaaggagatcaatgatcttctcaccacgctcatcaataagttcgataa catccagagtttcctcaaggtaatgcctcttatcggagtgaatgcaaagtttgttgaggaatatgccttcttcaaggacagcgcaaagattgctgacgaactcag gctgattaagagctttgccagaatgggagaacctatcgcagatgcaagacgtgctatgtatatcgatgctatcaggattctcggaacaaacctcagctatgatgccagaagaagcagggacagaacggaaagaatcagatcgacaggtactatgagacctgtatcggcaaggacaagggcaagtctgtctccgaaaaggttgat gccctcacaaagattatcaccggtatgaactacgatcagttcgataagaagagaagcgttattgaggatactggaagagaaaacgctgagagagaaaagttc aagaagatcatcagcctctatcttactgtcatttatcacatccttaagaatattgttaatatcaatgcgcgttacgttatcggcttccattgcgttgagcgtgatgcac agctctataaggaaaagggctatgatatcaacctcaagaagctcgaagaaaaggggttttcatcagtcacaaagctgtgtgcaggtattgatgagactgctcct gacaagcgtaaggatgttgaaaaggaaatggctgagcgtgcaaaggaatctatcgatagccttgaatctgcaaatcctaagctttacgcaaactatatcaagta ttctgacgagaagaaggctgaggaatttactagacagatcaaccgtgagaaggcaaagaccgctctgaatgcatatctcagaaatactaagtggaatgtgata atcagggaagatcttcttagaatcgataataagacatgtacgctctttagaaataaggccgttcatcttgaagttgcaagatatgttcatgcatatatcaacgatatt gccgaagtaaacagctatttccagctttatcattacatcatgcagagaatcatcatgaacgaaagatatgaaaagtcttctggaaaggtaagcgaatacttcgat gctgtgaacgatgaaaagaagtacaacgacaggcttctgaagctgttgtgcgttccatttggttactgcatcccgagattcaagaatctctccattgaagctttgtt cgacaggaacgaagcagctaagtttgacaaggaaaagaagaaagtatcaggtaattcatag (SEQ ID NO: 10) An exemplary Cas13Rx protein sequence is: MIEKKKSFAKGMGVKSTLVSGSKVYMTTFAEGSDARLEKIVEGDSIRSVNEGEAFSAEMADKNAG YKIGNAKFSHPKGYAVVANNPLYTGPVQQDMLGLKETLEKRYFGESADGNDNICIQVIHNILDIEKI LAEYITNAAYAVNNISGLDKDIIGFGKFSTVYTYDEFKDPEHHRAAFNNNDKLINAIKAQYDEFDNF LDNPRLGYFGQAFFSKEGRNYIINYGNECYDILALLSGLAHWVVANNEEESRISRTWLYNLDKNLD NEYISTLNYLYDRITNELTNSFSKNSAANVNYIAETLGINPAEFAEQYFRFSIMKEQKNLGFNITKLR EVMLDRKDMSEIRKNHKVFDSIRTKVYTMMDFVIYRYYIEEDAKVAAANKSLPDNEKSLSEKDIFV INLRGSFNDDQKDALYYDEANRIWRKLENIMHNIKEFRGNKTREYKKKDAPRLPRILPAGRDVSAF SKLMYALTMFLDGKEINDLLTTLINKFDNIQSFLKVMPLIGVNAKFVEEYAFFKDSAKIADELRLIKS FARMGEPIADARRAMYIDAIRILGTNLSYDELKALADTFSLDENGNKLKKGKHGMRNFIINNVISNK RFHYLIRYGDPAHLHEIAKNEAVVKFVLGRIADIQKKQGQNGKNQIDRYYETCIGKDKGKSVSEKV DALTKIITGMNYDQFDKKRSVIEDTGRENAEREKFKKIISLYLTVIYHILKNIVNINARYVIGFHCVER DAQLYKEKGYDINLKKLEEKGFSSVTKLCAGIDETAPDKRKDVEKEMAERAKESIDSLESANPKLY ANYIKYSDEKKAEEFTRQINREKAKTALNAYLRNTKWNVIIREDLLRIDNKTCTLFANKAVALEVA RYVHAYINDIAEVNSYFQLYHYIMQRIIMNERYEKSSGKVSEYFDAVNDEKKYNDRLLKLLCVPFG YCIPRFKNLSIEALFDRNEAAKFDKEKKKVSGNS (SEQ ID NO: 9) If the Cas13Rx protein has a native HEPN domain(s) or is fused to an appropriate effector domain bearing RNase activity, the RNA can be cut. If the Cas13Rx protein has a mutated HEPN domain(s), a guide array can be processed into mature gRNAs, but the target RNA is not cut. Using this system, RNA sequences are easily targeted, for example edited or detected, optionally with an effector domain. Thus, in one example, a Cas13Rx protein has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 138, 147, 19, 153, 155, 158, 160, 162, 164, 166, 168, 170, 175, 177, 179, 181, 183, 185, 187, 189, 194, 198, 200, 202, 204, 206, 208, 210, 212, 214, 216, 218, 220, 222, 224, 226, 229, 231, 233, 235, 237, 239, 241, 243, 245, 247, 249, 251, 253, 278, 279, 280, 281, 282, 283, 284, 285, 292, 293, 294, 295, or 296 of PCT Publication No. WO 2019 / 040664, incorporated herein by reference. In one example, the Cas13 protein is expressed in a recombinant cell and purified. The resulting purified Cas13 protein, along with an appropriate guide molecule specific for the target RNA, is then introduced into the retina where one or more RNAs can be targeted. In some examples, the Cas13 proteinand guide nucleic acid molecule are introduced as components into the retina. In other examples, the purified Cas13 protein is complexed with the nucleic acid (e.g., gRNA) specific for HERV-K, and this ribonucleoprotein (RNP) complex is introduced into cells in the retina (e.g., using transfection or injection). Once the Cas13 protein and HERV-K guide nucleic acid molecule are in cells in the retina, one or more HERV-K RNAs can be targeted. In some aspects, the Cas13 is Cas13a, Cas13b, Cas13c, Cas13Rx, Cas13x, or Cas13y. In other aspects, the Cas13 is Cas13Rx. In one example, the Cas13 protein is expressed from a nucleic acid molecule in a retinal cell containing a target HERV-K. In some such examples, the Cas13 protein is expressed from a vector, such as a viral vector, for example an adenovirus vector, lentivirus vector, or baculovirus vector, or plasmid introduced into cells in the retina. This results in the production of the Cas13 protein in the retinal cells. In addition, these nucleic acid molecules can be co-expressed in cells in the retina with the guide nucleic acid molecule (e.g., gRNA) specific for HERV-K. In one example, multiple plasmids or vectors are used for RNA targeting. The nucleic acid molecule encoding the Cas13 can be provided for example on one vector or plasmid, and the guide nucleic acid molecule (e.g., gRNA) on another plasmid or vector. Multiple plasmids or viral vectors can be mixed and introduced into retinal cells at the same time, or separately. In some examples, multiple nucleic acid molecules are expressed from a single vector or plasmid. For example, a single vector can include the nucleic acid molecule encoding the Cas13, and a separate vector can include the guide molecule. In some examples a plurality of different guide molecules (e.g., gRNAs), each specific for HERV-K (such as Gag, Pol and / or Env targets), are present on a single array and / or vector. In one example, the method includes delivering a plurality of gRNAs (such as at least 2, at least 3, at least 4, at least 5, different gRNAs), which are part of an array (which can be part of a vector, such as a viral vector or plasmid). Once introduced into the retinal cells, the array is processed by the Cas13 protein, such as a Cas13Rx protein, into the individual mature gRNAs. The nucleic acid molecules expressed from the vector can be under the control of a promoter and optionally contain selection markers (such as antibiotic resistance). In one example, the method of targeting the RNA results in editing the sequence of a target RNA. For example, by using a Cas13Rx protein with a non-mutated HEPN domain (e.g., SEQ ID NO: 1, 3, 42, 62, 70, 82, 83, or 92 of PCT Publication No. WO 2019 / 040664), and a gRNA containing at least one a spacer sequence specific for the target RNA, the target RNA can be cut or nicked at a precise location. In some examples, such a method is used to decrease expression of a target HERV-K RNA, which will decrease translation of Gag, Pol and / or Env. Combination of gRNAs for these targets are also of use. In one example, targeting the target HERV-K RNA (such as Gag, Pol and / or Env) allows for decreasing expression of the protein encoded by the RNA. For example, by using a Cas13Rx fusion protein with a mutated HEPN domain and a translational repression domain (such as Pumilio or FBF PUF proteins,deadenylases, CAF1, Argonaute proteins, and and a guide RNA containing at least one spacer sequence specific for the target HERV-K RNA, of a target HERV-K RNA, such as Gag, Pol, and / or Env can be decreased. In some examples, Cas13Rx can be fused to a ribonuclease (such as a PIN endonuclease domain, an NYN domain, an SMR domain from SOT1, or an RNase domain from Staphylococcal nuclease) or a domain that affects RNA stability (such as tristetraprolin or domains from UPF1, EXOSC5, and STAU1). In another example, RNA aptamer sequences can be appended to or inserted within the gRNA molecule, such as MS2, PP7, Qβ, and other aptamers. Proteins that specifically bind to these aptamers, e.g., the MS2 phage coat protein, can be fused to a translational repression domain, a ribonuclease, or a domain that affects RNA stability. This aptamer-effector domain fusion can be used to target the target RNA because the Cas13 and gRNA complex will guide the aptamer protein-effector domain in proximity to the target RNA. In one example, the target RNA is an HERV-K RNA, such as encoding Gag, Pol or Env. For example, a Cas13 protein and a guide RNA containing at least one spacer sequence specific for a HERV-K RNA can be used. In some examples, such a method is used to reduce HERV-K translation. In some examples, the gRNA that hybridizes with the one or more target HERV-K RNA molecules includes one or more direct repeat (DR) sequences, one or more spacer sequences, or one or more sequences comprising DR-spacer-DR-spacer. In some examples, the one or more DR sequences have at least 80%, at least 85%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to SEQ ID NO: 129, 130, 131, 132, 133, 134, 135, 136, 137, 148, 150, 151, 152, 154, 156, 157, 159, 161, 163, 165, 167, 169, 176, 178, 180, 182, 184, 186, 188, 190, 191, 192, 193, 199, 201, 203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, 227, 228, 230, 232, 234, 236, 238, 240, 242, 244, 246, 248, 250, 252, or 254 of PCT Publication No. WO 2019 / 040664, incorporated herein by reference. In one example, the gRNA includes additional sequences, such as an aptamer sequence. In some examples, a plurality of gRNAs are processed from a single array transcript, wherein each gRNA can be different, for example to target different RNAs (such as two or more of HERV-K Gag, Pol and Env) or target multiple regions of a single RNA (such as HERV-K Gag, Pol or Env). A guide sequence can also include one or more direct repeats (DRs). The DR is the constant portion of the guide, which contains strong secondary structure, which facilitates interaction between a Cas13 protein and the guide molecule. Methods of targeting one or more target HERV-K RNA molecules are provided. Targeting an RNA molecule can include one or more of cutting or nicking one or more target HERV-K RNA molecules, such as encoding Gag, Pol and / or Env, deactivating or downregulating one or more target HERV-K RNA molecules, deactivating or suppressing translation the one or more target HERV-K RNA molecules, visualizing, labeling, or detecting the one or more target HERV-K RNA molecules, binding the one or more target HERV-K RNA molecules, editing the one or more target HERV-K RNA molecules, trafficking the one or more target HERV-K RNA molecules, and masking the one or more target HERV-K RNA molecules. In some examples, modifying one or more target HERV-K RNA molecules includes one or more of anRNA base substitution, an RNA base deletion, an RNA base insertion, or a break in the target HERV-K RNA. gRNA molecules can include naturally occurring or non-naturally occurring nucleotides or ribonucleotides (such as LNAs or other chemically modified nucleotides or ribonucleotides, for example to protect a guide RNA from degradation). In some examples, the guide sequence is RNA. The guide nucleic acid can include modified bases or chemical modifications (e.g., see Latorre et al., Angewandte Chemie 55:3548-50, 2016). A guide sequence directs a Cas13 protein to a target HERV-K RNA, thereby targeting the HERV-K RNA (e.g., modifying or detecting the RNA). The ability of a guide sequence to direct sequence-specific binding of a CRISPR complex to a target HERV-K RNA may be assessed by any suitable assay. For example, the components of a CRISPR system sufficient to form a CRISPR complex, including the guide sequence to be tested, may be provided to a host cell having the corresponding target HERV-K RNA molecule, such as by transfection with vectors encoding the components of the CRISPR sequence, followed by an assessment of preferential cleavage within the target sequence. Similarly, cleavage of a target HERV-K RNA sequence may be evaluated in a test tube by providing the target HERV-K RNA, components of a CRISPR complex, including the guide sequence to be tested and a control guide sequence different from the test guide sequence, and comparing binding or rate of cleavage at the target HERV-K RNA between the test and control guide sequence reactions. Other assays are possible. Also provided are vectors, such as a viral vector or plasmid (e.g., retrovirus, lentivirus, adenovirus, adeno-associated virus, or herpes simplex virus), that includes a guide nucleic acid molecule that targets HERV-K. In some examples, the guide nucleic acid molecule is operably linked to a promoter or expression control element (specific examples of which are provided elsewhere in this application). As described elsewhere herein, such vectors can include other elements, such as a gene encoding a selectable marker, such as an antibiotic, such as puromycin, hygromycin, or a detectable marker such as GFP or other fluorophore. The vector can be an adenovirus vector. The vector can be a lentiviral vector. The vector can be a baculovirus vector. In some aspects, the lentiviral vector, the adenoviral vector, or the baculovirus vector comprises an inducible (such as a doxycycline inducible promoter) or constitutive (e.g., CMV) or tissue- specific (e.g., RPE-specific) promoter operably linked to a nucleic acid molecule encoding the Cas13, such as Cas13Rx. Guide molecules can include one or more regions referred to as spacers. A spacer has sufficient complementarity with a target HERV-K RNA sequence to hybridize with the target HERV-K RNA and direct sequence-specific binding of a Cas13 protein, such as Cas 13d, to the target HEV-K RNA. Thus, the spacer is the variable portion of the guide sequence. In some examples, a spacer has 100% complementarity to a target HERV-K RNA (or region of the HERV-K RNA to be target), but a spacer can have less than 100% complementarity to a target RNA, such as at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or at least 99% complementarity to a target RNA. In some aspects the gRNA specifically hybridizes to a) an RNA encoding glycosaminoglycan (Gag) protein of HERV-K or a nucleic acid moleculeencoding the gRNA; b) an RNA encoding (Pol) protein of HERV-K or a nucleic acid molecule encoding the gRNA; or c) an RNA encoding (Env) protein of HERV-K or a nucleic acid molecule encoding the gRNA. Exemplary guide molecules s are provided as SEQ ID NOs: 1-3 of the present disclosure. Delivery of nucleic acid molecules is described below. Host cells are also provided that are transduced with the disclosed vectors. These host cells can be in vitro. In some aspects, the cell is as a retinal pigment epithelial cell, a photoreceptor cell, or a choroidal cell. D. Anti-Retroviral Agents It is disclosed herein that one or more anti-viral agents can inhibit HERV-K, and thus are of use for treating AMD. In some aspects, an effective amount of reverse transcriptase inhibitor, such as lamivudine, zidovudine, abacavir, tenofovir, a tenofovir prodrug, emtricitabine (FTC), or a pharmaceutically acceptable salt thereof is administered to a subject that has AMD, or is at risk of developing AMD. In some aspects, an effective amount of a reverse transcriptase inhibitor is administered to the subject. The reverse transcriptase inhibitor can be abacavir or zidovudine. The reverse transcriptase inhibitor can be efavirenz, etravirine or nevirapine. In one non-limiting example, the reverse transcriptase inhibitor is nevirapine. In other aspects, and effective amount of an integrase inhibitor is administered to the subject. The integrase inhibitor can be raltegravir. In further aspects, an effective amount of a protease inhibitor can be administered to the subject. The protease inhibitor can be darunavir. The disclosed methods can use an effective amount of a NRTI, a NtRTI, an integrase inhibitor, and / or a protease inhibitor. Combinations of these agents are also of use. Suitable agents are also disclosed in Tyagi et al, supra, 2017, which is incorporated by reference herein. NtRTI operative in the treatment of AMD, or reducing the risk of developing AMD include tenofovir, tenofovir prodrugs such as tenofovir disproxil fumerate (TDF) or Tenofovir alafenamide (TAF), adefovir; 2′,3′-dideoxy-3′-fluoroadenisine; 2′,3′-dideoxy-3′-fluoroguanasine; 3′deoxy-3′-fluoro-5-O-[2-(L- valyloxy)-propionyl]guanosine and include pharmaceutically acceptable salts, esters, ester salts, nitrile oxides, and other prodrugs of any of the active agents. An A NRTI operative in the treatment of AMD, or of use in reducing the risk of developing AMD, includes FTC, lamivudine, zalcitabine, zidovudine, azidothymidine, didanosine, stavudine, and abacavir. Other antiretrovirals such as nonnucleoside reverse transcriptase inhibitors, protease inhibitors, fusion inhibitors, and combinations thereof, are also of use. Representative non-nucleoside reverse transcriptase inhibitors operative herein illustratively include delavirdine, efavirenz, nevirapine, and other diarylpyrimidine (DAPY) derivatives. Representative protease inhibitors operative herein illustratively include amprenavir, tipranavir, indinavir, saquinavir, lopinavir, ritonavir, fosamprenavir calcium, ritonavir, atazanavir sulfate nelfinavir mesylate, darunavir, and combinations thereof. An entry inhibitor operative herein as an optional active ingredient in an inventive composition illustratively includes enfuvirtide, Schering C (Schering Plough), S-1360 (Shionogi), and BMS806 (Bristol Myers Squibb). Derivates and salts of use in the disclosed methods include salts such asalkali metal salts; esters such as acetate, butyrate, palmitate, chlorobenzoates, benzoates, C1-C6 benzoates, succinates, and mesylate; salts of such esters; and nitrile oxides. Pharmaceutically acceptable salts, esters, ester salts, nitrile oxides, and prodrugs of any of the active agents are also of use in the disclosed methods. In some aspects, both a NRTI and / or an NtRTI is / are administered to the subject. The NRTI and / or the NtRTI can be administered as a prodrug. As used herein the term “prodrug” includes a compound that when administered to a primate host generates an active NRTI or NtRTI as a result of spontaneous reaction under physiological conditions, enzymatic catalysis, metabolic clearance, or combinations thereof. An exemplary NtRTI prodrug currently FDA approved for HAART use is tenofovir disoproxil fumarate (TDF) and is detailed in U.S. Patent 5,935,946, TAF and succinate salts of tenofovir. In some aspects, the methods include the administration of tenofovir, TAF and / or TDF. In further aspects, an effective amount of a protease inhibitor, such as amprenavir, tipranavir, indinavir, saquinavir, lopinavir, ritonavir, fosamprenavir calcium, ritonavir, atazanavir sulfate nelfinavir mesylate, and darunavir, is administered. In a specific non-limiting example, an effective amount of darunavir is administered to the subject. In another specific non-limiting example, an effective amount of a) tenofovir, TAF, and / or TDF is administered to the subject, and b) a protease inhibitor is administered to the subject. In another specific non-limiting example, an effective amount of a) tenofovir, TAF, and / or TDF is administered to the subject, and b) darunavir is administered to the subject. Other analogs of pharmaceutically active NRTIs, NtRTIs, or integrase inhibitors are also suitable for use. A pharmaceutically acceptable carrier or diluent includes agents that are compatible with other ingredients of a dosage and not injurious to the subject with AMD, or at risk for AMD. In some aspects, the methods include the administration of an effective amount of a) tenofovir, TAF and / or TDF, and b) FTC. In other aspects, the methods include the administration of an effective amount of a) tenofovir, TAF and / or TDF, and b) darunavir. In some aspects, an NRTI, NtRTI and optionally an integrase inhibitor are administered concurrently, such as in a single formulation, to the subject. This combination can be co-administered with or without a pharmacoenhancer, such as, but not limited to, cobistat (COBI). In some aspects, the methods include the administration of an effective amount of a) tenofovir, TAF and / or TDF, b) FTC; and c) COBI. In some aspects, the methods utilize a combination of at least one NRTI, at least one NtRTI, and optionally at an integrase inhibitor. The integrase inhibitor can be elvitegravir (EVG). In some aspects, the methods include the administration of an effective amount of a) tenofovir, TAF and / or TDF, b) FTC; c) COBI; and d) EVG. In further aspects, and effective amount of a protease inhibitor, such as, but not limited to darunavir, is administered to the subject. In some aspects, these can be compounded into a dosage form suitable for delivery by a route with administration by intraocular (e.g., into the eye), oral, rectal, topical, vaginal or parenteral routes of administration. Compositions and compounding methods are provided, for example in Remington’s Science and Practice of Pharmacology, 20th Edition, Chapters 37-47, pages 681-929, where parenteral injection includes subcutaneous, intramuscular, intravenous, and intradermal injection. In some aspects,administration is oral. The administration can be into the eye as a suspension, slow release implant or eye drops. In some aspects, the disclosed methods include co-administering to a subject, such as a human having or at risk of developing AMD, a combination of a pharmacologically effective amount of the nucleoside reverse transcriptase inhibitor, such as, but not limited to, FTC, an effective amount of the nucleotide reverse transcriptase inhibitor, such as, but not limited to, tenofovir or a tenofovir prodrug such as, but not limited to, a tenofovir salt such as TDF, TAF, or another salt form of tenofovir. Optionally, the subject can also be administered an effective amount of an integrase inhibitor, such as, but not limited to, EVG. Optionally, the subject can be administered an effective amount of a protease inhibitor, such as darunavir. These combinations can be co-administered with or without a pharmacoenhancer, such as, but not limited to, COBI. In some aspects, the co-administration is oral. In more aspects, the co-administration is simultaneous. In some aspects, an effective amount of a nucleoside reverse transcriptase inhibitor, such as, but not limited to, FTC, an