The Interaction between HIV-1 Gag and APOBEC3G

APOBEC3G, a member of an RNA/DNA cytidine deaminase superfamily, has been identified as a cellular inhibitor of HIV-1 infectivity, possibly through the dC to dU deamination of the first minus strand cDNA synthesized during reverse transcription. Virions incorporate APOBEC3G during viral assembly in non-permissive cells, and this incorporation is inhibited by the viral protein Vif. The mechanism of APOBEC3G incorporation into HIV-1 is examined in this report. In the absence of Vif, cytoplasmic APOBEC3G becomes membrane-bound in cells expressing HIV-1 Gag, and its incorporation into Gag viral-like particles (VLPs) is proportional to the amount of APOBEC3G expressed in the cell. The expression of Vif, or mutant Gag unable to bind to membrane, prevents the APOBEC3G association with membrane. HIV-1 Gag alone among viral proteins is sufficient for packaging of APOBEC3G into Gag VLPs, and this incorporation requires the presence of Gag nucleocapsid. The presence of amino acids 104-156 in APOBEC3G, located in the linker region between two zinc coordination motifs, is also required for its incorporation into Gag VLPs. Evidence against an RNA bridge facilitating the Gag/APOBEC3G interaction includes data indicating that 1) the incorporation of APOBEC3G occurs independently of viral genomic RNA, 2) a Gag/APOBEC3G complex is immunoprecipitated from cell lysate after RNase treatment, and 3) the zinc coordination motif, rather than the regions flanking this motif, have been implicated in RNA binding in another family member, APOBEC1. APOBEC3G, a member of an RNA/DNA cytidine deaminase superfamily, has been identified as a cellular inhibitor of HIV-1 infectivity, possibly through the dC to dU deamination of the first minus strand cDNA synthesized during reverse transcription. Virions incorporate APOBEC3G during viral assembly in non-permissive cells, and this incorporation is inhibited by the viral protein Vif. The mechanism of APOBEC3G incorporation into HIV-1 is examined in this report. In the absence of Vif, cytoplasmic APOBEC3G becomes membrane-bound in cells expressing HIV-1 Gag, and its incorporation into Gag viral-like particles (VLPs) is proportional to the amount of APOBEC3G expressed in the cell. The expression of Vif, or mutant Gag unable to bind to membrane, prevents the APOBEC3G association with membrane. HIV-1 Gag alone among viral proteins is sufficient for packaging of APOBEC3G into Gag VLPs, and this incorporation requires the presence of Gag nucleocapsid. The presence of amino acids 104-156 in APOBEC3G, located in the linker region between two zinc coordination motifs, is also required for its incorporation into Gag VLPs. Evidence against an RNA bridge facilitating the Gag/APOBEC3G interaction includes data indicating that 1) the incorporation of APOBEC3G occurs independently of viral genomic RNA, 2) a Gag/APOBEC3G complex is immunoprecipitated from cell lysate after RNase treatment, and 3) the zinc coordination motif, rather than the regions flanking this motif, have been implicated in RNA binding in another family member, APOBEC1. Vif 1The abbreviations used are: Vif, viral infectivity factor; HIV-1, human immunodeficiency virus type 1; BH10P-, HIV-1 containing an inactive viral protease; Gag, HIV-1 precursor protein containing sequences coding for HIV-1 structural proteins; MA, matrix; CA, capsid; NC, nucleocapsid; p6, p6 protein; VLP, viral-like particle; HA, hemagglutinin epitope. (virion infectivity factor) is a 190-240-amino acid protein that is encoded by all of the lentiviruses except for equine infectious anemia virus (1Simon J.H. Gaddis N.C. Fouchier R.A. Malim M.H. Nat. Med. 1998; 4: 1397-1400Crossref PubMed Scopus (246) Google Scholar, 2Madani N. Kabat D. J. Virol. 