HV1H2:POL

Species (Taxon ID)	Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)(HIV-1). (11706)
Gene Name(s)	gag-pol
Protein Name(s)	Gag-Pol polyprotein Pr160Gag-Pol Matrix protein p17 MA Capsid protein p24 CA Spacer peptide p2 Nucleocapsid protein p7 NC Transframe peptide TF p6-pol p6* Protease PR Retropepsin Reverse transcriptase/ribonuclease H Exoribonuclease H p66 RT p51 RT p15 Integrase IN
External Links
UniProt	P04585
EMBL	K03455 AF033819
RefSeq	NP_057849.4
PDB	1A30 1BV7 1BV9 1BVE 1BVG 1BWA 1BWB 1C0T 1C0U 1C1B 1C1C 1DMP 1DTQ 1DTT 1E6J 1EP4 1ESK 1EX4 1EXQ 1FB7 1FK9 1FKO 1FKP 1G6L 1HIV 1HVH 1HVR 1HWR 1HXB 1JKH 1JLA 1JLB 1JLC 1JLE 1JLF 1JLG 1JLQ 1KLM 1LV1 1LW0 1LW2 1LWC 1LWE 1LWF 1NCP 1O1W 1ODW 1ODY 1QBR 1QBS 1QBT 1QBU 1REV 1RT1 1RT2 1RT3 1RT4 1RT5 1RT6 1RT7 1RTD 1RTH 1RTI 1RTJ 1S1T 1S1U 1S1V 1S1W 1S1X 1T05 1TAM 1TKT 1TKX 1TKZ 1TL1 1TL3 1VRT 1VRU 2HND 2HNY 2HNZ 2KOD 2NPH 2OPP 2OPQ 2OPR 2OPS 2RF2 2RKI 2WHH 2WOM 2WON 2YNF 2YNG 2YNH 2YNI 3AO2 3C6T 3C6U 3DI6 3DLE 3DLG 3DM2 3DMJ 3DOK 3DOL 3DOX 3DRP 3DRR 3DRS 3DYA 3E01 3FFI 3I0R 3I0S 3KJV 3KK1 3KK2 3KK3 3KT2 3KT5 3LAK 3LAL 3LAM 3LAN 3LP0 3LP1 3LP2 3M8P 3M8Q 3MEC 3MED 3MEE 3MEG 3MIM 3N3I 3NBP 3PHV 3QIN 3QIO 3QIP 3T19 3T1A 3TAM 4B3O 4B3P 4B3Q 4I7F 4KSE 4KV8 4NCG 4QLH
PDBsum	1A30 1BV7 1BV9 1BVE 1BVG 1BWA 1BWB 1C0T 1C0U 1C1B 1C1C 1DMP 1DTQ 1DTT 1E6J 1EP4 1ESK 1EX4 1EXQ 1FB7 1FK9 1FKO 1FKP 1G6L 1HIV 1HVH 1HVR 1HWR 1HXB 1JKH 1JLA 1JLB 1JLC 1JLE 1JLF 1JLG 1JLQ 1KLM 1LV1 1LW0 1LW2 1LWC 1LWE 1LWF 1NCP 1O1W 1ODW 1ODY 1QBR 1QBS 1QBT 1QBU 1REV 1RT1 1RT2 1RT3 1RT4 1RT5 1RT6 1RT7 1RTD 1RTH 1RTI 1RTJ 1S1T 1S1U 1S1V 1S1W 1S1X 1T05 1TAM 1TKT 1TKX 1TKZ 1TL1 1TL3 1VRT 1VRU 2HND 2HNY 2HNZ 2KOD 2NPH 2OPP 2OPQ 2OPR 2OPS 2RF2 2RKI 2WHH 2WOM 2WON 2YNF 2YNG 2YNH 2YNI 3AO2 3C6T 3C6U 3DI6 3DLE 3DLG 3DM2 3DMJ 3DOK 3DOL 3DOX 3DRP 3DRR 3DRS 3DYA 3E01 3FFI 3I0R 3I0S 3KJV 3KK1 3KK2 3KK3 3KT2 3KT5 3LAK 3LAL 3LAM 3LAN 3LP0 3LP1 3LP2 3M8P 3M8Q 3MEC 3MED 3MEE 3MEG 3MIM 3N3I 3NBP 3PHV 3QIN 3QIO 3QIP 3T19 3T1A 3TAM 4B3O 4B3P 4B3Q 4I7F 4KSE 4KV8 4NCG 4QLH
ProteinModelPortal	P04585
SMR	P04585
IntAct	P04585
MINT	MINT-111862
BindingDB	P04585
GeneID	155348
Reactome	REACT_6266 REACT_6359 REACT_6818 REACT_6866 REACT_6903 REACT_6918 REACT_6965 REACT_7991 REACT_8990 REACT_9037 REACT_9055 REACT_9058 REACT_9406
SABIO-RK	P04585
EvolutionaryTrace	P04585
Proteomes	UP000002241
GO	GO:0030430 GO:0042025 GO:0020002 GO:0016020 GO:0019013 GO:0004190 GO:0003677 GO:0003887 GO:0004533 GO:0042802 GO:0003723 GO:0003964 GO:0004523 GO:0005198 GO:0008270 GO:0015074 GO:0006310 GO:0030260 GO:0075713 GO:0039651 GO:0006278 GO:0039657 GO:0019061 GO:0046718 GO:0019058 GO:0075732 GO:0016032 GO:0019076 GO:0019068
Gene3D	1.10.10.200 1.10.1200.30 1.10.150.90 1.10.375.10 2.30.30.10 2.40.70.10 3.30.420.10 4.10.60.10
InterPro	IPR001969 IPR000721 IPR001037 IPR001584 IPR017856 IPR003308 IPR000071 IPR012344 IPR018061 IPR001995 IPR021109 IPR008916 IPR008919 IPR010999 IPR012337 IPR002156 IPR000477 IPR010659 IPR010661 IPR001878
Pfam	PF00540 PF00607 PF00552 PF02022 PF00075 PF00665 PF00077 PF00078 PF06815 PF06817 PF00098
PRINTS	PR00234
SMART	SM00343
SUPFAM	SSF46919 SSF47353 SSF47836 SSF47943 SSF50122 SSF50630 SSF53098 SSF57756
PROSITE	PS50175 PS00141 PS50994 PS51027 PS50879 PS50878 PS50158 PS50876