effective amount of a nucleotide reverse transcriptase inhibitor, such as, but not limited to, tenofovir or a tenofovir prodrug such as TDF or TAF, and optionally an effective amount of an integrase inhibitor, such as EVG, can be formulated in a single composition, such as in a unit dose. Optionally, an effective amount of a pharmacoenhancer, such as COBI, is included in this same composition. In some aspects, the composition can be formulated for oral administration. Thus, these active agents can be combined into a single unit dose and administered to a subject having, or at risk of developing, AMD. The doses of individual active components are administered in effective amounts, to create a therapeutic concentration of the active composition at the retina. It is appreciated that establishing an effective concentration for a given active agent in the target cells, such as the retina, includes factors for the agent such as the route of administration, pharmacokinetics, absorption rate based on administration route, effects of food on oral absorption, in vivo distribution, metabolic pathways, elimination route, race, gender, and age of the subject, single dose incident side effects, long term administration side effects, and synergistic effects with co-administered active agents. Information related to these factors considered in dosing are available from the United States Food and Drug Administration (fda.gov / oashi / aids / virals.html). In some aspects, the dosing according to the present methods utilize as a starting point the maximal recommended tolerated dosing levels for the given active agent combination associated with HAART treatment protocols. In some aspects, the methods include oral administration of TAF / TDF / tenofovir / salt to a subject having AMD, or at risk of developing AMD. In more aspects, the methods include oral co-administration of FTC, TAF / TDF / tenofovir / salt to a subject having AMD, or at risk of developing AMD. In more aspects, FTC, TAF / TDF / tenofovir / salt, and EVG are administered to the subject having AMD, or at risk of developing AMD. In other aspects, the method includes oral co-administration of FTC, TAF / TDF / tenofovir / salt, optionally EVG and optionally COBI to the subject. In further aspects, FTC, TAF / TDF / tenofovir / salt, EVG, and COBI are administered to the subject. In specific non-limiting examples, TAF is used in any of the above combinations. In other non-limiting examples, TDF is used inany of the above combinations. U.S. Published Patent Application incorporated herein by reference, discloses the use of FTC, TAF and other tenofovir prodrugs, EVG, and COBI for the treatment of HIV infections. As disclosed in this published patent application, an oral dose of TAF can be in the range from about 0.0001 to about 100 mg / kg body weight per day, for example, from about 0.01 to about 10 mg / kg body weight per day, from about 0.01 to about 5 mg / kg body weight per day, from about 0.5 to about 50 mg / kg body weight per day, from about 1 to about 30 mg / kg body weight per day, from about 1.5 to about 10 mg / kg body weight per day, or from about 0.05 to about 0.5 mg / kg body weight per day. As a non-limiting example, the daily dose for an adult human of about 70 kg body weight will range from about 0.1 mg to about 1000 mg, or from about 1 mg to about 1000 mg, or from about 5 mg to about 500 mg, or from about 1 mg to about 150 mg, or from about 5 mg to about 150 mg, or from about 5 mg to about 100 mg, or about 10 mg, and may take the form of single or multiple doses. In one aspect, the oral dose of TAF may be in the form of a combination of agents (e.g., TAF / FTC / EVG / COBI). When COBI or a pharmaceutically acceptable salt thereof is combined with certain specific solid carrier particles (e.g., silica derivatives), the resulting combination possesses improved physical properties. For example, the resulting combination has low hygroscopicity as compared to COBI alone. Additionally, the resulting combination is a free-flowing powder, with high loading values for COBI, acceptable physical and chemical stability, rapid drug release properties, and excellent compressibility. Thus, the resulting combination can readily be processed into solid dosage forms (e.g., tablets). Thus, COBI can be used with any suitable solid carrier, provided the resulting combination has physical properties that allow it to be more easily formulated than the parent compound. For example, suitable solid carriers include kaolin, bentonite, hectorite, colloidal magnesium-aluminum silicate, silicon dioxide, magnesium trisilicate, aluminum hydroxide, magnesium hydroxide, magnesium oxide and talc. In one aspect, the solid carrier can comprise calcium silicate or magnesium aluminometasilicate. COBI can be coated in the pores and on the surface of a solid carrier. Suitable silica derivatives of use are disclosed in PCT Publication WO 03 / 037379. Exemplary oral dosages of use in the disclosed methods are (1) COBI: 10-500 mg, 50-500 mg, 75- 300 mg, 100-200 mg, or 150 mg; (2) TAF: 1-60 mg, 3-40 mg, 5-30 mg, 8-20 mg, or 10 mg; (3) FTC: 10-500 mg, 50-500 mg, 75-300 mg, 150-250 mg, or 200 mg; and (4) EVG: 10-500 mg, 50-500 mg, 75-300 mg, 100- 200 mg, or 150 mg. Tenofovir can be used in amounts of less than 300 mg, 200 mg or less and 100 mg or less. COBI can be used in amounts of 50-500 mg, 100-400 mg, 100-300 mg, and 150 mg. Tenofovir (or TDF or TAF or another salt form) and COBI or pharmaceutically acceptable salt(s) thereof, can be co-administered orally. Tenofovir (or TDF or TAF or another salt form), COBI, FTC, and EVG can be co-administered. Tenofovir (or TDF or TAF) and COBI can be co-administered in a single pharmaceutical composition. Tenofovir (or TDF or TAF or another salt form), COBI, FTC, and EVG can be co-administered in a single pharmaceutical composition. In the case of administering a pharmaceutically acceptable salt or complex of an agent, the amount administered can be adjusted relative to the weight of the component added to produce the salt or complex.The method can include co-administering 200 mg of FTC and 150 mg of EVG. The method can include co-administering 150 mg COBI, 100 mg or tenofovir, 150 mg EVG, and 200 mg FTC. The method can include co-administering 150 mg COBI, 200 mg or less tenofovir, 150 mg EVG, and 200 mg FTC. The method can include co-administering 150 mg COBI, less than 300 mg tenofovir, 150 mg EVG, and 200 mg FTC. The method can include co-administering 150 mg COBI, 50 mg tenofovir, 150 mg EVG, and 200 mg FTC. In some specific non-limiting example, the method can include co-administering 150 mg EVG, 150 mg COB, 200 mg FTC, and 10 mg TAF. These compositions can be administered orally. See U.S. Published Patent Application No.2015 / 0105350, incorporated herein by reference for additional dosing information. In some aspects, GENVOYA® is administered to the subject. In further aspects, administration is oral. An effective amount of one or more additional agents can be administered to a subject. These agents include, but are not limited to, and effective amount of L-745,870 trihydrochloride and an effective amount of metformin or metformin hydrochloride. The active agents may be administered to the subject in any conventional manner. Local modes of administration include, by way of example, intraocular, intraorbital, subconjunctival, sub-Tenon’s, subretinal or transscleral routes. In an aspect, significantly smaller amounts of the components (compared with systemic approaches) may exert an effect when administered locally (for example, intravitreally) compared to when administered systemically (for example, orally). In one aspect, the system disclosed herein is delivered by intravitreal injection. Intravitreal injection has a relatively low risk of retinal detachment. Any method for administration of agents to the eye can be used to administer components described herein. In some aspects, administration is from an internal reservoir (for example, from an implant disposed at an intra- or extra-ocular location (see, U.S. Pat. Nos.5,443,505 and 5,766,242)) or from an external reservoir (for example, from an intravenous bag). Components can be administered by continuous release for a particular period from a sustained release drug delivery device immobilized to an inner wall of the eye or via targeted transscleral controlled release into the choroid (see, for example, PCT / US00 / 00207, PCT / US02 / 14279, Ambati et al., Invest. Opthalmol. Vis. Sci.41:1181-1185, 2000, and Ambati et al., Invest. Opthalmol. Vis. Sci.41:1186-1191, 2000). A variety of devices suitable for administering components locally to the inside of the eye are known. See, for example, U. S. Patent No.6,251,090, U. S. Patent No.6,299,895, U. S. Patent No.6,416,777, U. S. Patent No.6,413,540, and PCT Publication No. PCT / US00 / 28187. Additional methods for intraocular administration are provided below, and can be used with antiretroviral agents. While it is possible for the active agents to be administered as raw compounds, they can be administered as one or more pharmaceutical compositions. The salt, carrier, or diluent should be acceptable in the sense of being compatible with the other ingredients and not deleterious to the recipient thereof. Examples of carriers or diluents for oral administration include cornstarch, lactose, magnesium stearate, talc, microcrystalline cellulose, stearic acid, povidone, crospovidone, dibasic calcium phosphate, sodium starch glycolate, hydroxypropyl cellulose (e.g., low substituted hydroxypropyl cellulose), hydroxypropylmethyl cellulose (e.g., hydroxypropylmethyl cellulose 2910), and sodium lauryl sulfate. The pharmaceuticalcompositions can be prepared by any suitable such as those methods well known in the art of pharmacy, for example, methods such as those in Gennaro et al., Remington's Pharmaceutical Sciences (18th ed., Mack Publishing Co., 1990), especially Part 8: Pharmaceutical Preparations and their Manufacture. In some aspects, the active agents are formulated for oral administration. In some aspects, the active agents are formulated for local administration to the eye. Such methods include the step of bringing into association the active agents with the carrier or diluent and optionally one or more accessory ingredients. Such accessory ingredients include those conventional in the art, such as, fillers, binders, excipients, disintegrants, lubricants, colorants, flavoring agents, sweeteners, preservatives (e.g., antimicrobial preservatives), suspending agents, thickening agents, emulsifying agents, and / or wetting agents. The pharmaceutical compositions of use in the methods disclosed herein can provide controlled, slow release or sustained release of the active agents over a period of time. The controlled, slow release or sustained release of the agents can maintain the agents in the bloodstream of the human for a longer period of time than with conventional formulations. Pharmaceutical compositions include, but are not limited to, coated tablets, pellets, solutions (such as eye drops), powders, capsules, and dispersions in a medium that is insoluble in physiologic fluids, or where the release of the therapeutic compound follows degradation of the pharmaceutical composition due to mechanical, chemical, or enzymatic activity. For oral administration, fine powders or granules may contain diluting, dispersing, and or surface-active agents and may be present, for example, in water or in a syrup, in capsules or sachets in the dry state, or in a non- aqueous solution or suspension wherein suspending agents may be included, or in tablets wherein binders and lubricants may be included. When administered in the form of a liquid solution or suspension, the formulation may contain one or more active ingredients and purified water. Optional components in the liquid solution or suspension include suitable sweeteners, flavoring agents, preservatives (e.g., antimicrobial preservatives), buffering agents, solvents, and mixtures thereof. A component of the formulation may serve more than one function. For example, a suitable buffering agent also may act as a flavoring agent as well as a sweetener. Suitable sweeteners include, for example, saccharin sodium, sucrose, and mannitol. A mixture of two or more sweeteners may be used. The sweetener or mixtures thereof are typically present in an amount of from about 0.001% to about 70% by weight of the total composition. Suitable flavoring agents may be present in the pharmaceutical composition to provide a flavor to make the pharmaceutical composition easier for a human to ingest. The flavoring agent or mixtures thereof are typically present in an amount of about 0.0001% to about 5% by weight of the total composition. Preservatives can also be present in the composition. Suitable preservatives include, for example, methylparaben, propylparaben, sodium benzoate, and benzalkonium chloride. A mixture of two or more preservatives may be used. The preservative or mixtures thereof are typically present in an amount of about 0.0001% to about 2% by weight of the total composition. Buffering agents can also be present in the compositions. Suitable buffering agents include, for example, citric acid, sodium citrate, phosphoric acid, potassium phosphate, and various other acids and salts. A mixture of two or more buffering agents may beused. The buffering agent can be present in an amount of about 0.001% to about 4% by weight of the total composition. A solvent can be used when a liquid suspension is desirable. Suitable solvents for a liquid solution or suspension include, for example, sorbitol, glycerin, propylene glycol, and water. A mixture of two or more solvents may be used. The solvent or solvent system can present in an amount of about 1% to about 90% by weight of the total composition. These types of formulations are disclosed, for example, in U.S. Published Patent Application No.2015 / 0105350, which is incorporated herein by reference. In further aspects, active agents (such as TAF / TDF / tenofovir / salt, FTC, EVG, darunavir, and optionally COBI) are co-administered to a subject at specific time points. In some aspects, the present methods utilize doses of agents. In some aspects, each dose can include oral co-administration of FTC, TAF / TDF / tenofovir / salt, and EVG. In other aspects, each dose can include oral co-administration of FTC, TAF / TDF, EVG and COBI. In specific non-limiting examples, TAF is included in the dose(s). E. Agents that increase ANG activity It is also disclosed herein that one or more agents that increass ANG activity, such as increasing ability of ANG to generate tRNA fragments that are inhibitory to HERV-K, and reduce expression of HERV-K, are of use for treating AMD. ANG itself, or a nucleic acid molecule encoding ANG, can be used treat AMD in a subject, or can can be used to decrease the risk of AMD. An increase in ANG activity generates tRNA fragments that are complementary to an HERV-K coding sequence. Without being bound by theory, downregulation of ANG expression is associated with an increase in HERV-K mRNA. ANG, a ribonuclease (cleaves double stranded RNA) uses a tRNA fragment complementary to HERV-K. This tRNA fragment forms a double strand to HERV-K allowing ANG to degrade this double stranded RNA. An increase in ANG expression (with or without the tRNA fragment) downregulates HERV-K expression, and can be used to treat AMD, or reduce the risk of developing AMD. In some aspects, agents that increase ANG activity are of use to treat AMD. These agents can increase ANG activity, for example, by about 1 to about 10 fold, such as about 2 to about 10 fold, for example, about 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 fold. The methods can include, without limitation, the administration of ANG, a nucleic acid molecule encoding ANG, tRNA fragment, or a nucleic acid molecule encoding a tRNA fragment. Combinations of these agents are also of use. 1. ANG Proteins An exemplary protein sequence for ANG is disclosed in GENBANK® Accession No.AAA51678.1, October 30, 1994, incorporated herein by reference. An exemplary amino acid sequence for ANG also is provided below: MVMGLGVLLLSH VFVLGLGLTP PTLAQDNSRY THFLTQHYDA KPQGRDDRYC ESIMRRRGLT SPCKDINTFI HGNKRSIKAI CENKNGNPHR ENLRISKSSF QVTTCKLHGG SPWPPCQYRATAGFRNVVVA CENGLPVHLD QSIFRRP 11). The amino acid sequence for an angiogenin precursor protein is provided in GENBANK® No. NP_001091046, August 16, 2022, incorporated herein by reference. An exemplary nucleic acid sequence encoding ANG is provided in GENBANK Accession No. NM_001145.4, August 15, 2022, incorporated herein by reference. GTCCTGCCAA AGAAAGCAGC AGCGAATAAG TACGTGGCAG ATGGTGCTGT CGACCAGTGT CAAGACCAAG TTTCATGGGT TCCTGGACGC TCAGCCAGGG GTAGTCTCTG AAGGGCCGCC TGGCAATTGG GAGCAGAAGC CAGTTTCCCG CCATCTGCTC TCCGTGGAGG CAGTGCTCTC GCGGCTGCTG CCCGTTGGGG TCCAGCTGAG GAAGGAGCGC GGATCCCAGG CTCGTTCTTT GCCTGGGCTG CCCCTGCGGC CCCTGGGGCG GGTGCTGCTG CGGCGCCAGC TCCAAGGGCG GATCCAGGCG GGAGGGGCCT CCTCGGAGAA GCGGGGCGCG GTCCCAACTA CGCAGAGGCT GGCACGCCGA CCCTCCACAC CTCACCACGC CCCCATCTCC GTCCGTGTAC ACACACTCAC ACAAGGACGC CAACCCCACC TAGATGCAAA GCAGGATTCA AAAGAACATC TTTGCGTTTT CTACCGGCTC CCCATCATCG TACTAGGGAG GAAGAAGCGG GTGAGAAACA AAACTTCTTT CCATTGTCCT GCCCGTTTCT GCGGACTTGT TCTGAGGCCG AGGAGCCTGT GTTGGAAGAG ATGGTGATGG GCCTGGGCGT TTTGTTGTTG GTCTTCGTGC TGGGTCTGGG TCTGACCCCA CCGACCCTGG CTCAGGATAA CTCCAGGTAC ACACACTTCC TGACCCAGCA CTATGATGCC AAACCACAGG GCCGGGATGA CAGATACTGT GAAAGCATCA TGAGGAGACG GGGCCTGACC TCACCCTGCA AAGACATCAA CACATTTATT CATGGCAACA AGCGCAGCAT CAAGGCCATC TGTGAAAACA AGAATGGAAA CCCTCACAGA GAAAACCTAA GAATAAGCAA GTCTTCTTTC CAGGTCACCA CTTGCAAGCT ACATGGAGGT TCCCCCTGGC CTCCATGCCA GTACCGAGCC ACAGCGGGGT TCAGAAACGT TGTTGTTGCT TGTGAAAATG GCTTACCTGT CCACTTGGAT CAGTCAATTT TCCGTCGTCC GTAACCAGCG GGCCCCTGGT CAAGTGCTGG CTCTGCTGTC CTTGCCTTCC ATTTCCCCTC TGCACCCAGA ACAGTGGTGG CAACATTCAT TGCCAAGGGC CCAAAGAAAG AGCTACCTGG ACCTTTTGTT TTCTGTTTGA CAACATGTTT AATAAATAAA AATGTCTTGA TATCAGTAAG AA (SEQ ID NO: 14) Any fragment, variant, or precursor protein of ANG having ANG activity, as well as nucleic acid molecules encoding such proteins, is of use in the methods disclosed herein, provided it functions to inhibit HERV-K. In some aspects, a variant of ANG of use in the methods disclosed herein includes an amino acid sequence having at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 11 (or a nucleic acid encoding such). The variant of ANG can include at most 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2 or 1 conservative substitutions in SEQ ID NO: 11. The protein can be naturally occurring or recombinant. In some aspects, a variant of ANG, of use in the disclosed methods, comprises, consists essentially of, or consists of an amino acid sequence at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identical to SEQ ID NO: 11 (or a nucleic acid encoding such). In other aspects, ANG comprises, consists essentially of, or consists of, SEQ ID NO: 11 (or a nucleic acid encoding such). In more aspects, a fragment of ANG is of use in the disclosed methods. The use of ANG, and variants thereof, is disclosed, for example, in U.S. Published Patent Application No.2013 / 0136727 A1. ANG, variants and fragments thereof, can be prepared usingrecombinant methods, such as expression in host cells. Exemplary nucleic acid molecules can be prepared by cloning techniques (see below). Examples of cloning and sequencing techniques, and instructions sufficient to direct persons of skill through many cloning exercises are known (see, e.g., Sambrook et al. (Molecular Cloning: A Laboratory Manual, 4thed, Cold Spring Harbor, New York, 2012) and Ausubel et al. (In Current Protocols in Molecular Biology, John Wiley & Sons, New York, through supplement 104, 2013). Hosts can include microbial, yeast, insect and mammalian organisms. DNA sequences having eukaryotic or viral sequences can be expressed in prokaryotes or eukaryotes. Non-limiting examples of suitable host cells include bacteria, archea, insect, fungi (for example, yeast), plant, and animal cells (for example, mammalian cells, such as human). Exemplary cells of use include Escherichia coli, Bacillus subtilis, Saccharomyces cerevisiae, Salmonella typhimurium, SF9 cells, C129 cells, HEK 293 cells, Neurospora, and immortalized mammalian myeloid and lymphoid cell lines. Techniques for the propagation of mammalian cells in culture are well-known (see, e.g., Helgason and Miller (Eds.), 2012, Basic Cell Culture Protocols (Methods in Molecular Biology), 4thEd., Humana Press). Examples of commonly used mammalian host cell lines are VERO and HeLa cells, CHO cells, and WI38, BHK, and COS cell lines, although cell lines may be used, such as cells designed to provide higher expression, desirable glycosylation patterns, or other features. In some aspects, the host cells include HEK 293 cells or derivatives thereof, such as GnTI- / -cells (ATCC® No. CRL-3022), or HEK-293F cells. Transformation of a host cell with recombinant DNA can be carried out by conventional techniques. In some aspects, where the host is prokaryotic, such as, but not limited to, E. coli, competent cells which are capable of DNA uptake can be prepared from cells harvested after exponential growth phase and subsequently treated by the CaCl2method. Alternatively, heat shock, MgCl2or RbCl can be used. Transformation can also be performed after forming a protoplast of the host cell if desired, or by electroporation. When the host is a eukaryote, such methods of transfection of DNA as calcium phosphate coprecipitates, conventional mechanical procedures such as microinjection, electroporation, insertion of a plasmid encased in liposomes, or viral vectors can be used. Eukaryotic cells can also be co-transformed with polynucleotide sequences encoding a disclosed antigen, and a second foreign DNA molecule encoding a selectable phenotype, such as the herpes simplex thymidine