1998; 72: 10251-10255Crossref PubMed Google Scholar, 3Fisher A.G. Ensoli B. Ivanoff L. Chamberlain M. Petteway S. Ratner L. Gallo R.C. Wong-Staal F. Science. 1987; 237: 888-893Crossref PubMed Scopus (277) Google Scholar, 4Gibbs J.S. Regier D.A. Desrosiers R.C. AIDS Res. Hum. Retroviruses. 1994; 10: 607-616Crossref PubMed Scopus (61) Google Scholar, 5Gabuzda D.H. Lawrence K. Langhoff E. Terwilliger E. Dorfman T. Haseltine W.A. Sodroski J. J. Virol. 1992; 66: 6489-6495Crossref PubMed Google Scholar, 6Kan N.C. Franchini G. Wong-Staal F. DuBois G.C. Robey W.G. Lautenberger J.A. Papas T.S. Science. 1986; 231: 1553-1555Crossref PubMed Scopus (93) Google Scholar, 7Lee T.H. Coligan J.E. Allan J.S. McLane M.F. Groopman J.E. Essex M. Science. 1986; 231: 1546-1549Crossref PubMed Scopus (89) Google Scholar, 8Dettenhofer M. Cen S. Carlson B.A. Kleiman L. Yu X.F. J. Virol. 2000; 74: 8938-8945Crossref PubMed Scopus (104) Google Scholar, 9Simon J.H. Malim M.H. J. Virol. 1996; 70: 5297-5305Crossref PubMed Google Scholar, 10Sodroski J. Goh W.C. Rosen C. Tartar A. Portetelle D. Burny A. Haseltine W. Science. 1986; 231: 1549-1553Crossref PubMed Scopus (164) Google Scholar, 11Strebel K. Daugherty D. Clouse K. Cohen D. Folks T. Martin M.A. Nature. 1987; 328: 728-730Crossref PubMed Scopus (348) Google Scholar, 12von Schwedler U. Song J. Aiken C. Trono D. J. Virol. 1993; 67: 4945-4955Crossref PubMed Google Scholar). Vif is required for HIV-1 to replicate in certain “non-permissive” cell types, such as primary T lymphocytes, macrophages, and some of T-cell lines, including H9, but is not required in other “permissive” cell types, such as SupT1 and Jurkat cells (3Fisher A.G. Ensoli B. Ivanoff L. Chamberlain M. Petteway S. Ratner L. Gallo R.C. Wong-Staal F. Science. 1987; 237: 888-893Crossref PubMed Scopus (277) Google Scholar, 5Gabuzda D.H. Lawrence K. Langhoff E. Terwilliger E. Dorfman T. Haseltine W.A. Sodroski J. J. Virol. 1992; 66: 6489-6495Crossref PubMed Google Scholar, 11Strebel K. Daugherty D. Clouse K. Cohen D. Folks T. Martin M.A. Nature. 1987; 328: 728-730Crossref PubMed Scopus (348) Google Scholar). The ability of Vif-negative viruses to replicate in target cells is determined by the cell producing the virus (5Gabuzda D.H. Lawrence K. Langhoff E. Terwilliger E. Dorfman T. Haseltine W.A. Sodroski J. J. Virol. 1992; 66: 6489-6495Crossref PubMed Google Scholar, 12von Schwedler U. Song J. Aiken C. Trono D. J. Virol. 1993; 67: 4945-4955Crossref PubMed Google Scholar). Thus, Vif-deficient viruses produced from non-permissive cells are impaired in their ability to replicate in target cells. Non-permissive cells have been found to contain a protein called APOBEC3G (also known as CEM-15), which prevents HIV-1 replication in the absence of Vif (13Sheehy A.M. Gaddis N.C. Choi J.D. Malim M.H. Nature. 2002; 418: 646-650Crossref PubMed Scopus (1922) Google Scholar). APOBEC3G belongs to an APOBEC superfamily containing at least 10 members, which share a cytidine deaminase motif (14Jarmuz A. Chester A. Bayliss J. Gisbourne J. Dunham I. Scott J. Navaratnam N. Genomics. 2002; 79: 285-296Crossref PubMed Scopus (593) Google Scholar). These include APOBEC1 and activation-induced cytidine deaminase (AID), which have been shown to deaminate C in RNA (14Jarmuz A. Chester A. Bayliss J. Gisbourne J. Dunham I. Scott J. Navaratnam N. Genomics. 