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0008270	zinc ion binding	PMID:1639074^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22804908^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04585	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21156026^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04585	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20227411^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04585	F	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004519	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004518	P	Seeded From UniProt	complete
involved_in	GO:0090502	RNA phosphodiester bond hydrolysis, endonucleolytic	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004523	P	Seeded From UniProt	complete
involved_in	GO:0090503	RNA phosphodiester bond hydrolysis, exonucleolytic	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004533	P	Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001037 InterPro:IPR001878 InterPro:IPR002156 InterPro:IPR036397 InterPro:IPR036862 InterPro:IPR036875	F	Seeded From UniProt	complete
enables	GO:0003964	RNA-directed DNA polymerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010659 InterPro:IPR010661	F	Seeded From UniProt	complete
enables	GO:0004190	aspartic-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001969 InterPro:IPR001995	F	Seeded From UniProt	complete
enables	GO:0004523	RNA-DNA hybrid ribonuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002156	F	Seeded From UniProt	complete
enables	GO:0005198	structural molecule activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000071	F	Seeded From UniProt	complete
involved_in	GO:0006278	RNA-dependent DNA biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010659 InterPro:IPR010661	P	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001969 InterPro:IPR001995	P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001878 InterPro:IPR003308 InterPro:IPR036875	F	Seeded From UniProt	complete
involved_in	GO:0015074	DNA integration	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001584	P	Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000721 InterPro:IPR008919	P	Seeded From UniProt	complete
enables	GO:0004533	exoribonuclease H activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.13.2	F	Seeded From UniProt	complete
enables	GO:0003887	DNA-directed DNA polymerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.7.7	F	Seeded From UniProt	complete
enables	GO:0003964	RNA-directed DNA polymerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.7.49	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:2162350^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19914170^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19914170^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04585:PRO_0000042440	F	Seeded From UniProt	complete
involved_in	GO:0019072	viral genome packaging	PMID:18343475^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0075713	establishment of integrated proviral latency	Reactome:R-HSA-175567 Reactome:R-HSA-162592	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051169	nuclear transport	Reactome:R-HSA-162590	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030260	entry into host cell	Reactome:R-HSA-173107	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019068	virion assembly	Reactome:R-HSA-175474	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019064	fusion of virus membrane with host plasma membrane	Reactome:R-HSA-164524	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019061	uncoating of virus	Reactome:R-HSA-173771 Reactome:R-HSA-162585	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019058	viral life cycle	Reactome:R-HSA-162588	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008907	integrase activity	Reactome:R-HSA-164523	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	Reactome:R-HSA-3139027	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006278	RNA-dependent DNA biosynthetic process	Reactome:R-HSA-182876 Reactome:R-HSA-164527 Reactome:R-HSA-164525 Reactome:R-HSA-164516	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0075732	viral penetration into host nucleus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1163	P	Seeded From UniProt	complete
involved_in	GO:0039651	induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1073	P	Seeded From UniProt	complete
involved_in	GO:0044826	viral genome integration into host DNA	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1179	P	Seeded From UniProt	complete
part_of	GO:0020002	host cell plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1032 UniProtKB-SubCell:SL-0375	C	Seeded From UniProt	complete
part_of	GO:0033644	host cell membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1043	C	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
enables	GO:0004190	aspartic-type endopeptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0064	F	Seeded From UniProt	complete
enables	GO:0008289	lipid binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0446	F	Seeded From UniProt	complete
enables	GO:0003887	DNA-directed DNA polymerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0239	F	Seeded From UniProt	complete
involved_in	GO:0039526	modulation by virus of host apoptotic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1119	P	Seeded From UniProt	complete
part_of	GO:0044174	host cell endosome	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1039	C	Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1035 UniProtKB-SubCell:SL-0381	C	Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	P	Seeded From UniProt	complete
involved_in	GO:0039657	suppression by virus of host gene expression	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1190	P	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	F	Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F	Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0255	F	Seeded From UniProt	complete
involved_in	GO:0006310	DNA recombination	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0233	P	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
involved_in	GO:0075713	establishment of integrated proviral latency	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1179	P	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P	Seeded From UniProt	complete
part_of	GO:0019012	virion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0946 UniProtKB-SubCell:SL-0274	C	Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0540	F	Seeded From UniProt	complete
involved_in	GO:0046718	viral entry into host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1160	P	Seeded From UniProt	complete
part_of	GO:0042025	host cell nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1048 UniProtKB-SubCell:SL-0414	C	Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
enables	GO:0016779	nucleotidyltransferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0548	F	Seeded From UniProt	complete
part_of	GO:0019028	viral capsid	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0167	C	Seeded From UniProt	complete
enables	GO:0003964	RNA-directed DNA polymerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0695	F	Seeded From UniProt	complete
involved_in	GO:0015074	DNA integration	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0229	P	Seeded From UniProt	complete
part_of	GO:0019013	viral nucleocapsid	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0543	C	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F	Seeded From UniProt	complete
part_of	GO:0055036	virion membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0275	C	Seeded From UniProt	complete
part_of	GO:0072494	host multivesicular body	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0453	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Morellet, N et al. (1992) Determination of the structure of the nucleocapsid protein NCp7 from the human immunodeficiency virus type 1 by 1H NMR. EMBO J. 11 3059-65 PubMed GONUTS page
↑ Matúz, K et al. (2012) Inhibition of XMRV and HIV-1 proteases by pepstatin A and acetyl-pepstatin. FEBS J. 279 3276-86 PubMed GONUTS page
↑ Levin, A et al. (2011) Peptides that bind the HIV-1 integrase and modulate its enzymatic activity--kinetic studies and mode of action. FEBS J. 278 316-30 PubMed GONUTS page
↑ Wielens, J et al. (2010) Crystal structure of the HIV-1 integrase core domain in complex with sucrose reveals details of an allosteric inhibitory binding site. FEBS Lett. 584 1455-62 PubMed GONUTS page
↑ Weber, IT (1990) Comparison of the crystal structures and intersubunit interactions of human immunodeficiency and Rous sarcoma virus proteases. J. Biol. Chem. 265 10492-6 PubMed GONUTS page
↑ ^6.0 ^6.1 Byeon, IJ et al. (2009) Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell 139 780-90 PubMed GONUTS page
↑ Kafaie, J et al. (2008) Mapping of nucleocapsid residues important for HIV-1 genomic RNA dimerization and packaging. Virology 375 592-610 PubMed GONUTS page