kinase gene. Another method is to use a eukaryotic viral vector, such as simian virus 40 (SV40) or bovine papilloma virus, to transiently infect or transform eukaryotic cells and express the protein (see for example, Viral Expression Vectors, Springer press, Muzyczka ed., 2011). Appropriate expression systems such as plasmids and vectors of use in producing proteins in cells including higher eukaryotic cells such as the COS, CHO, HeLa and myeloma cell lines. ANG also can be produced using chemical synthesis.2. Nucleic acid molecules encoding ANG and tRNA In some aspects, nucleic acid molecules ANG, a precursor, variant or fragment are also of use in the disclosed methods. By introducing a nucleic acid encoding ANG, a precursor, variant or fragment, the amount ANG is increased, and thus the activity of ANG is also increased. In more aspects, a tRNA complementary to HERV-K, or a fragment thereof, is also of use in the disclosed methods, and can be encoded by a DNA molecule (see Gene ID: 100189107). Two tRNA fragments (encoded by a DNA) that are complementary to HERV-K are LYS CTT (GCCCCACGTTGGGCGCCA, SEQ ID NO: 12) and LYS TTT (GTCCCTGTTCGGGCGCCA, SEQ ID NO: 13), see, for example, Tao et al., supra, 2020. SEQ ID NO: 12 and SEQ ID NO: 13 are the sequences from the genomic DNA of tRNA- CTT (Gene ID: 100189107, May 13, 2022 from the National Library of Medicine, incorporated herein by reference) and tRNA-TTT (Gene ID: 7206, May 13, 2022, for the National Library of Medicine, incorporated herein by reference). These tRFs or tiRNA are complementary to HERV-K. Three nucleotides, CCA, added at the end of a tRNA and may not be complementary to HERV-K. These are all of use in the methods disclosed herein. In some aspects, the tRNA fragment is 16 to 22 nucleotides in length, such as 17 to 21 nucleotides in length, for example, 16, 17, 18, 19.20, 21 or 22 nucleotides in length. In one aspect, the tRNA fragment is 18 nucleotides in length. In more aspects, the tRNA is encoded by SEQ ID NO: 12 or SEQ ID NO: 13. In further aspects, the tRNA includes CCA. One or both of these tRNA fragments can be expressed to increase ANG activity and downregulate HERV-K expression. tRFs are generated by ANG, but AGO proteins can also be involved in using these tRFs to target HERV-K coding sequence. Thus, increasing ANG activity can, in some aspects, block HERV-K translation into GAG, POL, ENV proteins and induce degradation of the entire mRNA due to double-stand loops between tRFS and the HERV-K coding RNA. See Shorn et al., Trends Cell Biol.28(10): 793–806. doi:10.1016 / j.tcb.2018.05.006 (October 2018). Expression of one or both of these tRNA fragments will increase the activity of ANG. Thus, in some aspects, a nucleic acid molecule encoding one or both of these tRNAs is of use in the disclosed methods. These tRNA can be used in the presently disclosed methods, with, or without, ANG or a nucleic molecule encoding exogenous ANG. Nucleic acid molecules can be prepared by amplification methods. Amplification methods include polymerase chain reaction (PCR), the ligase chain reaction (LCR), the transcription-based amplification system (TAS), the self-sustained sequence replication system (3SR). A wide variety of cloning methods, host cells, and in vitro amplification methodologies are well known to persons of skill. RNA molecules are also of use. The polynucleotides encoding ANG (ora precursor, variant, or fragment thereof), or encoding a tRNA, can include a recombinant DNA which is incorporated into a vector (such as an expression vector) into an autonomously replicating plasmid or virus or into the genomic DNA of a prokaryote or eukaryote, or which exists as a separate molecule (such as a cDNA) independent of other sequences. The nucleotides canbe ribonucleotides, deoxyribonucleotides, or modified forms of either nucleotide. The term includes single and double forms of DNA. Polynucleotides encoding ANG, a precursor, variant or fragment thereof, or encoding a tRNA fragment, are of use in the disclosed methods include DNA, cDNA, tRNA sequences themselves, and an RNA sequences that encode ANG, a precursor, variant, or fragment thereof. Silent mutations in the coding sequence result from the degeneracy (i.e., redundancy) of the genetic code, whereby more than one codon can encode the same amino acid residue. Thus, for example, leucine can be encoded by CTT, CTC, CTA, CTG, TTA, or TTG; serine can be encoded by TCT, TCC, TCA, TCG, AGT, or AGC; asparagine can be encoded by AAT or AAC; aspartic acid can be encoded by GAT or GAC; cysteine can be encoded by TGT or TGC; alanine can be encoded by GCT, GCC, GCA, or GCG; glutamine can be encoded by CAA or CAG; tyrosine can be encoded by TAT or TAC; and isoleucine can be encoded by ATT, ATC, or ATA. Tables showing the standard genetic code can be found in various sources (e.g., L. Stryer, 1988, Biochemistry, 3.sup.rd Edition, W.H.5 Freeman and Co., NY). Degenerate variants are also of use in the methods disclosed herein. Additional nucleic acid molecules encoding ANG, a precursor, variant, or fragment thereof, or encoding a tRNA fragment, can readily be produced using the amino acid sequences provided herein and the genetic code. Nucleic acid sequences encoding ANG, a precursor, variant or fragment thereof, or encoding a tRNA fragment, can be prepared by any suitable method including, for example, cloning of appropriate sequences or by direct chemical synthesis by methods such as the phosphotriester method of Narang et al., Meth. Enzymol.68:90-99, 1979; the phosphodiester method of Brown et al., Meth. Enzymol.68:109-151, 1979; the diethylphosphoramidite method of Beaucage et al., Tetra. Lett.22:1859-1862, 1981; the solid phase phosphoramidite triester method described by Beaucage & Caruthers, Tetra. Letts.22(20):1859-1862, 1981, for example, using an automated synthesizer as described in, for example, Needham-VanDevanter et al., Nucl. Acids Res.12:6159-6168, 1984 and the solid support method of U.S. Patent No.4,458,066. Chemical synthesis produces a single-strand (ss) oligonucleotide, which can be converted into double-strand (ds) DNA by hybridization with a complementary sequence or by polymerization with a DNA polymerase using the single strand as a template. Exemplary nucleic acids that include sequences encoding ANG, a precursor, variant, or fragment thereof, or encoding a tRNA fragment, can be prepared by cloning. A nucleic acid molecule encoding ANG, a precursor, variant, or fragment thereof, or encoding a tRNA fragment, can be cloned or amplified by in vitro methods, such as the polymerase chain reaction (PCR), the ligase chain reaction (LCR), the transcription-based amplification system (TAS), the self- sustained sequence replication system (3SR), and the Qβ replicase amplification system (QB). For example, a polynucleotide encoding ANG, a precursor, variant, or fragment thereof, or encoding a tRNA fragment, can be isolated by a polymerase chain reaction of cDNA using primers based on the DNA sequence of the molecule. A wide variety of cloning and in vitro amplification methodologies can be used. PCR methods are described in, for example, U.S. Patent No.4,683,195; Mullis et al., Cold Spring Harbor Symp. Quant. Biol.51:263, 1987; and Erlich, ed., PCR Technology, (Stockton Press, NY, 1989). Polynucleotides also canbe isolated by screening genomic or cDNA libraries with probes selected from the sequences of the desired polynucleotide under stringent hybridization Typically, a polynucleotide sequence encoding ANG, a precursor, variant, or fragment thereof, or encoding a tRNA fragment, is operably linked to transcriptional control sequences including, for example a promoter and a polyadenylation signal. Any promoter can be used that is a polynucleotide sequence recognized by the transcriptional machinery of the host cell (or introduced synthetic machinery) that is involved in the initiation of transcription. A polyadenylation signal is a polynucleotide sequence that directs the addition of a series of nucleotides on the end of the mRNA transcript for proper processing and trafficking of the transcript out of the nucleus into the cytoplasm for translation. Exemplary promoters include viral promoters, such as cytomegalovirus immediate early gene promoter (“CMV”), herpes simplex virus thymidine kinase (“tk”), SV40 early transcription unit, polyoma, retroviruses, papilloma virus, hepatitis B virus, and human and simian immunodeficiency viruses. Other promoters include promoters isolated from mammalian genes, such as the immunoglobulin heavy chain, immunoglobulin light chain, T cell receptor, HLA DQ α and DQ β, β-interferon, interleukin-2, interleukin-2 receptor, MHC class II, HLA-DRα, β-actin, muscle creatine kinase, prealbumin (transthyretin), elastase I, metallothionein, collagenase, albumin, fetoprotein, β-globin, c-fos, c-HA-ras, neural cell adhesion molecule (NCAM), α1-antitrypsin, H2B (TH2B) histone, type I collagen, glucose-regulated proteins (GRP94 and GRP78), rat growth hormone, human serum amyloid A (SAA), troponin I (TNI), platelet-derived growth factor, and dystrophin, as well as promoters specific for retinal pigment epithelial cells, such as a RPE65, BEST1, DCT, TYR, or TYRP1 promoter, see Nicoletti et al., Invests Ophthalmol. Vis. Sci.1998 Mar;39(3):637-44; Esumi et al., Hum. Mol. Gen.18: 128-141, 2009; Takeda et al., Biochem. Biophys. Res. Comm.300: 908-914, 2003; Murisier et al., Dev. Biol.303: 838-847, 2007; and Beermann, Cell. Mol. Biol. (Noisy-le-grand) 45(7):961-8, 1999. The promoter can be either inducible or constitutive. An inducible promoter is a promoter that is inactive or exhibits low activity except in the presence of an inducer substance. Additional examples of promoters include, but are not limited to, MT II, MMTV, collagenase, stromelysin, SV40, murine MX gene, α-2-macroglobulin, MHC class I gene h-2kb, HSP70, proliferin, tetracycline inducible, tumor necrosis factor, or thyroid stimulating hormone gene promoter. One example of an inducible promoter is the interferon inducible ISG54 promoter. In some aspects, the promoter is a constitutive promoter that results in high levels of transcription upon introduction into a host cell in the absence of additional factors. In more aspects, the constitutive promoter is a human β-actin, human elongation factor-1α, chicken β-actin combined with cytomegalovirus early enhancer, cytomegalovirus (CMV), simian virus 40, or a herpes simplex virus thymidine kinase promoter (see Damdindorj et al., PLOS One 9(8): e106472, 2014). The promoter can be a human β-actin promoter, human elongation factor-1α promoter, β-actin promoter, simian virus 40 promoter, or a herpes simplex virus thymidine kinase promoter.Optionally, transcription control include one or more enhancer elements, which are binding recognition sites for one or more factors that increase transcription above that observed for the minimal promoter alone, and also be operably linked to the polynucleotide encoding the nucleic acid molecule encoding ANG, a precursor, variant, or fragment, or encoding a tRNA fragment. Introns can also be included that help stabilize mRNA and increase expression. A polyadenylation signal can be included to effect proper termination and polyadenylation of the transcript. Exemplary polyadenylation signals have been isolated from beta globin, bovine growth hormone, SV40, and the herpes simplex virus thymidine kinase genes. A nucleic acid molecule encoding ANG, a precursor, variant, or fragment thereof, or encoding a tRNA fragment can be included in a viral vector, for example for expression of the protomer to produce the corresponding protein, variant or fragment thereof, or encoding a tRNA fragment in a host cell, or for administration to a subject as disclosed herein. Typically, such viral vectors include a nucleic acid molecule encoding ANG, a precursor, variant or fragment thereof, or encoding a tRNA fragment. In some examples, the viral vector encoding ANG, a precursor, variant, or fragment, or encoding a tRNA fragment can be replication-competent. For example, the viral vector can have a mutation (e.g., insertion of nucleic acid encoding the protomer) in the viral genome that attenuates, but does not completely block viral replication in host cells. Various viral vectors which can be utilized for nucleic acid based therapy as taught herein include adenovirus or adeno-associated virus (AAV), herpes virus, vaccinia, or an RNA virus such as a retrovirus (including HVJ, see Kotani et al., Curr. Gene Ther.4:183-194, 2004). In one aspect, the retroviral vector is a derivative of a murine or avian retrovirus, or a human or primate lentivirus. Examples of retroviral vectors in which a foreign gene can be inserted include, but are not limited to: Moloney murine leukemia virus (MoMLV), Harvey murine sarcoma virus (HaMuSV), murine mammary tumor virus (MuMTV), and Rous Sarcoma Virus (RSV). In one aspect, when the subject is a human, a vector such as the gibbon ape leukemia virus (GaLV) can be utilized. A pseudotyped retroviral vector can be utilized that includes a heterologous envelope gene. In one example the viral vector is AAV. Some retroviral vectors can incorporate multiple genes. These vectors can transfer or incorporate a gene for a selectable marker so that transduced cells can be identified and generated. By inserting a nucleic acid encoding ANG, a precursor, variant, or fragment thereof, or encoding a tRNA fragment into the viral vector, along with another gene which can serve as viral envelope protein and also can encode the ligand for a receptor on a specific target cell, for example, the vector is now target specific. Retroviral vectors can be made target specific by modifications of the envelope protein by attaching, for example, a sugar, a glycolipid, or a protein. In one specific, non-limiting example, targeting is accomplished by using an antibody to target the retroviral vector. Since recombinant retroviruses are non-replicating by design, they require assistance in order to produce infectious vector particles. This assistance can be provided, for example, by using helper cell lines that contain plasmids encoding all of the structural genes of the retrovirus under the control of regulatorysequences within the long terminal repeat (LTR). These plasmids are missing a nucleotide sequence which enables the packaging mechanism to recognize an transcript for encapsidation. Helper cell lines which have deletions of the packaging signal include, but are not limited to ψ2, PA317, and PA12, for example. These cell lines produce empty virions, since no genome is packaged. If a retroviral vector is introduced into such cells in which the packaging signal is intact, but the structural genes are replaced by other genes of interest, the vector can be packaged and vector virion produced. Alternatively, NIH 3T3 or other tissue culture cells can be directly transfected with plasmids encoding the retroviral structural genes gag, pol and env, by conventional transfection methods. These cells are then transfected with the vector plasmid containing the genes of interest. The resulting cells release the retroviral vector into the culture medium. The adenovirus vectors include replication competent, replication deficient, gutless forms thereof. Defective viruses, such as adenovirus vectors or adeno-associated virus (AAV) vectors, that entirely or almost entirely lack viral genes, can be used. Use of defective viral vectors allows for administration to specific cells without concern that the vector can infect other cells. The AAV vectors of use are replication deficient. In some non-limiting examples, a vector of use is an attenuated adenovirus vector, such as the vector described by Stratford-Perricaudet et al. (J. Clin. Invest., 90:626-6301992; La Salle et al., Science 259:988-990, 1993); or a defective AAV vector (Samulski et al., J. Virol., 61:3096-3101, 1987; Samulski et al., J. Virol., 63:3822-3828, 1989; Lebkowski et al., Mol. Cell. Biol., 8:3988-3996, 1988). Recombinant AAV vectorsey are capable of directing the expression and the production of the selected transgenic products in targeted cells. Thus, the recombinant vectors can include at least all of the sequences of AAV essential for encapsidation and the physical structures for infection of target cells. AAV belongs to the family Parvoviridae and the genus Dependovirus. AAV is a small, non- enveloped virus that packages a linear, single-stranded DNA genome. Both sense and antisense strands of AAV DNA are packaged into AAV capsids with equal frequency. In some aspects, the AAV DNA includes a nucleic acid including a promoter operably linked to a nucleic acid molecule encoding ANG, a precursor, variant, or fragment thereof, or encoding a tRNA fragment. Further provided are recombinant vectors, such as recombinant adenovirus vectors and recombinant adeno-associated virus (rAAV) vectors comprising a nucleic acid molecule(s) disclosed herein. In some aspects, the AAV is rAAV8, and / or AAV2. However, the AAV serotype can be any other suitable AAV serotype, such as AAV1, AAV2, AAV3, AAV4, AAV5, AAV6, AAV7, AAV9, AAV10, AAV11 or AAV12, or a hybrid of two or more AAV serotypes. An exemplary AAV8 vector is disclosed, for example, in PCT Publication No. WO 2014 / 127196. Gene therapy vectors that utilize AAV can infect both dividing and quiescent cells and persist in an extrachromosomal state without integrating into the genome of the host cell. The present disclosure contemplates the use of an rAAV for the methods disclosed herein. AAV including has the ability to bind and enter target cells, enter the nucleus, the ability to be expressed in the nucleus for a prolonged period of time, and low toxicity. AAV can be used to transfect cells, and suitable vector are known i, see for example, U.S. Published Patent Application No.2014 / 0037585, incorporated herein by reference. Methods for producing rAAV suitable for gene therapy are known (see, for example, U.S. Published Patent Nos.2012 / 0100606; 2012 / 0135515; 2011 / 0229971; and 2013 / 0072548; and Ghosh et al., Gene Ther 13(4):321-329, 2006), and can be utilized with the methods disclosed herein. In some aspects, the vector is a rAAV8 vector, a rAAV2 vector, a rAAV9 vector. In a specific non- limiting example, the vector is an AAV8 vector. AAV8 vectors are disclosed, for example, in U.S. Patent No.8,692,332, which is incorporated by reference herein. The location and sequence of the capsid, rep 68 / 78, rep 40 / 52, VP1, VP2 and VP3 are disclosed in this U.S. Patent No.8,692,332. The location and hypervariable regions of AAV8 are also provided. In some aspects, the vector is an AAV2 variant vector, such as AAV7m8. The vectors of use in the methods disclosed herein can contain nucleic acid sequences encoding an intact AAV capsid which may be from a single AAV serotype (e.g., AAV2, AAV6, AAV8 or AAV9). As disclosed in U.S. Patent No.8,692,332, vectors of use can also be recombinant, and thus can contain sequences encoding artificial capsids which contain one or more fragments of the AAV8 capsid fused to heterologous AAV or non-AAV capsid proteins (or fragments thereof). These artificial capsid proteins are selected from non-contiguous portions of the AAV2, AAV6, AAV8 or AAV9 capsid or from capsids of other AAV serotypes. For example, a AAV vector may have a capsid protein comprising one or more of the AAV8 capsid regions selected from the VP2 and / or VP3, or from VP1, or fragments thereof selected from amino acids 1 to 184, amino acids 199 to 259; amino acids 274 to 446; amino acids 603 to 659; amino acids 670 to 706; amino acids 724 to 738 of the AAV8 capsid, which is presented as SEQ ID NO: 2 in U.S. Patent No.8,692,332. In another example, it may be desirable to alter the start codon of the VP3 protein to GTG. Alternatively, the AAV may contain one or more of the AAV serotype 8 capsid protein hypervariable regions, for example aa 185- 198; aa 260-273; aa447-477; aa495-602; aa660-669; and aa707-723 of the AAV8 capsid which is presented as SEQ ID NO: 2 in U.S. Patent No.8,692,332. Additional viral vectors that can be used for expression of ANG, a precursor, variant, or fragment, or encoding a tRNA fragment, include polyoma, i.e., SV40 (Madzak et al., 1992, J. Gen. Virol., 73:15331536), herpes viruses including HSV and EBV and CMV (Margolskee, 1992, Curr. Top. Microbiol. Immunol., 158:67-90; Johnson et al., 1992, J. Virol., 66:29522965; Fink et al., 1992, Hum. Gene Ther.3:11-19; Breakfield et al., 1987, Mol. Neurobiol., 1:337-371; Fresse et al., 1990, Biochem. Pharmacol., 40:2189- 2199), Sindbis viruses (H. Herweijer et al., 1995, Human Gene Therapy 6:1161-1167; U.S. Pat. Nos. 5,091,309 and 5,2217,879), alphaviruses (S. Schlesinger, 1993, Trends Biotechnol.11:18-22; I. Frolov et al., 1996, Proc. Natl. Acad. Sci. USA 93:11371-11377) and retroviruses of avian (Brandyopadhyay et al., 1984, Mol. Cell Biol., 4:749-754; Petropouplos et al., 1992, J. Virol., 66:3391-3397), murine (Miller, 1992, Curr. Top. Microbiol. Immunol., 158:1-24; Miller et al., 1985, Mol. Cell Biol., 5:431-437; Sorge et al., 1984, Mol. Cell Biol., 4:1730-1737; Mann et al., 1985, J. Virol., 54:401-407), and human origin (Page et al., 1990, J. Virol., 64:5370-5276; Buchschalcher et al., 1992, J. Virol., 66:2731-2739). Baculovirus (Autographa californica multinuclear polyhedrosis virus; AcMNPV) vectors.Another targeted delivery system for a encoding ANG, a precursor, variant, or fragment thereof, or encoding a tRNA fragment is a dispersion system. These systems are also of use in the disclosed methods. Colloidal dispersion systems include macromolecule complexes, nanocapsules, microspheres, beads, and lipid-based systems including oil-in-water emulsions, micelles, mixed micelles, and liposomes. One colloidal dispersion system is a liposome. Liposomes are artificial membrane vesicles which are useful as delivery vehicles in vitro and in