2002; 79: 285-296Crossref PubMed Scopus (593) Google Scholar) and DNA (15Neuberger M.S. Harris R.S. Di Noia J. Petersen-Mahrt S.K. Trends Biochem. Sci. 2003; 28: 305-312Abstract Full Text Full Text PDF PubMed Scopus (205) Google Scholar), respectively. It is not known if APOBEC3G can edit RNA, but several reports suggest that the anti-HIV-1 activity of this protein stems from its ability to form dU by deaminating dC in the first minus strand cDNA produced during HIV-1 reverse transcription (16Mangeat B. Turelli P. Caron G. Friedli M. Perrin L. Trono D. Nature. 2003; 424: 99-103Crossref PubMed Scopus (1252) Google Scholar, 17Zhang H. Yang B. Pomerantz C. L. Nature. 2003; 424: PubMed Scopus Google Scholar, R.S. A.M. Petersen-Mahrt S.K. M.S. Malim M.H. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar, D. F. F. Science. 2003; PubMed Scopus Google Scholar). Vif-negative HIV-1 produced in non-permissive cells APOBEC3G during assembly not (13Sheehy A.M. Gaddis N.C. Choi J.D. Malim M.H. Nature. 2002; 418: 646-650Crossref PubMed Scopus (1922) Google Scholar, B. Turelli P. Caron G. Friedli M. Perrin L. Trono D. Nature. 2003; 424: 99-103Crossref PubMed Scopus (1252) Google Scholar). cDNA is in the target cell with Vif-negative and the minus strand cDNA of the to for cDNA by the DNA The coding strand found in cDNA also an in to that also to the activity of APOBEC3G through mutant coding regions for viral Vif is to bind to APOBEC3G D. B. F. B. C. H. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar) and can the cellular expression of APOBEC3G and its incorporation into S. M.A. E. A. K. J. Virol. 2003; PubMed Scopus Google Scholar). The in cellular expression has been to of APOBEC3G and its in the by Vif K. C. W. W.C. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar), and that Vif with cytoplasmic APOBEC3G as of a in the of APOBEC3G and its Yu B. K. W. P. Yu X.F. Science. 2003; PubMed Scopus Google Scholar). to the human APOBEC superfamily are also encoded by the and D. B. F. B. C. H. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar), and a amino acid and structural with human APOBEC3G (13Sheehy A.M. Gaddis N.C. Choi J.D. Malim M.H. Nature. 2002; 418: 646-650Crossref PubMed Scopus (1922) Google Scholar, J.E. Trends 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). Vif is not in the and Vif from HIV-1 is unable to of APOBEC into HIV-1, packaging in of HIV-1 replication D. B. F. B. C. H. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). APOBEC is into to have the replication of this virus (16Mangeat B. Turelli P. Caron G. Friedli M. Perrin L. Trono D. Nature. 2003; 424: 99-103Crossref PubMed Scopus (1252) Google Scholar, R.S. A.M. Petersen-Mahrt S.K. M.S. Malim M.H. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar, D. B. F. B. C. H. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). the other the human APOBEC3G can the infectivity of including and immunodeficiency and equine infectious anemia virus (16Mangeat B. Turelli P. Caron G. Friedli M. Perrin L. Trono D. Nature. 2003; 424: 99-103Crossref PubMed Scopus (1252) Google Scholar, R.S. A.M. Petersen-Mahrt S.K. M.S. Malim M.H. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar), at than for The mechanism by which APOBEC3G is into Vif-negative HIV-1 is not In this data that the incorporation of APOBEC3G into HIV-1 requires sequences found between the two zinc coordination found in this protein acids and the in HIV-1 Gag alone among viral proteins is sufficient to APOBEC3G into Gag viral-like particles Evidence is also that suggest that an RNA bridge between two is not in facilitating the Gag/APOBEC3G is a virus that HIV-1 DNA containing an inactive viral and a from E. of at the from to which prevents during the of Gag protein and viruses that contain Gag but not S. M. J. F. Kleiman L. J. Virol. PubMed Scopus Google Scholar). a HIV-1 in which the has been with a M.A. B. J. Virol. 