[PMID:1639074-1] Morellet, N et al. (1992) Determination of the structure of the nucleocapsid protein NCp7 from the human immunodeficiency virus type 1 by 1H NMR. EMBO J. 11 3059-65 PubMed GONUTS page

[PMID:22804908-2] Matúz, K et al. (2012) Inhibition of XMRV and HIV-1 proteases by pepstatin A and acetyl-pepstatin. FEBS J. 279 3276-86 PubMed GONUTS page

[PMID:21156026-3] Levin, A et al. (2011) Peptides that bind the HIV-1 integrase and modulate its enzymatic activity--kinetic studies and mode of action. FEBS J. 278 316-30 PubMed GONUTS page

[PMID:20227411-4] Wielens, J et al. (2010) Crystal structure of the HIV-1 integrase core domain in complex with sucrose reveals details of an allosteric inhibitory binding site. FEBS Lett. 584 1455-62 PubMed GONUTS page

[PMID:2162350-5] Weber, IT (1990) Comparison of the crystal structures and intersubunit interactions of human immunodeficiency and Rous sarcoma virus proteases. J. Biol. Chem. 265 10492-6 PubMed GONUTS page

[PMID:19914170-6] 6.0 ^6.1 Byeon, IJ et al. (2009) Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell 139 780-90 PubMed GONUTS page

[PMID:18343475-7] Kafaie, J et al. (2008) Mapping of nucleocapsid residues important for HIV-1 genomic RNA dimerization and packaging. Virology 375 592-610 PubMed GONUTS page

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HV1H2:POL

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