vivo. It has been shown that large unilamellar vesicles (LUV), which range in size from about 0.2-4 microns, can encapsulate a substantial percentage of an aqueous buffer containing large macromolecules. RNA, DNA and intact virions can be encapsulated within the aqueous interior and be delivered to cells in a biologically active form (Fraley et al., Trends Biochem. Sci.6:77, 1981). In addition to mammalian cells, liposomes have been used for delivery of polynucleotides in plant, yeast and bacterial cells. In order for a liposome to be an efficient gene transfer vehicle, the following characteristics should be present: (1) encapsulation of the nucleic acid of interest at high efficiency while not compromising their biological activity; (2) preferential and substantial binding to a target cell in comparison to non-target cells; (3) delivery of the aqueous contents of the vesicle to the target cell cytoplasm at high efficiency; and (4) accurate and effective expression of genetic information (Mannino et al., Biotechniques 6:682, 1988). The composition of the liposome is usually a combination of phospholipids, particularly high-phase- transition-temperature phospholipids, usually in combination with steroids, especially cholesterol. Other phospholipids or other lipids may also be used. The physical characteristics of liposomes depend on pH, ionic strength, and the presence of divalent cations. Examples of lipids useful in liposome production include phosphatidyl compounds, such as phosphatidylglycerol, phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine, sphingolipids, cerebrosides, and gangliosides. Particularly useful are diacylphosphatidyl-glycerols, where the lipid moiety contains from 14-18 carbon atoms, particularly from 16-18 carbon atoms, and is saturated. Illustrative phospholipids include, for example, phosphatidylcholine, dipalmitoylphosphatidylcholine and distearoylphosphatidylcholine. The targeting of liposomes can be classified based on anatomical and mechanistic factors. Anatomical classification is based on the level of selectivity, for example, organ-specific, cell-specific, and organelle-specific. Mechanistic targeting can be distinguished based upon whether it is passive or active. Passive targeting utilizes the natural tendency of liposomes to distribute to cells of the reticuloendothelial system (RES) in organs which contain sinusoidal capillaries. Active targeting, on the other hand, involves alteration of the liposome by coupling the liposome to a specific ligand such as a monoclonal antibody, sugar, glycolipid, or protein, or by changing the composition or size of the liposome in order to achieve targeting to organs and cell types other than the naturally occurring sites of localization. Another targeting delivery system is the use of biodegradable and biocompatible polymer scaffolds (see Jang et al., Expert Rev. Medical Devices 1:127-138, 2004) for use in the bone. These scaffolds usually contain a mixtures of one or more biodegradable polymers, for example and without limitation, saturatedaliphatic polyesters, such as poly(lactic acid) (glycolic acid), or poly(lactic-co-glycolide) (PLGA) copolymers, unsaturated linear as polypropylene fumarate (PPF), or microorganism produced aliphatic polyesters, such as polyhydroxyalkanoates (PHA), (see Rezwan et al., Biomaterials 27:3413-3431, 2006; Laurencin et al., Clin. Orthopaed. Rel. Res.447:221-236). By varying the proportion of the various components, polymeric scaffolds of different mechanical properties are obtained. An exemplary scaffold contains a ratio of PLA to PGA is 75:25, but this ratio may change depending upon the specific application. Other exemplary scaffolds include surface bioeroding polymers, such as poly(anhydrides), such as trimellitylimidoglycine (TMA-gly) or pyromellitylimidoalanine (PMA-ala), or poly(phosphazenes), such as high molecular weight poly(organophasphazenes) (P[PHOS]), and bioactive ceramics. The gradual biodegradation of these scaffolds allows the gradual release of drugs or gene from the scaffold. Thus, these polymeric carriers represent not only a scaffold but also a drug or gene delivery system. This system is applicable to the delivery of plasmid DNA and also applicable to viral vectors, such as AAV or retroviral vectors, as well as transposon-based vectors. The disclosed nucleic acid molecules can be included in a nanodispersion system, see, e.g., U.S. Pat. No.6,780,324; U.S. Pat. Publication No.2009 / 0175953. For example, a nanodispersion system includes a biologically active agent and a dispersing agent (such as a polymer, copolymer, or low molecular weight surfactant). Exemplary polymers or copolymers include polyvinylpyrrolidone (PVP), poly(D,L-lactic acid) (PLA), poly(D,L-lactic-co-glycolic acid (PLGA), poly(ethylene glycol). Exemplary low molecular weight surfactants include sodium dodecyl sulfate, hexadecyl pyridinium chloride, polysorbates, sorbitans, poly(oxyethylene) alkyl ethers, poly(oxyethylene) alkyl esters, and combinations thereof. In one example, the nanodispersion system includes PVP and ODP or a variant thereof (such as 80 / 20 w / w). In some examples, the nanodispersion is prepared using the solvent evaporation method, see for example, Kanaze et al., Drug Dev. Indus. Pharm.36:292-301, 2010; Kanaze et al., J. Appl. Polymer Sci.102:460-471, 2006. Dendrimers are synthetic three-dimensional macromolecules that are prepared in a step-wise fashion from simple branched monomer units, the nature and functionality of which can be easily controlled and varied. Dendrimers consist of an initiator core, surrounded by a layer of a selected polymer that is grafted to the core, forming a branched macromolecular complex. Dendrimers are typically produced using polymers such as poly(amidoamine) or poly(L-lysine). A dendrimer can be synthesized from the repeated addition of building blocks to a multifunctional core (divergent approach to synthesis), or towards a multifunctional core (convergent approach to synthesis) and each addition of a three-dimensional shell of building blocks leads to the formation of a higher generation of the dendrimers. Polypropylenimine dendrimers contain 100% protonable nitrogens and up to 64 terminal amino groups. Protonable groups are usually amine groups which are able to accept protons at neutral pH. For nucleic acid molecules, dendrimers can be formed from polyamidoamine and phosphorous containing compounds with a mixture of amine / amide or N- P(O2)S as the conjugating units. Dendrimers of use for delivery of nucleic acid molecules is disclosed, for example, in PCT Publication No.2003 / 033027, incorporated herein by reference.The surface of the targeted delivery be modified in a variety of ways. In the case of a liposomal targeted delivery system, lipid groups can incorporated into the lipid bilayer of the liposome in order to maintain the targeting ligand in stable association with the liposomal bilayer. Various linking groups can be used for joining the lipid chains to the targeting ligand. In another aspect, an mRNA can be used to deliver a nucleic acid encoding ANG, a precursor, variant, or fragment thereof, directly into cells. In further aspects, a tRNA fragment is delivered. In some aspects, nucleic acid-based vaccines based on mRNA may provide a potent alternative to the previously mentioned approaches. mRNA delivery precludes safety concerns about DNA integration into the host genome and can be directly translated in the host cell cytoplasm. Moreover, the simple cell-free, in vitro synthesis of RNA avoids the manufacturing complications associated with viral vectors. Two exemplary forms of RNA that can be used to deliver a nucleic acid include conventional non-amplifying mRNA (see, e.g., Petsch et al., “Protective efficacy of in vitro synthesized, specific mRNA vaccines against influenza A virus infection,” Nature biotechnology, 30(12):1210–6, 2012) and self-amplifying mRNA (see, e.g., Geall et al., “Nonviral delivery of self-amplifying RNA vaccines,” PNAS, 109(36): 14604-14609, 2012; Magini et al., “Self-Amplifying mRNA Vaccines Expressing Multiple Conserved Influenza Antigens Confer Protection against Homologous and Heterosubtypic Viral Challenge,” PLoS One, 11(8):e0161193, 2016; and Brito et al., “Self-amplifying mRNA vaccines,” Adv Genet., 89:179-233, 2015). 3. CRISR / Cas9 Included are in the present disclosure are methods for site-specific modification of a nucleic acid molecule in a cell to introduce ANG or another molecule that increases ANG activity, such as one or more tRNA fragments. These modifications can include, but are not limited to, site-specific insertions, and replacements of nucleotides (a “knock-in”), such that an increase in ANG activity is produced. These modifications can be made anywhere within the genome, for example, in genomic elements, including, among others, coding sequences, regulatory elements, and non-coding DNA sequences. However, in some aspects, an insertion is made into a safe harbor locus (see Pavani and Amendola, Front Genome Ed., https: / / doi.org / 10.3389 / fgeed.2020.609650, 20 January 2021). Any number of such insertions can be made, in any order or combination. Such methods may be used to modify expression of a gene, such as to increase expression of ANG or a tRNA fragment. These modifications include a “knock-in” of a nucleic acid molecule encoding ANG and one or more tRNA fragments. Techniques for making such modifications by genome editing include, for example, use of CRISPR-Cas systems, zinc-finger nucleases (ZFNs), and transcription activator-like effector nucleases (TALENs), among others. These modifications can be used to introduce (knock-in) a nucleic acid molecule encoding ANG, a precursor, variant, or fragment into a safe harbor locus in a genome. These modifications can be used to introduce (knock-in) a nucleic acid molecule encoding a tRNA fragment into a safe harbor locus in the genome. Cas9 mediated integration of genes is disclosed, for example, in Li et al., G3 10(2):467-473. doi: 10.1534 / g3.119.400810 (2020) and Jacinto et al., J Cell Mol Med.24:3766–3778, DOI:10.1111 / jcmm.14916 (2020). A typical set of CRISPR system is two components, a CRISPR-associated nuclease 9 (Cas9) and one or more guide RNAs (gRNAs), each of which contains a CRISPR RNA (crRNA) and a trans-activating CRISPR RNA (tracrRNA). Simple gene disruptions can be generated by cleavage of the target site, followed by alteration of nucleic acids, such as a deletion, and repair by the non-homologous- end-joining pathway (NHEJ). Target recognition by crRNAs occurs through complementary base pairing with target DNA, which directs cleavage of foreign sequences by means of Cas proteins. In some aspects, DNA recognition by guide RNA and consequent cleavage by the endonuclease requires complementary base-pairing with a protospacer adjacent motif (PAM) (e.g., 5’-NGG-3’) and with a protospacer region in the target. (Jinek et. al., Science.337:816-821, 2012). The PAM motif recognized by a Cas9 varies for different Cas9 proteins. Any Cas9 protein can be used in the systems and methods disclosed herein, including mutant Cas9 proteins (such as those having an R691A, D10A, H840A, or combination of such substitutions). In other aspects of the systems and methods disclosed herein, a promoter, is operably linked to the nucleic acid encoding Cas9. In one non-limiting example, a retinal pigment epithelial cell promoter is utilized, such as, but not limited to, RPE65, BEST1, DCT, TYR, or a TYRP1 promoter. As noted above, the Cas9 RNA guide system includes a mature crRNA that is base-paired to trans- activating crRNA (tracrRNA), forming a two-RNA structure that directs Cas9 to the locus of a desired double-stranded (ds) break in target DNA. In some aspects base-paired tracrRNA:crRNA combination is engineered as a single RNA chimera to produce a guide sequence (e.g., gRNA) which preserves the ability to direct sequence-specific Cas9 dsDNA cleavage. In some aspects, the Cas9-guide sequence complex results in cleavage of one or both strands at a target sequence within a safe harbor locus, which allows a knock in. Thus, the Cas9 endonuclease and the gRNA molecules are used sequence-specific target recognition, cleavage, and genome editing of the safe harbor locus. In one aspect, the cleavage site is at a specific nucleotide, such as, but not limited to the 16, 17, or 18thnucleotide (nt) of a 20-nt target. In one non-limiting example, the cleavage site is at the 17thnucleotide of a 20-nt target sequence. The cleavage can be a double stranded cleavage. In some aspects, the gRNA molecule is selected so that the target genomic targets bear a protospacer adjacent motif (PAM). In some aspects, DNA recognition by guide RNA and consequent cleavage by the endonuclease requires the presence of a protospacer adjacent motif (PAM) (e.g., 5’-NGG-3’) in immediately after the target. The PAM is present in the targeted nucleic acid sequence but not in the crRNA that is produced to target it. In some aspects, the proto-spacer adjacent motif (PAM) corresponds to 2 to 5 nucleotides starting immediately or in the vicinity of the proto-spacer at the leader distal end. The PAM motif also can be NNAGAA, NAG, NGGNG, AWG, CC, CC, CCN, TCN, or TTC. In some aspects, cleavage occurs at a site about 3 base-pairs upstream from the PAM. In some aspects, the Cas9 nuclease cleaves a double stranded nucleic acid sequence. In some aspects, the guide sequence is selected to reduce the degree of secondary structure within the sequence. Secondary structure may be determined by any suitable polynucleotide folding algorithm.Some programs are based on calculating the minimal Gibbs free energy. An example of one such algorithm is mFold (Zuker and Stiegler, Nucleic Acids , 133-148). Another example folding algorithm is the online webserver RNAfold, which uses the centroid structure prediction algorithm (see e.g., Gruber et al., 2008, Cell 106(1): 23-24; and Can and Church, 2009, Nature Biotechnology 27(12): 1151-62). Guide sequences can be designed using the MIT CRISPR design tool found at crispr.mit.edu, Harvard and University of Bergen CHOPCHOP web tool found at chopchop.cbu.uib.no, or the E-CRISP tool found at www.e-crisp.org / E-CRISP. Additional tools for designing tracrRNA and guide sequences are described in Naito et al., Bioinformatics.2014 Nov 20, and Ma et al. BioMed Research International, Volume 2013 (2013), Article ID 270805. The crRNA can be 18-48 nucleotides in length. The crRNA can be 18, 19, 20, 21, 22, 23, 24 or 25 nucleotides in length. In one example, the crRNA is 20 nucleotides in length. The system disclosed herein introduces double stranded DNA breaks, such that the target, e.g., the safe harbor locus, is cleaved by Cas9. This allows insertion of a nucleic acid sequence encoding ANG, a precursor, variant, or fragment, and / or encoding a tRNA fragment. In some aspects, more than one DNA break can be introduced by using more than one gRNA. For example, two gRNAs can be utilized, such that two breaks are achieved. When two or more gRNAs are used to position two or more cleavage events, in a target nucleic acid, it is contemplated that in an aspect the two or more cleavage events may be made by the same or different Cas9 proteins. For example, when two gRNAs are used to position two double strand breaks, a single Cas9 nuclease may be used to create both double strand breaks. In some aspects, the disclosed methods include the use of one or more vectors comprising: a) a retinal specific promoter operably linked to a nucleotide sequence encoding a Type II Cas9 nuclease, b) a promoter, such as a U6 promoter, operably linked to one or more nucleotide sequences encoding one or more CRISPR-Cas guide RNAs that hybridize with a safe harbor locus in a target cell, such as a human cell; and c) a nucleic acid molecule encoding ANG, a precursor, variant, or fragment, and / or encoding a tRNA fragment that is introduced into the target cell. These components can be located on same or different vectors, whereby the one or more guide RNAs target the noncoding region, such that the Cas9 protein cleaves the DNA and the nucleic acid molecule encoding ANG, a precursor, variant, or fragment, or encoding a tRNA fragment, is introduced. In specific non-limiting examples, the one or more vectors are viral vectors such as lentiviral vectors. In other non-limiting examples, the viral vectors are adenovirus vectors, adeno-associated virus vectors, or retroviral vectors. Without limitation, Cas9 and gRNAs can be delivered to the using AAV, a lentivirus, piggybac, an episomal constructs, or injected as purified nanoparticles constituted by pure Cas9 protein and pure guides RNAs (see, for example, Steyer et al., Drug Discov Today Technol 28: 3-12, 2018). 4. Chemical Compounds Agents that increase ANG activity include L-minosine (Janjic et al., BMC Oral Health 17: 87 (7 pages), DOI 10.1186 / s12903-017-0373-6, 2017), muscone (Zhou et al., Mol. Neurol.59: 5891-5901, July 9,2022), opioids, DMOG and ML228. Agents that increase ANG activity include molecules that are identified from large libraries of both natural product or (or semi-synthetic) extracts or chemical libraries. Screening methods that detect increases in ANG activity are useful for identifying compounds from a variety of sources for activity. The initial screens may be performed using a diverse library of compounds, a variety of other compounds and compound libraries. Thus, molecules that increase the activity of ANG can be identified. These small molecules can be identified from combinatorial libraries, natural product libraries, or other small molecule libraries. In addition, ANG agonists can be identified as compounds from commercial sources, as well as commercially available analogs of identified agonists. The precise source of test extracts or compounds is not critical to the identification of agents that increase ANG activity. Accordingly, such agents can be identified from virtually any number of chemical extracts or compounds. Examples of such extracts or compounds include, but are not limited to, plant-, fungal-, prokaryotic- or animal-based extracts, fermentation broths, and synthetic compounds, as well as modification of existing compounds. Numerous methods are also available for generating random or directed synthesis (e.g., semi-synthesis or total synthesis) of any number of chemical compounds, including, but not limited to, saccharide-, lipid-, peptide-, and nucleic acid-based compounds. Synthetic compound libraries are commercially available from Brandon Associates (Merrimack, N.H.) and Aldrich Chemical (Milwaukee, Wis.). ANG protein agonists can be identified from synthetic compound libraries that are commercially available from a number of companies including Maybridge Chemical Co. (Trevillet, Cornwall, UK), Comgenex (Princeton, N. J.), Brandon Associates (Merrimack, N.H.), and Microsource (New Milford, Conn.). La protein agonists can be identified from a rare chemical library, such as the library that is available from Aldrich (Milwaukee, Wis.). La protein agonists can be identified in libraries of natural compounds in the form of bacterial, fungal, plant, and animal extracts are commercially available from a number of sources, including Biotics (Sussex, UK), Xenova (Slough, UK), Harbor Branch Oceangraphics Institute (Ft. Pierce, Fla.), and PharmaMar, U.S.A. (Cambridge, Mass.). Natural and synthetically produced libraries and compounds are readily modified through conventional chemical, physical, and biochemical means. Useful compounds may be found within numerous chemical classes, though typically they are organic compounds, including small organic compounds. Small organic compounds have a molecular weight of more than 50 yet less than about 2,500 daltons, such as less than about 750 or less than about 350 daltons can be utilized in the methods disclosed herein. Exemplary classes include heterocycles, peptides, saccharides, steroids, and the like. The compounds may be modified to enhance efficacy, stability, pharmaceutical compatibility, and the like. III. Methods of Treatment and Pharmaceutical Compositions Methods are disclosed herein for treating, or reducing the risk of developing, AMD. In some aspects, the methods inhibit drusen formation. The disclosed agents can administered systemically (for example by peripheral vein infusion or orally) and may be administered locally or regionally (intraocularadministration). The agent can be an agent that inhibits HERV-K. The agent can be an agent that increases ANG activity. The subject can be at the early, or advanced stages of AMD. In some examples the subject is a mammalian subject, such as a human or veterinary subject. In some aspects, the subject has wet AMD. In other aspects, the subject has dry AMD. In further aspects, the subject is at risk of developing AMD. In some aspects, the disclosed methods reduce or arrest loss of vision. Anti-retroviral agents can be administered according to approved dosing methods, see above. Chemical compounds that increase ANG activity can be administered to the subject. In some aspects, administration is systemic, such as oral or intravenous. However, other routes of administration are contemplated, such as inhalation, vaginal, rectal and intranasal are of use. In some aspects, an anti-retroviral agent is formulated for local administration, such as to the eye. Therapeutic compounds can be prepared for storage by mixing a polypeptide(s) having the desired degree of purity, such as ANG, a precursor, variant, or fragment thereof, an antibody, or another agent, such as an inhibitory nucleic acid molecule or a CRISPR / Cas13 system, a nucleic acid molecule encoding ANG, a precursor, variant, or fragment thereof, or a CRISPR / Cas9 system, with optional pharmaceutically acceptable carriers, excipients or stabilizers (Remington's Pharmaceutical Sciences 16th edition, Osol, A. Ed.