2000; 74: PubMed Scopus Google Scholar). and by a after of the Vif at a with the of and The human APOBEC3G cDNA from by reverse the of and The cDNA into the which human APOBEC3G with a at the C mutant APOBEC3G, this cDNA and with and in of the These into the and of the used the and The expressing and mutant APOBEC3G into cells. The which the HIV-1 Gag have been for and a from G. of J. Virol. PubMed Scopus Google Scholar). the or Gag and with and in of the These into the and of The used to and and cells in of and of the of cells to the from by in a at for The viral by in a at for through a The of virus and in in a at for RNA and cellular and viral RNA and the amount of HIV-1 viral RNA by as M. J. A. Cohen E. M. B. Kleiman L. J. Virol. 1993; 67: PubMed Google Scholar). known of used as a and of cellular or viral RNA and with a DNA for the from to of the HIV-1 in The of HIV-1 viral RNA and the amount of viral RNA in cell and virus and viral proteins with The cell and viral by by with that are with HIV-1 and or with of AIDS and of proteins by as and and and from in cells from and in of at for The used as the of immunoprecipitated Gag/APOBEC3G of protein with of for at by the of protein for a of cell of lysate protein used for from for the lysate of lysate protein used for protein determined by the The with and with the of and and the for to the the In the and RNase the cell with of or RNase the as A. M.A. Kleiman L. J. Virol. 2002; PubMed Scopus Google Scholar). and at by in with The cell at for to and cells. of the into of of in of the and of of the The at in a at and with 10 of and at at for The from in and by and of APOBEC3G into Gag cells with a coding for human APOBEC3G containing a and containing or mutant HIV-1 and contain a after the of the Vif and an inactive viral a HIV-1 Gag for in cells J. Virol. PubMed Scopus Google and HIV-1 Gag and Gag are produced S. M. J. F. Kleiman L. J. Virol. PubMed Scopus Google Scholar). The cell of cells by and as Vif is in cells with In cells producing or Gag Vif, APOBEC3G is in cells producing APOBEC3G is in the The viruses produced from cells by and APOBEC3G is in is found in not expressing Vif. These also that Gag alone is sufficient among the viral proteins for facilitating APOBEC3G also of a presence of APOBEC3G in the and in in the presence of Vif and this has been shown to to the of APOBEC3G and by the K. C. W. W.C. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar, Yu B. K. W. P. Yu X.F. Science. 2003; PubMed Scopus Google Scholar, M. Kabat D. Nat. Med. 2003; PubMed Scopus Google Scholar, A.M. Gaddis N.C. Malim M.H. Nat. Med. 2003; PubMed Scopus Google Scholar, B. Yu K. Yu Yu X.F. J. Virol. PubMed Scopus Google Scholar). as coding sequences of Gag, the RNA coding for has the and of the viral RNA with a is not that this RNA, which viral packaging that APOBEC3G incorporation into particles occurs independently of viral genomic RNA RNA from cells with APOBEC3G and or and from the produced from cells. in the cells and viruses by a DNA for the p6 coding which is in and The for viral in the and viral in is in cytoplasmic expression of viral genomic RNA is in cells expressing the genomic in is to of that found in incorporation of viral RNA APOBEC3G incorporation into indicating that APOBEC3G incorporation into occurs independently of viral RNA The Gag for the of of Gag used to the motif Gag in the incorporation of APOBEC3G into These are shown in cells with APOBEC3G and or mutant Gag and cells in of cell with or The first cells with Gag expressed at in the except for the Gag has NC, and p6 from the C and is expressed than of mutant Gag are impaired in their ability to form particles to the absence of or have the interaction between APOBEC3G and mutant Gag to cellular The presence