[1980] ), in the form of lyophilized formulations or aqueous solutions. Acceptable carriers, excipients, or stabilizers are nontoxic to recipients at the dosages and concentrations employed, and include buffers such as phosphate, citrate, and other organic acids; antioxidants including ascorbic acid and methionine; preservatives (such as octadecyldimethylbenzyl ammonium chloride; hexamethonium chloride; benzalkonium chloride, benzethonium chloride; phenol, butyl or benzyl alcohol; alkyl parabens such as methyl or propyl paraben; catechol; resorcinol; cyclohexanol; 3-pentanol; and m-cresol); low molecular weight (less than about 10 residues) polypeptides; proteins, such as serum albumin, gelatin, or immunoglobulins; hydrophilic polymers such as polyvinylpyrrolidone; amino acids such as glycine, glutamine, asparagine, histidine, arginine, or lysine; monosaccharides, disaccharides, and other carbohydrates including glucose, mannose, or dextrins; chelating agents such as EDTA; sugars such as sucrose, mannitol, trehalose or sorbitol; salt-forming counter-ions such as sodium; metal complexes (e.g., Zn-protein complexes); and / or non-ionic surfactants such as TWEEN™, PLURONICS™ or polyethylene glycol (PEG). The pharmaceutical composition can be formulated for local delivery, such as to the eye. In one aspect, the pharmaceutical composition is formulated as an eye drop. The active ingredients can be entrapped in microcapsules prepared, for example, by coacervation techniques or by interfacial polymerization, for example, hydroxymethylcellulose or gelatin-microcapsules and poly-(methylmethacylate) microcapsules, respectively, in colloidal drug delivery systems (for example, liposomes, albumin microspheres, microemulsions, nano-particles and nanocapsules) or in macroemulsions. Such techniques are disclosed in Remington's Pharmaceutical Sciences 16th edition, Osol, A. Ed. (1980). The formulations to be used for in vivo administration can be sterile. This is readily accomplished by filtration through sterile filtration membranes. Sustained-release preparations may be prepared. In someaspects, such as for the delivery of nucleic acid antibody, or antigen binding fragment thereof to the subject, the agent is administered A pharmaceutical composition can be prepared, packaged, or sold in bulk, as a single unit dose, or as a plurality of single unit doses. As used herein, a “unit dose” is a discrete amount of the pharmaceutical composition comprising a predetermined amount of the active ingredient. The amount of the active ingredient is generally equal to the dosage of the active ingredient which would be administered to a subject or a convenient fraction of such a dosage such as, for example, one-half or one-third of such a dosage. The relative amounts of the active ingredient, the pharmaceutically acceptable carrier, and any additional ingredients in a pharmaceutical composition can vary, depending upon the identity, size, and condition of the subject treated and further depending upon the route by which the composition is to be administered. By way of example, the composition may include 0.1% to 100% (w / w) active ingredient. In addition to the principal active ingredients, the vehicles and compositions can include various formulatory ingredients, such as anti-microbial preservatives and tonicity agents. For example, antimicrobial preservatives include: benzalkonium chloride, thimerosal, chlorobutanol, methylparaben, propylparaben, phenylethyl alcohol, EDTA, sorbic acid, POLYQUAD® or other agents. Such preservatives, if employed, can be used in an amount from about 0.0001 wt. % to 1.0 wt. %. Suitable agents which may be used to adjust tonicity or osmolality of the compositions include: mannitol, dextrose, glycerine and propylene glycol. If used, such agents will be employed in an amount of about 0.1 wt. % to 10.0 wt. %. In some aspects, the composition does not include preservatives or tonicity agents which adversely affect or irritate the eye. Ophthalmic compositions are provided herein, such as eye drops, that include, in addition to the active ingredient(s), a preservative and optionally a viscosifier. The preservative can be, for example, benzalkonium chloride, benzethonium chloride, chlorhexidine gluconate, chlorobutanol, benzyl alcohol, sodium dehydroacetate, paraoxybenzote esters, sodium edetate, boric acid and the like. The viscosifier can be, for example, hydroxypropyl methyl cellulose (HPMC), or water-soluble cellulose derivatives such as methylcellulose, hydroxyethylcellulose, carboxymethylcellulose and the like. Other additives include, but are not limited to, e.g., isotonicity agents such as sodium chloride, potassium chloride, glycerol, mannitol, sorbitol, boric acid, glucose, propylene glycol and the like; buffering agents such as phosphate buffer, acetate buffer, borate buffer, carbonate buffer, citrate buffer, tris buffer, glutamic acid, Ɛ-aminocaproic acid and the like; stabilizers such as e.g., sodium bisulfite, sodium thiosulfate, sodium edetate, sodium citrate, ascorbic acid, dibutylhydroxytoluene and the like, thickeners such as sodium chondroitin sulfate, sodium hyaluronate, corboxyvinyl polymer, polyvinyl alcohol, polyvinylpyrrolidone, macrogol and the like, pH adjusters such as hydrochloric acid, sodium hydroxide, phosphoric acid, acetic acid, and the like. In particular aspects, the disclosed eye drops may further include one or more other ingredients or additives, which can be contained in artificial tears, i.e., aminoethylsulfonic acid, sodium chondroitin sulfate, potassium L-aspartate, magnesium L-aspartate, potassium magnesium L-aspartate (equimolar mixture),sodium hydrogen carbonate, sodium carbonate, chloride, calcium chloride, sodium chloride, sodium hydrogen phosphate, sodium dihydrogen potassium dihydrogen phosphate, exsiccated sodium carbonate, magnesium sulfate, polyvinylalcohol, polyvinylpyrrolidone, hydroxyethylcellulose, glucose and methylcellulose. While the amount of these additives varies depending on the kind, use and the like of the additive, such additives only need to be added at a concentration capable of achieving the object of the additive. In some aspects, eye drops are provided that include agent can be an agent that inhibits HERV-K and / or an agent that increases ANG activity. The pharmaceutical composition can include a preservative and / or a viscosifier. Optionally, other ingredients can be included. The concentrations of other ingredients or additives contained in a pharmaceutical composition formulated for ocular administration, such as eye drops, are generally, but without limitation, not less than 0.01% w / v, not less than 0.1% w / v, not less than 0.5% w / v, and not more than 20% w / v, such not more than 10% w / v, or not more than 7% w / v, or not more than 5% w / v. The ophthalmic compositions may be made as micronized suspensions in isotonic, pH adjusted sterile saline, or, preferably as solutions in isotonic, pH adjusted sterile saline. The pH of the compositions provided herein can vary across a range acceptable for the eye, as known to a person of ordinary skill in the art. Preferably, the pH of the formulations is within the range of approximately 4-8. Alternatively, the ophthalmic compositions can be formulated in an ointment such as petrolatum. In certain aspects, the ophthalmic formulations include lipophiliccally modified compositions and transplantable carriers. Ophthalmic compositions, formulated for topical ocular administration, can be eye drops, such as aqueous eye drops, for example, monophasic aqueous eye drops. Ophthalmic compositions also be formulated and used in the form of a mist, a frost, a foam, a cream, an ointment or an emulsion for direct application to the eye, or used in ocular implants or injectable ocular therapies or else administered to the eyelid or sclera. An ophthalmic composition can also include a compound such as a Nox4 inhibitor, a compound that modulates NF-kB, mTOR, or one or more Rho GTPases such as CDC42 and / or RACI; a compound that modulates AMPK or a compound that regulates RPE epithelial to mesenchymal transition or RPE dedifferentiation, cholesterol pathway modulators, complement inhibitors, epigenetic modifiers, mitochondrial activity inducers, oxidative stress inhibitors, and metabolic stress inhibitors. Examples of such compounds include, but are not limited to, aminocapropic acid, L-701,324, Vas2870, L-745,870 hydrochloride, Me3,4-dephostatin, N-Methyl- I-deoxynojirimycin, L-750,667 trihydrochloride, (+)-MK- 801 hydrogen maleate, Hemidine tartrate, (-)-Naproxen sodium, Raloxifene hydrochloride, SKF 83959 hydrobromide, L-687,384 hydrochloride, 7,7-Dimethyl-(5Z,8Z)-eicosadienoic acid, SP600125, Ro 41-0960, Ancitabine hydrochloride, Risperidone, Telenzepine dihydrochloride, NO-711 hydrochloride, U-99194A maleate, S(+)-Rac10pride L-tartrate, Pirenzepine dihydrochloride, Captopril, thioperamide maleate, alprenolol hydrochloride, Ritodrine hydrochloride, Putrescine dihydrochloride, 1-(2- Methoxyphenyl)piperazine hydrochloride, PAPP, U-69593, AG-1478, riluzole, Phentolamine mesylate,DBO-83, Formestane, Carbamazepine, 4-(2- benzenesulfonyl fluoride hydrochloride, Terbutaline hemisulfate, UK 14304, GR 113808, Acetylthiocholine chloride, spermidine, 5- (N-Methy1-N-isobuty1)amiloride, ATPO, Acadenisine or a combination thereof. See U.S. Published Patent Application No. US20220339127A1, incorporated herein by reference. The presently disclosed compositions and methods can be used in combination with a compound, or a pharmaceutically acceptable salt thereof, which inhibits Nox4 or reactive oxygen species formation, or modulates serine protease, a dopamine receptor, NF-kB, mTOR, AMPK, RPE epithelial to mesenchymal transition, RPE dedifferentiation, or one or more Rho GTPases. In some non-limiting examples, the compound is a Nox4 inhibitor or an inhibitor of reactive oxygen species formation. In other aspects, the compound modulates NF-kB, mTOR, or one or more Rho GTPases. In further aspects, the compound modulates one or more Rho GTPases, wherein the Rho GTPase is CDC42 and / or RACl. In yet other aspects, the compound inhibits serine protease. In more aspects, the compound regulates AMPK. In more aspects, the compound modulates a dopamine receptor. The compound can be a dopamine receptor D4 antagonist. In some aspects, the compound is the compound is Aminocapropic acid, L-701,324, Vas2870, L-745,870 hydrochloride, Me-3,4-dephostatin, N-Methyl-l-deoxynojirimycin, L- 750,667 trihydrochloride, (+)-MK-801 hydrogen maleate, Pempidine tartrate, (-)-Naproxen sodium, Raloxifene hydrochloride, SKF 83959 hydrobromide, L-687,384 hydrochloride, 7,7-Dimethyl-(5Z,8Z)- eicosadienoic acid, SP-600125, Ro 41-0960, Ancitabine hydrochloride, Risperidone, Telenzepine dihydrochloride, NO-711 hydrochloride, U- 99194A maleate, S(+)-Raclopride L-tartrate, Pirenzepine dihydrochloride, Captopril, Thioperamide maleate, Alprenolol hydrochloride, Ritodrine hydrochloride, Putrescine dihydrochloride, l-(2- Methoxyphenyl)piperazine hydrochloride, PAPP, U-69593, AG- 1478, riluzole, Phentolamine mesylate, DBO-83, Formestane, Carbamazepine, 4-(2-Aminoethyl)benzenesulfonyl fluoride hydrochloride, Terbutaline hemisulfate, UK 14304, GR 113808, Leflunomide, Acetylthiocholine chloride, spermidine, 5- (N-Methyl-N-isobutyl)amiloride, ATPO, Acadenisine or Metformin, or a combination thereof. In some non-limiting examples, the compound is Aminocaproic Acid; Vas2870, L-745,870; Riluzole; Acadenisine; Metformin or a pharmaceutically acceptable salt thereof. Suitable compounds are disclosed, for example, in PCT Publication No. WO2021 / 050980 A1, incorporated herein by reference. Dosage treatment may be a single dose schedule or a multiple dose schedule to ultimately deliver the amount specified above. The doses can be intermittent. Moreover, the subject may be administered as many doses as appropriate. Individual doses are typically not less than an amount required to produce a measurable effect on the subject, and may be determined based on the pharmacokinetics and pharmacology for absorption, distribution, metabolism, and excretion ("ADME") of the subject composition or its by- products, and thus based on the disposition of the composition within the subject. This includes consideration of the route of administration as well as dosage amount, which can be adjusted for local applications. Effective amounts of dose and / or dose regimen can readily be determined empirically from preclinical assays, from safety and escalation and dose range trials, individual clinician-patient relationships, as well as in vitro and in vivo assays.Administration may be provided as a a periodic bolus or as continuous infusion (for example, from an implant disposed at an location. Intraocular injection of the nucleic acid molecules, antibodies, and CRISPR / Cas13 systems disclosed herein can be performed once, or can be performed repeatedly, such as 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 20, 30, 40, 50, 60, 70, 80, 90, or 100 or more times. Administration can be performed biweekly, weekly, every other week, monthly, or every 2, 3, 4, 5, or 6 months. Local modes of administration include intraocular routes, as discussed below. In an aspect, significantly smaller amounts (compared with systemic approaches) may exert an effect when administered locally (for example, intraocularly) compared to when administered systemically (for example, intravenously). Local modes of administration can reduce or eliminate the incidence of potential side effects. In some aspect, the method includes administraton of an agent, such as, but not lmited to, an anti- retroviral agent, inhibitory RNA, or an agent that increases ANG activity, to the eye. The amount of the ophthalmic formulation to be administered to the eye can depend on the individual to be subjected to the treatment, and is preferably an amount optimized to achieve the desired treatment without accompanying marked side effects. Dosage can include administration to the eye, such as, but not limited to, in the form of an eye drop. These drops can be administered, for example, 1, 2, 3, 4, 5, 6, or more times a day (such as every hour, every 2 hours, every 4 hours, every 6 hours, every 12 hours, or every 24 hours). The eye drops can be administered once a day, every other day, bi-weekly, or weekly. The vision of a subject can be evaluated, as discussed below. A. Intraocular administration Intraocular administration can be by subretinal, direct retinal, suprachoroidal or intravitreal injection. The volume of the medicament composition injected may, for example, be about 10-500μL, for example about 50-500, 100-500, 200-500, 300-500, 400-500, 50-250, 100-250, 200-250 or 50-150 μL. The volume may, for example, be about 10, 50, 100, 150, 200, 250, 300, 350, 400, 450 or 500 μL. In some aspects, the volume of the pharmaceutical composition injected is 100μL. Subretinal injections are injections into the subretinal space, i.e., underneath the neurosensory retina. During a subretinal injection, the injected material is directed into, and creates a space between, the photoreceptor cell and retinal pigment epithelial (RPE) layers. When the injection is carried out through a small retinotomy, a retinal detachment may be created. The detached, raised layer of the retina that is generated by the injected material is referred to as a “bleb.” The hole created by the subretinal injection can be sufficiently small that the injected solution does not significantly reflux back into the vitreous cavity after administration. Such reflux can be particularly problematic when a medicament is injected, if effects of the medicament are directed away from the target zone. Preferably, the injection creates a self-sealing entry point in the neurosensory retina, i.e. once the injection needle is removed, the hole created by the needle reseals such that very little or substantially no injected material is released through the hole.Subretinal injection needles are available (e.g., DORC 41 G Teflon subretinal injection needle, Dutch Ophthalmic Research BV, Zuidland, The Netherlands). Unless damage to the retina occurs during the injection, and as long as a sufficiently small needle is used, substantially all injected material remains localized between the detached neurosensory retina and the RPE at the site of the localized retinal detachment (i.e., does not reflux into the vitreous cavity). Indeed, the typical persistence of the bleb over a short time frame indicates that there is usually little escape of the injected material into the vitreous. The bleb may dissipate over a longer time frame as the injected material is absorbed. Visualizations of the eye, in particular the retina, for example using optical coherence tomography can be performed. Under certain circumstances, for example during end-stage retinal degenerations, identifying the retina is difficult because it is thin, transparent and difficult to see against the disrupted and heavily pigmented epithelium on which it sits. The use of a blue vital dye (e.g., BRILLIANT PEEL®, Geuder; MEMBRANEBLUE-DUAL®, Dore) may facilitate the identification of the retinal hole made for the retinal detachment procedure (i.e., step (a) in the two-step subretinal injection method of the invention) so that the medicament can be administered through the same hole without the risk of reflux back into the vitreous cavity. The use of the blue vital dye also identifies any regions of the retina where there is a thickened internal limiting membrane or epiretinal membrane, as injection through either of these structures would hinder clean access into the subretinal space. Furthermore, contraction of either of these structures in the immediate post-operative period could lead to stretching of the retinal entry hole, which could lead to reflux of the medicament into the vitreous cavity. Suprachoridal injection can be utilized. In this method, the agent be delivered to the suprachoroidal space using an ab extemo approach that utilizes an microcatheter (see, for example, Peden et al. (2011) PLoS One 6(2): e17140). In this method a limbal conjunctival peritomy is performed to expose bare sclera, followed by sclerotomy to expose bare choroid. A microcatheter (such as the iTrack 250A from iScience Interventional, optionally connected to an illumination system such as the iLumin laser-diode based micro- illumination system (iScience Interventional)) is introduced into the suprachoroidal space and advanced posteriorly towards the optic disc. Following manipulation of the microcatheter tip into the desired position, injection of the product, polynucleotide or vector forms a bleb within the retina and choroid. In some aspects, the agent delivered suprachoroidally by a method that includes (i) introduction of a microcatheter into the suprachoroidal space; (ii) advancing the microcatheter within said space until the tip is in the proximity of the afflicted region of the retina; and (iii) injecting the product, polynucleotide or vector from the microcatheter tip to create a bleb. In some aspects, a therapeutically effective amount of an agent disclosed herein is administered by intraocular, for example intravitreal, injection. A general method for intravitreal injection may be illustrated by the following brief outline. This example is merely meant to illustrate certain features of the method, and is in no way meant to be limiting. Procedures for intravitreal injection are known in the art (see, for example Peyman, et al. (2009) Retina 29(7):875-912 and Fagan and Al-Qureshi, (2013) Clin. Experiment.Ophthalmol.41(5):500-7). Other methods of intraocular administration are known in the art, and include subretinal administration. Briefly, a subject for intravitreal injection may be prepared for the procedure by pupillary dilation, sterilization of the eye, and administration of anesthetic. Any suitable mydriatic agent known in the art may be used for pupillary dilation. Adequate pupillary dilation may be confirmed before treatment. Sterilization may be achieved by applying a sterilizing eye treatment, e.g., an iodide-containing solution such as povidone-iodine (BETADINE®). A similar solution may also be used to clean the eyelid, eyelashes, and any other nearby tissues (e.g., skin). Any suitable anesthetic may be used, such as lidocaine or proparacaine, at any suitable concentration. Anesthetic may be administered by any method known in the art, including without limitation topical drops, gels or jellies, and subconjuctival application of anesthetic. Prior to injection, a sterilized eyelid speculum may be used to clear the eyelashes from the area. The site of the injection may be marked with a syringe. The site of the injection may be chosen based on the lens of the patient. For example, the injection site may be 3-3.5 mm from the limus in pseudophakic or aphakic patients, and 3.5-4 mm from the limbus in phakic patients. The patient may look in a direction opposite the injection site. During injection, the needle can be inserted perpendicular to the sclera and pointed to the center of the eye. The needle can be inserted such that the tip ends in the vitreous, rather than the subretinal space. Any suitable volume known in the art for injection may be used. After injection, the eye can be treated with a sterilizing agent such as an antibiotic. The eye can also be rinsed to remove excess sterilizing agent. Intravitreal injection of an agent as disclosed herein can be performed once, or can be performed repeatedly, such as 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 times. Administration can be performed biweekly, weekly, every other week, monthly, or every 2, 3, 4, 5, or 6 months. In some aspects, the method can include administering a therapeutically effective amount of an agent to inhibit unwanted angiogenesis, for example, to counteract the choroidal new vessel (CNV) growth under the macula in AMD patients. An exemplary therapeutic agent can reduce activity of vascular endothelial growth factor (VEGF), for example, by binding to the receptor site of active forms of VEGF and preventing interaction of VEGF with its receptors. A therapeutically effective amount of and that suppresses the expression of VEGF by inhibiting pathways leading to VEGF secretion, such as STAT3, NF-kB, HIF- 1α. Other drugs can prevent atrophy of RPE cells by targeting complement pathway, autophagy, or NF-kB pathways. Treatments of use for AMD include medications directed to stopping the growth of new blood vessels, such as bevacizumab (AVASTIN®), ranibizumab (LUCENTIS®), and aflibercept (EYLEA®); photodynamic therapy; photocoagulation; and low vision rehabilitation In further aspect, the method includes administering to the subject a therapeutically effective amount of Ciliary Neurotrophic Factor (CNTF), Brain-Derived Neurotrophic Factor (BDNF), or Pigment Epithelial Derived Factor (PEDF), which can be used, for example, to promote development or function of neurons such as photoreceptor cells. Other exemplary, non-limiting aspects include administering to the subject a therapeutically effective amount of thrombospondin 1, an anti-inflammatory cytokine (for example,interleukin (IL)-lra, IL-6, Fas ligand or tumor factor (TGF)-beta, a neurotrophic / neuroprotective growth factor such as, but not limited to, glial cell derived growth factor, brain-derived neurotrophic factor, nerve growth factor, neurotrophin-3, - 4 / 5, -6, and vitamin E. Such agents may be provided singly or in combination. Implants are also of use in the methods disclosed herein. The implants can be inserted into the eye by a variety of methods, including placement by forceps or by trocar following making an incision in the sclera (for example, a 2-3 mm incision) or other suitable sites. In some cases, the implant can be placed by trocar without making a separate incision, but instead by forming a hole directly into the eye with the trocar. The method of placement can influence the release kinetics. For example, implanting the device into the vitreous or the posterior chamber with a trocar may result in placement of the device deeper within the vitreous than placement by forceps, which may result in the implant being closer to the edge of the vitreous. The location of the implanted device may influence the concentration gradients of the therapeutic agent surrounding the device, and thus influence the release rates (for example, a device placed closer to the edge of the vitreous may result in a slower release rate, see U.S. Patent No.5,869,079 and U.S. Patent No. 6,699,493). In one aspect, an implant is formulated with a bioerodible polymer matrix. Generally, when implants are used, the therapeutic agent is homogeneously distributed through the polymeric matrix, such that it is distributed evenly enough that no detrimental fluctuations in rate of release occur because of uneven distribution of the immunosuppressive agent in the polymer matrix. The selection of the polymeric composition to be employed varies with the desired release kinetics, the location of the implant, patient tolerance, and the nature of the implant procedure. The polymer can be included as at least about 10 weight percent of the implant. In one example, the polymer is included as at least about 20 weight percent of the implant. In another aspect, the implant comprises more than one polymer. These factors are described in detail in U.S. Patent No.6,699,493. Characteristics of the polymers generally include biodegradability at the site of implantation, compatibility with the agent of interest, ease of encapsulation, and water insolubility, amongst others. Generally, the polymeric matrix is not fully degraded until the drug load has been released. The chemical composition of suitable polymers is known in the art (for example, see U.S. Patent No.6,699,493). Topical administration to the eye is also of use with the disclosed methods. Topical preparations can include eye drops, ointments, sprays and the like. Eye drops or sprays can be provided in unit dose dispensers (such as eye drop bottles that dispense a metered unit dose. These can include, for example, wetting agents and an inert matrix. As one example of an inert matrix, liposomes may be prepared from dipalmitoyl phosphatidylcholine (DPPC), such as egg phosphatidylcholine (PC). Liposomes can be applied topically, either in the form of drops or as an aqueous based cream, or can be injected intraocularly. In a formulation for topical application, the active agent is slowly released over time as the liposome capsule degrades due to wear and tear from the eye surface. In a formulation for intraocular injection, the liposome capsule degrades due to cellular digestion. Both of these formulations provide advantages of a slow release drug delivery system, allowing the subject to be exposed to a substantially constant concentration of the active agent over time. In one example, the active agent can be dissolved in an organic solvent such asDMSO or alcohol as previously described and contain a polyanhydride, poly(glycolic) acid, poly(lactic) acid, or polycaprolactone polymer. B. Pharmaceutical Compositions including Nucleic Acid Molecules Pharmaceutical compositions including a nucleic acd moleucle can be formulated and administered in a variety of ways (see, e.g., U.S. Published Application No.2005 / 0054567, which discloses pharmaceutical compositions as well as administration of such compositions and is incorporated herein by reference). The pharmaceutical compositions can include a nanoparticle or dendrimer. These pharmaceutical compositions are of use in the methods disclosed herein. Pharmaceutical compositions including a nucleic acid molecule are provided that are formulated for local delivery to the eye. These include nucleic acid molecules encoding antibodies and antigen binding fragments thereof, inhibitory RNA molecules, Cas13 proteins, and gRNAs. The nucleic acid molecule can be administered in vivo to the subject, such as, but not limited to, oral, intravenous, or intraoclar (such as instravitreous) administration. Generally, it is desirable to prepare the compositions as pharmaceutical compositions appropriate for the intended application. Accordingly, methods for making a pharmaceutical composition containing the nucleic acid molecules, or vectors described above, are included herein. Typically, preparation of a pharmaceutical composition entails preparing a pharmaceutical composition that is essentially free of pyrogens, as well as any other impurities that could be harmful to humans or animals. Typically, the pharmaceutical composition contains appropriate salts and buffers to render the composition stable and allow for uptake of nucleic acids or virus by target cells. Pharmaceutical compositions including nucleic acid molecules can be formulated for injection, such as for introcular or intravenous administration. Such compositions are formulated generally by mixing a disclosed nucleic acid molecule at the desired degree of purity in a unit dosage injectable form (solution, suspension, or emulsion) with a pharmaceutically acceptable carrier, for example, one that is non-toxic to recipients at the dosages and concentrations employed and is compatible with other ingredients of the formulation. Pharmaceutical compositions can include an effective amount of the nucleic acid molecule dispersed (for example, dissolved or suspended) in a pharmaceutically acceptable carrier or excipient. Pharmaceutically acceptable carriers and / or pharmaceutically acceptable excipients are known in the art and are described, for example, in Remington’s Pharmaceutical Sciences by E. W. Martin, Mack Publishing Co., Easton, PA, 19th Edition (1995). The nature of the carrier will depend on the particular mode of administration being employed. For example, formulations usually contain injectable fluids that include pharmaceutically and physiologically acceptable fluids, such as water, physiological saline, balanced salt solutions, aqueous dextrose, glycerol, or the like, as a vehicle. In addition, pharmaceutical compositions to be administered can contain minor amounts of non-toxic auxiliary substances, such as wetting or emulsifying agents, preservatives, pH buffering agents and the like, for example, sodium acetate or sorbitan monolaurate. A disclosed nucleic acid molecule can be suspended in an aqueous carrier, for example, in anisotonic or hypotonic buffer solution at a pH of about 3.0 to about 8.5, such as about 4.0 to about 8.0, about 6.5 to about 8.5, or about 7.4. Useful buffers buffered phosphate or an ionic boric acid buffer. The active ingredient, optionally together with excipients, can also be in the form of a lyophilisate and can be made into a solution prior to administration by the addition of suitable solvents. The pharmaceutically acceptable carriers include any and all solvents, dispersion media, coatings, isotonic and absorption delaying agents, and the like. The use of such media and agents for pharmaceutically active substances is well-known in the art. Supplementary active ingredients also can be incorporated into the compositions. For example, certain pharmaceutical compositions can include the vectors or viruses in water, mixed with a suitable surfactant, such as hydroxy-propylcellulose. Dispersions also can be prepared in glycerol, liquid polyethylene glycols, and mixtures thereof as well as in oils. Under ordinary conditions of storage and use, these preparations contain a preservative to prevent the growth of microorganisms. Pharmaceutically acceptable salts can be included therein, for example, mineral acid salts such as hydrochlorides, hydrobromides, phosphates, sulfates, and the like; and the salts of organic acids such as acetates, propionates, malonates, benzoates, and the like. Additionally, auxiliary substances, such as wetting or emulsifying agents, pH buffering substances, and the like, may be present in such vehicles. In some aspects, the excipients confer a protective effect to a virus including the nucleic acid molecules, such as AAV virion or lentivirus virion, such that loss of AAV virions or lentivirus virions, as well as transduceability resulting from formulation procedures, packaging, storage, transport, and the like, is minimized. These excipient compositions are therefore considered "virion-stabilizing" in the sense that they provide higher virion titers and higher transduceability levels than their non-protected counterparts, as measured using standard assays, see, for example, Published U.S. Application No.2012 / 0219528 Exemplary excipients that can used to protect a virion from activity degradative conditions include, but are not limited to, detergents, proteins, e.g., ovalbumin and bovine serum albumin, amino acids, e.g., glycine, polyhydric and dihydric alcohols, such as but not limited to polyethylene glycols (PEG) of varying molecular weights, such as PEG-200, PEG-400, PEG-600, PEG-1000, PEG-1450, PEG-3350, PEG-6000, PEG-8000 and any molecular weights in between these values, with molecular weights of 1500 to 6000 preferred, propylene glycols (PG), sugar alcohols, such as a carbohydrate, preferably, sorbitol. The detergent, when present, can be an anionic, a cationic, a zwitterionic or a nonionic detergent. An exemplary detergent is a nonionic detergent. One suitable type of nonionic detergent is a sorbitan ester, e.g., polyoxyethylenesorbitan monolaurate (TWEEN®-20) polyoxyethylenesorbitan monopalmitate (TWEEN®- 40), polyoxyethylenesorbitan monostearate (TWEEN®-60), polyoxyethylenesorbitan tristearate (TWEEN®- 65), polyoxyethylenesorbitan monooleate (TWEEN®-80), polyoxyethylenesorbitan trioleate (TWEEN®- 85), such as TWEEN®-20 and / or TWEEN®-80. These excipients are commercially available from a number of vendors, such as Sigma, St. Louis, Mo. The amount of the various excipients in any of the disclosed compositions including virus, such as AAV or a lentivirus, varies and is readily determined by one of skill in the art. For example, a protein excipient, such as BSA, if present, will can be present at a concentration of between 1.0 weight (wt.) % toabout 20 wt. %, such as 10 wt. %. If an amino acid such as glycine is used in the formulations, it can be present at a concentration of about 1 wt. % to wt. %. A carbohydrate, such as sorbitol, if present, can be present at a concentration of about 0.1 wt % to about 10 wt. %, such as between about 0.5 wt. % to about 15 wt. %, or about 1 wt. % to about 5 wt. %. If polyethylene glycol is present, it can generally be present on the order of about 2 wt. % to about 40 wt. %, such as about 10 wt. % top about 25 wt. %. If propylene glycol is used in the subject formulations, it will typically be present at a concentration of about 2 wt. % to about 60 wt. %, such as about 5 wt. % to about 30 wt. %. If a detergent such as a sorbitan ester (TWEEN®) is present, it can be present at a concentration of about 0.05 wt. % to about 5 wt. %, such as between about 0.1 wt. % and about 1 wt %, see U.S. Published Patent Application No.2012 / 0219528, which is incorporated herein by reference. In one example, an aqueous virion-stabilizing formulation comprises a carbohydrate, such as sorbitol, at a concentration of between 0.1 wt. % to about 10 wt. %, such as between about 1 wt. % to about 5 wt. %, and a detergent, such as a sorbitan ester (TWEEN®) at a concentration of between about 0.05 wt. % and about 5 wt. %, such as between about 0.1 wt. % and about 1 wt. %. Virions are generally present in the composition in an amount sufficient to provide a therapeutic effect when given in one or more doses, as defined above. In some aspects, a compositon can be formulated in unit dosage form, suitable for individual administration of precise dosages. The amount of active compound(s) administered will depend on the subject being treated, the severity of the affliction, and the manner of administration and is best left to the judgment of the prescribing clinician. Within these bounds, the formulation to be administered will contain a quantity of the active compound(s) in amounts effective to achieve the desired effect in the subject being treated. Nucleic acid molecules can be incporated into an inert matrix. As one example of an inert matrix, liposomes may be prepared from dipalmitoyl phosphatidylcholine (DPPC), such as egg phosphatidylcholine (PC). Liposomes, including cationic and anionic liposomes, can be prepared and used in the persent methods. In a formulation for intrahepatic injection, the liposome capsule degrades due to cellular digestion. These formulations can provide a slow-release drug delivery system, exposing a subject to a substantially constant concentration of nucleic acid molecule over time. In one example, the nucleic acid molecule can be dissolved in an organic solvent, such as DMSO or alcohol, as previously described, and contain a polyanhydride, poly(glycolic) acid, poly(lactic) acid, or polycaprolactone polymer. The nucleic acid molecule may be formulated to permit release over a specific period of time. A release system can include a matrix of a biodegradable material or a material which releases the incorporated nucleic acid molecule by diffusion. The nucleic acid molecule can be homogeneously or heterogeneously distributed within the release system. A variety of release systems may be useful; however, the choice of the appropriate system will depend upon rate of release required by a particular application. Both non- degradable and degradable release systems can be used. Suitable release systems include polymers and polymeric matrices, non-polymeric matrices, or inorganic and organic excipients and diluents such as, butnot limited to, calcium carbonate and sugar (for trehalose). Release systems may be natural or synthetic. However, synthetic release systems are because generally they are more reliable, more reproducible and produce more defined release profiles. The release system material can be selected so that active ingredients having different molecular weights are released by diffusion through or degradation of the material. Representative synthetic, biodegradable polymers include, for example: polyamides such as poly(amino acids) and poly(peptides); polyesters such as poly(lactic acid), poly(glycolic acid), poly(lactic- co-glycolic acid), and poly(caprolactone); poly(anhydrides); polyorthoesters; polycarbonates; and chemical derivatives thereof (substitutions, additions of chemical groups, for example, alkyl, alkylene, hydroxylations, oxidations, and other modifications routinely made by those skilled in the art), copolymers and mixtures thereof. Representative synthetic, non-degradable polymers include, for example: polyethers such as poly(ethylene oxide), poly(ethylene glycol), and poly(tetramethylene oxide); vinyl polymers-polyacrylates and polymethacrylates such as methyl, ethyl, other alkyl, hydroxyethyl methacrylate, acrylic and methacrylic acids, and others such as poly(vinyl alcohol), poly(vinyl pyrolidone), and poly(vinyl acetate); poly(urethanes); cellulose and its derivatives such as alkyl, hydroxyalkyl, ethers, esters, nitrocellulose, and various cellulose acetates; polysiloxanes; and any chemical derivatives thereof (substitutions, additions of chemical groups, for example, alkyl, alkylene, hydroxylations, oxidations, and other modifications routinely made by those skilled in the art), copolymers, and mixtures thereof. Poly(lactide-co-glycolide) microspheres can also be used for intrahepatic injection. Typically the microspheres are composed of a polymer of lactic acid and glycolic acid, which are structured to form hollow spheres. The spheres can be approximately 15-30 microns in diameter and can be loaded with the biologicla molecules described herein. An implant can be uised, that can be inserted into the eye by a variety of methods, which can influence the release kinetics. The location of the implanted device may influence the concentration gradients of the nucleic acid molecule surrounding the device and, thus, influence the release rates. Generally, when implants are used, the nucleic acid molecule is homogeneously distributed through the polymeric matrix, such that it is distributed evenly enough that no detrimental fluctuations in rate of release occur due to uneven distribution in the polymer matrix. The selection of the polymeric composition to be employed varies with the desired release kinetics, the location of the implant, patient tolerance, and the nature of the implant procedure. The polymer can be included as at least about 10 weight percent of the implant. In one example, the polymer is included as at least about 20 weight percent of the implant. In another aspect, the implant comprises more than one polymer. These factors are described in detail in U.S. Patent No.6,699,493. Characteristics of the polymers can include biodegradability at the site of implantation, compatibility with the agent of interest, ease of encapsulation, and water insolubility, among others. Generally, the polymeric matrix is not fully degraded until the drug load has been released. The chemical composition of suitable polymers is known in the art (for example, see U.S. Patent No.6,699,493). The nucleic acid molecule can be formulated in an implantable form with other carriers and solvents. Forexample, buffering agents and preservatives can be The implant sizes and shape can also be varied for use in particular regions of the liver Patent No.5,869,079). In some aspects, a nanoparticle or dendrimer is used. Nucleic acid molecules can be delivered by microinjection, electroporation, lipid-mediated transfection, peptide-mediated delivery, nanoparticle mediated delivery (such as lipid or polymeric nanoparticle mediate delivery), dendrimer mediated delivery, as a conjugate to GalNAc, as an mRNA modified by base linker sugars, in association with a degradable polymer, as an mRNA-Lipoplex, as mRNA cargo of PEG-10, or other methods known in the art. In some aspects, the mRNA, An appropriate dose depends on the subject being treated (e.g., human or nonhuman primate or other mammal), age and general condition of the subject to be treated, the severity of the condition being treated, the mode of administration, among other factors. An appropriate effective amount can be readily determined by one of skill in the art. Thus, a “therapeutically effective amount” will fall in a relatively broad range that can be determined through clinical trials. In some embodiemtns, a viral vector is utilzed. In some aspects, a therapeutically effective dose will be on the order of from about 105to 1016of virions (such as AAV virions, lentivirus or baculovirs), such as 108to 1014virions. The dose can depend on the efficiency of transduction, promoter strength, the stability of the message and the protein encoded thereby, and clinical factors. Effective dosages can be readily established by one of ordinary skill in the art through routine trials establishing dose response curves. In some aspects, if the nucleic acid molecule is included in an AAV vector, an effective amount will be about 1 X108vector genomes or more, in some cases about 1 X 109, about 1 X 1010, about 1 X 1011, about 1 X 1012, or about 1 X 1013vector genomes or more, in certain instances, about 1 X 1014vector genomes or more, and usually no more than about 1 X 1015vector genomes administered to the recipient. In some aspects, the amount of vector that is delivered is about 1 X 1014vectors or less, for example about 1 X 1013, about 1 X 1012, about 1 X 1011, about 1 X 1010, or about 1 X 109vectors or less, in certain instances about 1 X 108vectors, and typically no less than 1 X 108vectors administered to the recipient. In some non-limiting examples, the amount of vector genomes that is