of Gag and APOBEC3G in the cell lysate first by with and The at the of to the are for all mutant Gag except for which a expression of APOBEC3G in cell lysate immunoprecipitated by and the presence of Gag and APOBEC3G in the by and The at the of to the in the association of Gag with APOBEC3G with of the sequences and a with of the sequences a of Gag, which also in a in the interaction of Gag with APOBEC3G, the expression of this mutant Gag is in the cell lysate than for Gag in which and the region of the have been also interaction with These data suggest that sequences Gag are for the interaction between APOBEC3G and The in the APOBEC3G found with of the sequences an the in Gag S. J. Virol. PubMed Google Scholar) and of the APOBEC including APOBEC3G (14Jarmuz A. Chester A. Bayliss J. Gisbourne J. Dunham I. Scott J. Navaratnam N. Genomics. 2002; 79: 285-296Crossref PubMed Scopus (593) Google Scholar), can bind to RNA, that the interaction between Gag and APOBEC3G by an RNA the data in suggest that an RNA bridge is not cells with and APOBEC3G, and the cell to RNase or treatment, by with or respectively. The by to the presence of Gag in the The of the of and RNase the of Gag with which with have that not Gag in the presence of RNase A. M.A. Kleiman L. J. Virol. 2002; PubMed Scopus Google Scholar), and the the of The of a in which APOBEC3G is immunoprecipitated with and the of Gag is It can that of the to RNase or not the of APOBEC3G with this the of an RNA or DNA bridge between two the that a RNA bridge from RNase by the two The for is shown in in which the in HIV-1 has been with a to for It has been shown that the can viruses M.A. B. J. Virol. 2000; 74: PubMed Scopus Google Scholar). in which been to Gag, used as a cells with APOBEC3G and mutant HIV-1 and expression of APOBEC3G in cells by with and The that of APOBEC3G produced in all the cells with and cellular APOBEC3G if the viral produced Vif and The absence or presence of Vif cellular Gag The ability of the viruses to APOBEC3G by of viral with or The that can APOBEC3G as as the other the ability of to incorporate APOBEC3G is with These data that the motif can for Gag and virus its ability to APOBEC3G in APOBEC3G for into Gag cells with and a coding for or or APOBEC3G with These are shown in APOBEC3G has with APOBEC1 and two or containing a zinc coordination The cytoplasmic expression and viral incorporation of the APOBEC3G determined by with and for cells or and for viruses The mutant in the cell or in the viral are to a of for APOBEC3G and are at the of shown in of the amino acids or the amino acids not the ability of APOBEC3G to into Gag VLPs, the of the amino acids its incorporation into that amino acids found in the of a linker between the two zinc coordination in APOBEC3G, are required for its incorporation into Gag VLPs. APOBEC3G shown in expression in the cell lysate of to has been that of APOBEC3G are Harris R.S. M.S. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). the viral of is of APOBEC3G, not their cytoplasmic Thus, the of the regions of APOBEC3G to in a in its in the cell lysate a in its incorporation into Gag VLPs. this suggest that the APOBEC3G are not the of viral APOBEC3G, is as for the of cellular APOBEC3G Thus, the of as shown in that all cytoplasmic APOBEC3G with Gag and to the membrane, and other reports (16Mangeat B. Turelli P. Caron G. Friedli M. Perrin L. Trono D. Nature. 2003; 424: 99-103Crossref PubMed Scopus (1252) Google Scholar, K. C. W. W.C. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar) have that cellular APOBEC3G is that the APOBEC3G with Gag than Gag is also not as shown in of APOBEC3G in the with have for this of APOBEC3G into Gag is proportional to its cellular cell with of and of coding of cell lysate or Gag for APOBEC3G with are shown in the and respectively. in and the the of APOBEC3G expressed in the cell APOBEC3G into Gag of Gag the of cells with the coding for APOBEC3G alone or with this and coding for mutant of in the presence or absence of Vif. cell in and after a to cells and the into and membrane-bound as A. Cen S. Kleiman L. J. Virol. 2003; PubMed Scopus Google Scholar). by with or shown in in the absence of Gag, APOBEC3G is the of the in the cytoplasmic and in the presence of Gag of APOBEC3G is in the membrane-bound protein the of the at the a for Gag A. Cen S. Kleiman L. J. Virol. 2003; PubMed Scopus Google Scholar). Vif is also the APOBEC3G in the at cells APOBEC3G and the mutant Gag the of APOBEC3G in the Gag is found at cells are with a mutant Gag that can bind to but that the ability to bind to APOBEC3G, the APOBEC3G in the These data that binding to Gag cytoplasmic APOBEC3G to the during viral interaction is cells are with the and of the expressing APOBEC3G, the amount of APOBEC3G into viruses is proportional to the amount of APOBEC3G expressed in the cell In this have shown that Gag alone among viral proteins is sufficient for the incorporation of APOBEC3G, and that Gag and amino acids 104-156 in APOBEC3G are required for the Gag/APOBEC3G that the cytoplasmic interaction between Gag and APOBEC3G requires The for Gag a interaction of this Gag with APOBEC3G but also a for Gag or for an RNA bridge binding the two The that the Gag/APOBEC3G interaction is after RNase that Gag is not required for the Gag is not sufficient for the incorporation of APOBEC3G into viral Thus, with a virus in which the has been with a for facilitating protein that the Gag particles produced not incorporate APOBEC3G the presence of is that the incorporation of APOBEC3G into Gag is proportional to its expression in the cell APOBEC3G is not into Gag or The of viral particles not a incorporation of the other the that APOBEC3G is into with Gag including HIV-1, immunodeficiency and equine infectious anemia virus (16Mangeat B. Turelli P. Caron G. Friedli M. Perrin L. Trono D. Nature. 2003; 424: 99-103Crossref PubMed Scopus (1252) Google Scholar, R.S. A.M. Petersen-Mahrt S.K. M.S. Malim M.H. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar), some of Gag other than is structural motifs, or their ability to bind the data not the of an RNA bridge facilitating the interaction between Gag and APOBEC3G, not the of such a The RNA producing not contain viral genomic RNA packaging The containing as viral genomic RNA as containing Gag APOBEC3G that APOBEC3G packaging occurs independently of HIV-1 viral genomic RNA and an that used a to that APOBEC3G to and RNA but not to HIV-1 RNA (14Jarmuz A. Chester A. Bayliss J. Gisbourne J. Dunham I. Scott J. Navaratnam N. Genomics. 2002; 79: 285-296Crossref PubMed Scopus (593) Google Scholar). for cellular RNA in facilitating an interaction is also not by the The ability to a cytoplasmic Gag/APOBEC3G complex is with RNase the of a complex is inhibited by a RNase the that RNA Gag and APOBEC3G is not from RNase by the APOBEC3G are not have been in the family member APOBEC1 to its zinc coordination motif N. S. T. D. Scott J. Full Text PDF PubMed Scopus Google Scholar, S. J. Full Text Full Text PDF PubMed Scopus Google Scholar). APOBEC3G to zinc in and has an RNA binding to APOBEC1 (14Jarmuz A. Chester A. Bayliss J. Gisbourne J. Dunham I. Scott J. Navaratnam N. Genomics. 