delivered is about 1 X 1010to about 1 X 1011vectors. In additional non-limiting examples, the amount of vector that is delivered is about 1 X 1010to about 1 X 1012vector genomes. In some aspects, the amount of pharmaceutical composition to be administered may be measured using multiplicity of infection (MOI). In some aspects, MOI refers to the ratio, or multiple of vector or viral genomes to the cells to which the nucleic may be delivered. In some aspects, the MOI may be about 1 X 106. In some cases, the MOI can be about 1 X 105to about 1 X 107. In some cases, the MOI may be about 1 X 104to about 1 X 108. In some cases, recombinant viruses of the disclosure are at least about 1 X 101, about 1 X 102, about 1 X 103, about 1 X 104, about 1 X 105, about 1 X 106, about 1 X 107, about 1 X 108, about 1 X 109, about 1 X 1010, about 1 X 1011, about 1 X 1012, about 1 X 1013, about 1 X 1014, about 1 X 1015, about 1 X 1016, about 1 X 1017, and about 1 X 1018MOI. In some cases, recombinant viruses of this disclosure are about 1 X 108to 1 X 1014MOI. In some the amount of pharmaceutical composition deliveredcomprises about 1 X 108to about 1 X 1015of recombinant viruses, about 1 X 109to about 1 X 1014particles of recombinant viruses, about 1 X 1010to 1 X 1013particles of recombinant viruses, or about 1 X 1011to about 1 X 10s12particles of recombinant viruses. Dosage treatment may be a single dose schedule or a multiple dose schedule to ultimately deliver the amount specified above. Moreover, the subject may be administered as many doses as appropriate. Thus, the recipientmay be given, e.g., 105to 1016AAV virions in a single dose, or two, four, five, six or more doses that collectively result in delivery of, e.g., 105to 1016AAV virions. One of skill in the art can readily determine an appropriate number of doses to administer. In some aspects, an AAV is administered to the recipient and / or to the donor liver (such as in an ex vivo perfusion system) at a dose of about 1 x 1011to about 1 x 1014viral particles (vp) / kg. In some examples, the AAV is administered to the recipient at a dose of about 1 x 1012to about 8 x 1013vp / kg. In other examples, the AAV is administered to the recipient liver at a dose of about 1 x 1013to about 6 x 1013vp / kg. In specific non-limiting examples, the AAV is administered to the recipient at a dose of at least about 1 x 1011, at least about 5 x 1011, at least about 1 x 1012, at least about 5 x 1012, at least about 1 x 1013, at least about 5 x 1013, or at least about 1 x 1014vp / kg. In other non-limiting examples, the AAV is administered to the recipient at a dose of no more than about 5 x 1011, no more than about 1 x 1012, no more than about 5 x 1012, no more than about 1 x 1013, no more than about 5 x 1013, or no more than about 1 x 1014vp / kg. In one non-limiting example, the AAV is administered to the recipient at a dose of about 1 x 1012vp / kg. The AAV can be administered in a single dose, or in multiple doses (such as 2, 3, 4, 5, 6, 7, 8, 9 or 10 or more doses) as needed for the desired therapeutic results. In some aspects, a lentivirus is administered at a dose of about 1 x 1011to about 1 x 1014viral particles (vp) / kg. In some examples, the lentivirus is administered to the recipient at a dose of about 1 x 1012to about 8 x 1013vp / kg. In other examples, the lentivirus is administered to the recipient at a dose of about 1 x 1013to about 6 x 1013vp / kg. In specific non-limiting examples, the lentivirus is administered to the recipient at a dose of at least about 1 x 1011, at least about 5 x 1011, at least about 1 x 1012, at least about 5 x 1012, at least about 1 x 1013, at least about 5 x 1013, or at least about 1 x 1014vp / kg. In other non-limiting examples, the lentivirus is administered to the recipient at a dose of no more than about 5 x 1011, no more than about 1 x 1012, no more than about 5 x 1012, no more than about 1 x 1013, no more than about 5 x 1013, or no more than about 1 x 1014vp / kg. In one non-limiting example, the lentivirus is administered to the recipient at a dose of about 1 x 1012vp / kg. The lentivirus can be administered in a single dose, or in multiple doses (such as 2, 3, 4, 5, 6, 7, 8, 9 or 10 or more doses) as needed for the desired therapeutic results. C. Evaluation Following administration of one or more therapeutic agents provided herein, the subject can be evaluated for response. Exemplary methods include, but are not limited to, ophthalmoscopy, microperimetry, gonioscopy, pachymetry, optical coherence tomography, reading speed, electro-retinograms, adaptive optics, ETDRS reading chart, or nerve fiber analysis. In some aspects, retinal ganglion cell number and / or viability can beassessed. One of skill in the art can readily determine that the disclosed methods are effective. For example, it can be determined by whether the cup-to-disc stabilized. Scanning laser polarimetry or optical coherence tomography could be used, for example to perform retinal nerve fiber layer analysis. A visual field test could be used to monitor progression. For any of the disclosed methods, therapeutic efficacy in treating a vision deficiency can as an alteration in the individual's vision. EXAMPLES Example 1 HERV-K RNA Expression Observed in Cadaveric AMD eyes Age-related macular degeneration (AMD) is caused by death and degeneration of the retinal pigment epithelium (RPE) cells. Several factors including aging and the complement pathway have been linked to AMD but the actual mechanism of RPE degeneration is not known. An in vitro model was developed using induced pluripotent stem (iPSC)-derived RPE cells that recapitulates disease pathogenesis of AMD. Treatment of iPSC-RPE cells with activated complement (CC-HS) induced hallmark features of AMD in iPSC-RPE cells including the formation of subRPE drusen deposits that stain for antibodies against lipoprotein APOE and dye that stains lipids (BODIPY® fluorophore) (FIG.1). 48 hours treatment of CC- HS led to significant change in APOE localization from the apical side of cells to the basal sides of cells (FIG.1). BODIPY® fluorophore staining revealed higher staining for the dye in CC-HS treated cells. Drusen are not formed if cells are treated with inactive complement (CI-HS). Furthermore, treatment with CC-HS led to degeneration of the RPE monolayer as confirmed by reduced F-ACTIN staining that marks cell borders (FIG.1) and loss of trans-epithelial resistance (TER) of the monolayer. TER of the monolayer is formed by functional tight junctions between neighboring RPE cells. As cells degenerate in a diseased state, the tight junctions fall apart dropping the TER of cells, as seen in CC-HS treatment conditions (FIG. 1B). Activation of endogenous retroviruses can cause degeneration of cells. Endogenous retroviral RNA (FIG.2) and the three translated proteins – gag, pol, and env may induce degeneration of cells. Comparative RNAseq analysis was used to identify that the expression of several members of the HERV-K family of endogenous retroviruses was significantly increased in CC-HS treated cells as compared to CI-HS treated cells (FIGS.3A-3B). Approximately, 80 different loci were discovered that showed differential expression of HERV-K retroviruses (FIG.3A). Sixteen of the most differentially expressed HERV-K loci between CI-HS and CC-HS, were highlighted, and their exact location in the genome was determined (FIG. 3B). Temporal analysis of CC-HS treatment showed that the expression of different components of HERV-K family of endogenous retroviruses (ENV and GAG) was increased in CC-HS treated cells, as compared to CI-HS treated cells (FIG.4A, 4B and 5). Expression of other retroviruses like HERV-R were not increased in this context (FIG.4A, 4B). Similar increase in expression of HERV-K RNA was noted in cadaveric AMD eyes, confirming physiological relevance (FIG.6). Overall, this analysis revealed that theexpression of a specific HERV-K class of retroviruses was increased in CC-HS treated iRPE and this increase in HERV-K expression was co- with the formation of subRPE deposits and degeneration of the RPE monolayer. Example 2 Reduction of HERV-K RNA Expression in Cadaveric AMD eyes CC-HS treatment increases the expression of inflammatory cytokines (IL 6 and IL 8) secreted by RPE cells towards apical and basal sides (FIGS.7A, 7B). It was determined whether this increase in expression of inflammatory cytokines was mediated by increased HERV-K expression in CC-HS treated cells. To suppress the expression of HERV-K we used anti-retroviral drug Tenofovir that block transcription of HERV-K mRNA. Co-treatment of iRPE cells with CC-HS and Tenofovir decreased apical and basal secretions of both IL6 and IL8 (FIGS.7A, 7B). HERV-K ENV protein and RNA are thought to trigger inflammatory changes inside cells by activating receptors TLR3 and TLR4. Hence, it was determined if blocking the activity of both these receptors would reduce the expression of IL6 and IL8. Blocking the activity of these receptors also reduced the expression of proinflammatory cytokines in CC-HS treated RPE cells, suggesting ENV proteins do work through these receptors in RPE cells (FIGS.7A, 7B). Furthermore, blocking TLR3 and TLR4 activity along with cotreatment of iRPE with CC-HS also reduced the formation of subRPE drusen deposits stained with lipid staining dye BODIPY® (FIGS.8A, 8B). These data indicate that degenerative phenotype seen in iRPE cells are driven by HERV-K mediated signaling changes likely mediated by TLR3 and TLR4 receptors. To confirm that virus activation in RPE cells can trigger AMD phenotype without CC-HS treatment, HERV-K ENV protein was overexpressed in healthy cells (FIGS.9A-9C). The ENV protein of HERV-K that is thought to drive HERV-K pathology in cells was fused to a V5 tag allowing detection of the overexpressed protein separate from the endogenously make ENV protein. Red fluorescent protein mcherry was driven from the same expression cassette driving ENV protein expression. However, once transcribed the two proteins were made separately because of the presence of an internal ribosome entry site (IRES) in between ENV and mcherry. Expression of the entire cassette was driven by a CMV promoter allowing high expression. This construct was packaged into a lentivirus and iRPE cells were transduced with it. Western blot performed on cell lysates from iRPE transduced with ENV-expressing lentivirus compared to non- transduced cells showed the construct was able to derive the expression of ENV protein of HERV-K. Immunostaining for the ENV protein in cells transduced at different multiplicities of infection (MOI) of 0.5 and 3.0 showed a lentivirus dose dependent increase in expression of the ENV protein (FIG.9A-9C). Overexpression of ENV protein in wildtype iRPE was sufficient to trigger the AMD phenotype without CC- HS treatment, measured as loss of cellular barrier resistance (TER) and increased BODIPY® staining (FIGS.10A-10C). The decrease in monolayer TER was dose dependent for the ENV protein. For instance, higher MOI led to higher amount of ENV protein (FIG.10C) and led to higher decrease in monolayer TER(FIG.10A) but the increase in subRPE lipid as stained by BODIPY® was not a dose dependent phenomenon (FIG.10B). Overall, this indicates ENV protein of HERV-K was sufficient to trigger AMD phenotype in iRPE cells. To determine the mechanism of increased HERV-K expression in CC-HS treated cells, the expression of angiogenin (ANG), a ribonuclease enzyme that is thought to degrade HERV-K RNA via the use of Lys-specific tRNA half, was determined using RNA-seq. The analysis revealed that, as compared to untreated or CI-HS treated cells, in CC-HS treated cells, ANG expression reduced significantly, coincidental with the increase in expression of HERV-K (FIG.11A). Temporal qRT-PCR analysis of CC-HS treated cells, after 2, 4, 6 days of treatment, showed that ANG expression progressively decreased in lysates of CC- HS treated cells. In contrast the expression of another RNA degrading enzyme, DICER, did not decrease (FIG.11B). Next, it was determined whether the concentration of ANG protein that is secreted by RPE cells into cell media was also reduced after 2, 4, and 6 days of CC-HS treatment of RPE cells, according to a different analysis. Consistent with the RNAseq and qRT-PCR analyses, an ELISA revealed that levels of secreted ANG progressively reduced in CC-HS treated cells, as compared to CI-HS treated cells (FIG.11C). The reduction of ANG expression was consistent across three biological replicates. Similar findings about lower ANG expression in CC-HS treated cells was seen by Western blot and immunostaining (FIG.12). It was determined whether the expression of Lys-specific tRNA is used by ANG as a template to degrade HERV-K RNA. qRT-PCR confirmed that fragments of Lys-specific tRNA (LysCTT, LysTTT, pro-AGG) were all decreased within 24 hours of CC-HS treatment of iRPE cells, whereas the expression of another tRNA fragment for a leucine-specific tRNA (LeuTAA) that doesn’t act as a template for HERV-K degradation by ANG, did not decrease in CC-HS treated iRPE cells (FIGS.13A, 13B). Overall, this analysis indicates that HERV-K levels increase in CC-HS treated iRPE via downregulation of ANG expression and downregulation of tRNA fragment required for HERV-K degradation. A gene therapy strategy was developed to reduce HERV-K levels in CC-HS treated iRPE cells. HERV-K is made from multiple loci within the genome and these loci have slight sequence variations between them. Therefore, to develop a gene therapy for HERV-K, RNA made from most of these different loci of HERV-K was targeted. CAS13 is a nuclease that can target RNA using a complementary guide sequence and degrade it. Using bioinformatics analysis, three guide sequences were identified in HERV-K that are used to target HERV-K expression in RPE cells. These sequences were designed against the GAG part of HERV-K mRNA, which is the start of the RNA. Degradation of the start of RNA leads to degradation of the entire RNA. Using bioinformatics analysis, it was discovered three guide sequences in HERV-K that are used to target HERV-K expression in RPE cells (Fig.14A-14B). The sequences selected showed complementarity across multiple HERV-K loci and also showed good consensus for CAS13 based targeting (FIGS.15A-15B). First, it was confirmed that using a lenti-viral based overexpression, high levels of Cas13Rx enzyme were detected in iRPE cells. HA-tagged Cas13Rx was overexpressed using a lentivirus construct. Western blot and immunostaining for the HA-tag confirmed expression of the enzyme in iRPE cells at MOI of 1.0 of the vector. (FIGS.16A-16B).FIGS.17A-17E show Cas13Rx mediated HERV-K knock down reverses complement-induced lipid accumulation. As shown in FIG.17A, to overexpress Cas13Rx in iRPE cells cells were transduced with lentivirus expressing a HA-tagged CAS13Rx under the control of a doxycycline inducible promoter. Seven days of doxycycline treatment induced the expression of CAS13Rx (FIG.16). At this stage, iRPE cells were transduced with another lentiviral construct that expresses one of the three guide RNAs along or together and the control guide RNA. Another 7 days was allowed for guide RNAs to be expressed at high levels and then treated cells with CC-HS. Four days after CC- HS or CI-HS treatment, HERV-K levels were measured in cells and measured monolayer TER and BODIPY® levels in cells. FIG.17B shows a TER graph of CIHS (grey bars) and CCHS (black bars) treated samples that were tranduced with a scrambled guide RNA (NEG) or no guide RNA (Cas13Rx) or guide RNA #2 (FIG.15). Only guide RNA#2 is able to rescue TER downregulated by CCHS treatment. In FIG.17C, the top panel shows digital images of CIHS or CCHS treated iRPE, transduced either with a scrambled control (NEG) or guide RNA#2. CCHS-induced increase in HERV-K expression (compare CIHS NEG samples with CCHS NEG samples) is downregulated by guide RNA 2 against HERV-K. The bottom panel shows digital images of CIHS or CCHS treated iRPE, transduced either with a scrambled control (NEG) or guideRNA#2. CCHS-induced increase in lipid deposits (measured as BODIPY® signal) in CCHS is downregulated by guide RNA 2 against HERV-K. FIG.17D shows quantification of HERV-K levels seen in FIG.17C, the top panel shows guide RNA#2 is able to downregulate HERV-K levels in CCHS treated iRPE cells. FIG.17E shows quantification of BODIPY® levels seen in FIG.17C, bottom panel shows guide RNA#2 is able to downregulate BODIPY in CCHS treated iRPE cells. FIG.18 shows Cas13Rx mediated HERV K knock down reverses complement-induced lipid accumulation by all three guides selected in FIG.15. Digital images of CCHS treated iRPE, transduced either with a scrambled control (NEG) or three guide RNAs #1, 2, 3 alone or in combination. CCHS induced increase in lipid deposits (measured as BODIPY® signal) in CCHS is downregulated by all three guides against HERV-K. Left graph shows quantification of digital imaging data. Additional results are provided in FIG.19. Overall, the data showed that physiological stressors like CC-HS increase the expression of HERV- K endogenous retrovirus in iRPE cells, and that this virus is required and sufficient for the induction of AMD phenotype in iRPE cells. Downregulation of HERV-K transcription by anti-HIV drugs or a gene therapy that targets the expression of HERV-K and other similar endogenous retroviruses can be used to treat AMD and other neuronal degenerative diseases. Furthermore, three target sites were identified for gene therapy targeting of HERV-K.3 Methods This example provides the materials and methods used for the data described in Examples 1 and 2 above. Immunofluorescent or BODIPY®-fluorescent staining: 6–8 week old fully differentiated iRPE monolayers, grown on transwells, were used for all experiments. iRPE cells were treated for 48 h with either 5% CC-HS (S1-LITER, EMD Millipore) or 5% CI-HS (heat-inactivated CC-HS), supplemented in RPE maintenance medium (RPEMM), with daily medium change. For chronic treatment, 0.1% CC-HS (or CI- HS) were added to both apical and basal media of iRPE for up to 6 days. Medium was changed daily. Immunostaining was carried out as described previously (see Sharma et al., Nature Comm.12: 7293, doi.org / 10.1038 / s41467-021-27488-x, 2021). iRPE either prepared as cross-sections or a monolayer on transwell membranes (TWM), were fixed in 4% paraformaldehyde and blocked in immunocytochemistry (ICC) buffer containing 1× phosphate buffered saline (PBS) (10010-023, ThermoFisher), 1% bovine serum albumin (BSA) (160069, MP Biomedicals), 0.25% TWEEN®20 (900-64-5, Affymetrix), 0.25% TRITON® X-100 (9002-64-5, Sigma)) for 1 h at RT. Cells were incubated with primary antibodies diluted in ICC buffer overnight at 4 °C. Primary antibodies against the following proteins were used: APOE (~250 ng / mL; AB947, Millipore, FIG.1), HERV-K (~1 µg / mL, HERM-1811-5, Austral Biologicals, Angiogenin (1ug / ml, AF265, R&D systems, FIGS.13, 17), HA tag ( 2µg / mL, SAB2702217, Sigma Aldrich,), ZO-1 (5 µg / mL; MA3-39100-A488, ThermoFisher). The cells were then washed with ICC buffer and incubated with secondary antibodies diluted in ICC buffer for 1h at RT in the dark. Secondary antibodies include the following: ALEXA FLUOR® 555 goat anti-rabbit (1:200)(5 µg / mL; A21429, ThermoFisher), ALEXA FLUOR® 488 goat anti-rabbit (1:1000) (5 µg / mL; A11078, ThermoFisher), ALEXA FLUOR® 555 goat anti-mouse (1:500) (5 µg / mL; A-21422, ThermoFisher), ALEXA FLUOR® 488 goat anti-mouse (1:200) (5 µg / mL; A32723, ThermoFisher), Hoechst-33542 (1:1000) (H3570, ThermoFisher), and Phalloidin (1:300) (ALEXA FLUOR® 488, A12379, ThermoFisher) or (1:400) (Phalloidin-iFluor 647 Reagent, ab176759, Abcam). The cells were washed with ICC buffer and mounted on a glass slide with Fluoromount-G aqueous mounting medium (0100-01; Southern tech) and a glass coverslip. Samples were imaged using Zeiss 880 confocal microscopes (Carl Zeiss). Images were processed and exported as tiff files using Zenblue3.2 software (Carl Zeiss). Lipid deposits were stained using BODIPY® dye (D3922, or D3835, ThermoFisher, Figure 1 bottom, 9a, 11b bottom, 17C bottom). The cells were fixed in 4% paraformaldehyde for 20 m at RT and washed with 1× PBS. The BODIPY® stock solution was prepared in a concentration of 1 mg / mL (3.8 mM) in DMSO then diluted 1:1000 in 1× PBS to generate the working solution. Bring both the stock and working solutions to RT, then filtering with a 0.22-μm filter before use. Cells were incubated in the working solution for 30 minutes at RT, washed with 1× PBS, mounted, and imaged using the procedure described above. Quantification of lipid droplets (BODIPY® dye) was performed in ImageJ (v1.8.0, Bethesda, USA). For HERV-K, particles were counted with maxima prominence 8000, and for BODIPY® dye, maximaprominence 2900. RNAscope to localize mRNA of HERV-K: Probes and reagents were obtained from Advanced Cell Diagnostics (acdbio.com) except as otherwise stated. Fully matured confluent monolayer of iRPE grown on transwells were treated with CI-HS or CC-HS (5%) for 48 hours. Cells were fixed in 10% formalin. The transwell membrane was punched out and embedded in paraffin and sectioned transversely into 5 uM cross sections in RNA free environment. The assays were performed using RNAscope 2.5 HD Chromogenic Detection Kit (PN332360) according to the manufacturer’s protocol. Briefly, baked slides for 1h at 60C (HybEZ oven), submerged into xylene 2X for 5 minutes, then 100% ETOH 2X for 1 minute with agitation, air dried, proceed with pigment removal in buffer containing (250ul deionized formamide, 4ml water, 250 ul 20x SSC (1X final), 817ul 30% hydrogen peroxide) in a humid chamber about 3-5 inches away from fluorescent tube light, for 20 mins (check regularly for the disappearance of the pigment), wash slides with 1X PBS, dehydrated sequentially through 70% ETOH for 1mi...

Claims

We claim:

1. A method of treating or reducing the risk of developing age-related macular degeneration (AMD) in a subject, comprising: selecting a subject having, or at risk of developing, the AMD; and administering to the subject an effective amount of an agent that inhibits HERV-K, thereby treating or reducing the risk of developing AMD in the subject.

2. The method of claim 1, wherein the method comprises selecting the subject having the AMD; and administering to the subject the effective amount of the agent that inhibits HERV-K, thereby treating the AMD in the subject.

3. The method of claim 1 or claim 2, wherein the subject has wet AMD.

4. The method of claim 1 or claim 2, wherein the subject has dry AMD.

5. The method of any one of claims 1-4, wherein the agent comprises an anti-retroviral agent.

6. The method of claim 5, wherein the anti-retroviral agent is a reverse transcriptase inhibitor, a protease inhibitor, an integrase inhibitor, a virus fusion inhibitor, or a viral entry inhibitor.

7. The method of claim 6, wherein the anti-retroviral agent is a reverse transcriptase inhibitor.

8. The method of claim 7, wherein the reverse transcriptase inhibitor comprises lamivudine, zidovudine, abacavir, tenofovir, a tenofovir prodrug, emtricitabine (FTC), delavirdine, efavirenz, nevirapine or a pharmaceutically acceptable salt thereof.

9. The method of claim 8, wherein the reverse transcriptase inhibitor comprises tenofovir or the tenofovir prodrug, and wherein the tenofovir prodrug is tenofovir disproxil fumerate, tenofovir alafenamide, or a pharmaceutically acceptable salt thereof.

10. The method of any one of claims 1-9, wherein the method comprises administering to the subject a) an effective amount of FTC, or a pharmaceutically acceptable salt thereof, and b) an effective amount of tenofovir disoproxil fumarate (TDF) and / or tenofovir alafenamide (TAF), or a pharmaceutically acceptable salt thereof.

11. The method of any one of claims 5- comprising administering to the subject an effective amount of a pharmacoenhancer.

12. The method of claim 11, wherein the pharmacoenhancer is cobistat.

13. The method of any one of claims 5-12, further comprising administering to the subject an effective amount of elvitegravir (EVG).

14. The method of any one of claims 7-9, further comprising administering to the subject a second antiretroviral agent, wherein the antiretroviral agent is a protease inhibitor.

15. The method of claim 14, wherein the protease inhibitor is darunavir.

16. The method of any one of claims 1-15, further comprising administering to the subject an effective amount of an additional agent, wherein the additional agent is metformin hydrochloride or L-745,870 trihydrochloride.

17. The method of any one of claims 1-16, wherein the agent comprises an inhibitory oligonucleotide or an inhibitory peptide.

18. The method of claim 17, wherein the inhibitory oligonucleotide is an antisense RNA, a small inhibitory RNA, a ribozyme, or a short hairpin (sh)RNA.

19. The method of any one of claims 1-18, wherein the agent comprises a CRISPR / Cas13 system.

20. The method of claim 19, wherein the CRISPR / Cas13 system comprises a guide RNA (gRNA) that specifically hybridizes to a) an RNA encoding glycosaminoglycan (Gag) protein of HERV-K or a nucleic acid molecule encoding the gRNA; b) an RNA encoding polymerase (Pol) protein of HERV-K or a nucleic acid molecule encoding the gRNA; or c) an RNA encoding envelope (Env) protein of HERV-K or a nucleic acid molecule encoding the gRNA.

21. The method of claim 20, wherein the gRNA comprises one or more of SEQ ID NOs: 1-3.

22. The method of any one of claims 19-21, wherein the CRISPR / Cas13 system comprises a lentiviral vector encoding a Cas13 protein.

23. The method of any one of claims 19- wherein the CRISPR / Cas13 system comprises an adenoviral vector, a lentivirus vector, a vector, or nanoparticles.

24. The method of claim 22 or 23, wherein the lentiviral vector, the adenoviral vector, or the baculovirus vector, or nanoparticles comprises an inducible, constitutive or tissue-specific promoter operably linked to a nucleic acid molecule encoding the Cas13 protein.

25. The method of claim 24, wherein the a) the constitutive promoter is CMV; b) the inducible promoter is a doxycycline or other inducible promoter; or c) the tissue specific promoter is a retinal pigment epithelial cell specific promoter.

26. The method of any one of claims 19-25, wherein the CRISPR / Cas13 system comprises a ribonucleoprotein complex comprising a Cas13Rx protein and the gRNA.

27. The method of any one of claims 19-26, wherein the Cas13 is Cas13a, Cas13b, Cas13c, Cas13Rx, Cas13x, or Cas13y.

28. The method of any one of claims 1-27, wherein the agent comprises an antibody that specifically binds a Gag, Pol, or Env of HERV-K, or an antigen binding fragment thereof.

29. The method of any one of claims 1-28, wherein administering to the subject an effective amount of an agent that inhibits HERV-K, comprises administering the agent that inhibits HERV-K to an eye of the subject.

30. A non-naturally occurring or engineered clustered regularly interspaced short palindromic repeats (CRISPR)-associated (Cas) system for targeting HERV-K, comprising: (a) at least one Cas13 protein, or a nucleic acid molecule encoding the at least one Cas13 protein; and (b) at least one CRISPR-Cas system guide RNA (gRNA) comprising SEQ ID NO: 1, 2, and / or 3, which hybridizes with HERV-K RNA molecules, or at least one nucleic acid molecule encoding the at least one gRNA, whereby the Cas13 protein forms a complex with the at least one gRNA, wherein the at least one gRNA directs the complex to HERV-K RNA molecules.

31. A ribonucleoprotein (RNP) complex, comprising: at least one Cas13 protein; and one or more guide RNAs, wherein at least one of the one or more guide RNAs comprisesSEQ ID NO: 1, 2, and / or 3.

32. An isolated cell comprising the system of claim 30 or the RNP complex of claim 31.

33. The isolated cell of claim 32, wherein the isolated cell is a retinal cell.

34. The isolated cell of claim 33, wherein the retinal cell is as a retinal pigment epithelial cell, a photoreceptor cell, or a choroidal cell.

35. A method of treating or reducing the risk of developing age-related macular degeneration (AMD) in a subject, comprising: selecting a subject having, or at risk of developing, the AMD; and administering to the subject an effective amount of an agent that increases angiogenin (ANG) activity, thereby treating or reducing the risk of developing AMD in the subject.

36. The method of claim 35, wherein the method comprises: selecting the subject having the AMD; and administering to the subject the effective amount of the agent that increases ANG activity, thereby treating the AMD in the subject.

37. The method of claim 35 or claim 36, wherein the subject has wet AMD.

38. The method of claim 35 or claim 36, wherein the subject has dry AMD.

39. The method of any one of claims 35-38, wherein the agent comprises ANG or a nucleic acid molecule encoding ANG.

40. The method of claim 39, wherein the ANG comprises a) an amino acid sequence 95% identical to SEQ ID NO: 11; or b) the amino acid sequence of SEQ ID NO:

11.

41. The method of claim 39 or 40, wherein the agent comprises the nucleic acid molecule encoding ANG.

42. The method of claim 41, comprising administering to the subject an expression vector comprising the nucleic acid molecule encoding ANG.

43. The method of claim 42, wherein the vector is an adenovirus vector, a lentiviral vector, or an adeno-associated viral vector.

44. The method of claim 42 or 43, wherein the expression vector comprises a retinal pigment epithelial cell specific promoter operably linked to the nucleic acid molecule encoding ANG.

45. The method of claim 44, wherein the retinal pigment epithelial cell specific promoter is a RPE65, BEST1, DCT, TYR, or a TYRP1 promoter.

46. The method of claim 42 or 43, wherein the expression vector comprises a constitutive promoter operably linked to the nucleic acid molecule encoding ANG.

47. The method of claim 46, wherein the constitutive promoter is a human β-actin promoter, human elongation factor-1α promoter, β-actin promoter, simian virus 40 promoter, or a herpes simplex virus thymidine kinase promoter.

48. The method of any one of claims 35-47, wherein the agent comprises a CRISPR / Cas9 system that increases the expression of ANG in the subject.

49. The method of any one of claims 35-38, wherein the agent comprises a small molecule that increases ANG activity.

50. The method of claim 49, wherein the small molecule is L-minosine, muscone, an opioid, DMOG or ML228.

51. The method of any one of claims 35-50, wherein the agent comprises a tRNA fragment complementary to HERV-K, or a nucleic acid molecule encoding the tRNA fragment.

52. The method of claim 51, wherein the tRNA fragment comprises GCCCCACGTTGGGCGCCA (SEQ ID NO: 12) or GTCCCTGTTCGGGCGCCA (SEQ ID NO: 13).

53. The method of claim 51 or 52, wherein the agent comprises the nucleic acid molecule encoding the tRNA fragment.

54. The method of claim 53, comprising administering to the subject an expression vector comprising the nucleic acid molecule encoding the tRNA fragment.

55. The method of claim 54, wherein the vector is an adenovirus vector, a lentiviral vector, or an adeno-associated viral vector.

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