2002; 79: 285-296Crossref PubMed Scopus (593) Google Scholar). acids 104-156 in APOBEC3G are required for the incorporation of this into Gag zinc coordination motif, which not a for RNA in the Gag/APOBEC3G also not to of amino acids amino acids which to the binding of or APOBEC3G incorporation into with the of zinc coordination motif The data in the in not a in Gag in or cells expressing APOBEC3G, the cellular expression of APOBEC3G is in cells, Gag not In the presence of Vif in non-permissive cells the cytoplasmic of APOBEC3G, not the cytoplasmic of is shown in APOBEC3G in the is found in the of non-permissive cells In cells also expressing Gag, all of is to the in the absence of Vif but Gag not APOBEC3G to the in the presence of Vif It can also that the cellular of Gag between and is Vif is or The ability of Gag to the cytoplasmic of APOBEC3G the ability of Gag to with cell APOBEC3G in which the mutant Gag is or with in which the mutant Gag which is The data in and suggest that if Gag is with the a of Gag and Vif in the cell J.H. Fouchier R.A. Malim M.H. J. Virol. PubMed Google Scholar), an interaction of Vif with some viral assembly and the presence of Vif in D. Trono D. J. Virol. 1996; 70: PubMed Google Scholar, U. J.H. J. Virol. 2000; 74: PubMed Scopus Google Scholar, M. Yu X.F. J. Virol. PubMed Google Scholar, R.A. J.H. Malim M.H. J. Virol. 1996; 70: PubMed Google Scholar, S. H. M.A. M. Yu X.F. K. J. Virol. 2003; PubMed Scopus Google Scholar, M.A. C. S. H. S. K. J. Virol. PubMed Scopus Google Scholar, H. M. J. Virol. PubMed Google Scholar, P. L. W. J. Virol. PubMed Scopus Google Scholar). In cells with expressing Gag and Vif, that Vif Gag in Gag particles or of Vif for of Gag I. C. B. J. C. M. B. P. J. Virol. 1998; 79: PubMed Scopus Google Scholar). Gag to Vif at this an complex for in the this for of Gag and a in Gag in the cell not by the of an complex by binding the ability to Gag and Vif from cell has with of M. M. G. D. D. N. P. J. B. J. Virol. PubMed Google Scholar, Fouchier Malim M.H. J. Virol. PubMed Google Scholar), the in interaction between Vif and Gag has been used to two I. C. B. J. C. M. B. P. J. Virol. 1998; 79: PubMed Scopus Google Scholar). These that the Gag include the of the zinc the and the region of is in binding to Vif and APOBEC3G, the two for binding to the for Vif and Gag have been to include amino acids for Vif Harris R.S. M.S. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar) and amino acids 104-156 for Gag, as The of of a complex also binding between Gag and Vif for APOBEC3G or to binding to cytidine as or A. C. L. Sci. U. S. A. 1994; PubMed Scopus Google Scholar, N. T. Bayliss J. A. A. N. A. S. C. Scott J. J. 1998; PubMed Scopus Google Scholar). It has been for APOBEC1 that amino or amino RNA RNA and N. T. Bayliss J. A. A. N. A. S. C. Scott J. J. 1998; PubMed Scopus Google Scholar). has been for APOBEC3G that and that not activity and that this is to of APOBEC3G K. A. M. A. K. T. J. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). that and of APOBEC3G can into HIV-1 which that APOBEC3G its binding to RNA is required for this It is not if the deaminase activity of APOBEC3G is the in HIV-1 two reports have that in in of deaminase activity and activity (16Mangeat B. Turelli P. Caron G. Friedli M. Perrin L. Trono D. Nature. 2003; 424: 99-103Crossref PubMed Scopus (1252) Google Scholar, 17Zhang H. Yang B. Pomerantz C. L. Nature. 2003; 424: PubMed Scopus Google Scholar), a reports that in deaminase activity to but have the activity K. A. M. A. K. T. J. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). that deaminase activity of APOBEC3G not the of It is that the interaction of APOBEC3G with in the of viral with nucleocapsid. Gag sequences to viral genomic RNA S. A. M.A. Kleiman L. J. Virol. PubMed Google Scholar), which the that viral RNA to viral genomic from Vif-negative HIV-1 produced in non-permissive cells a ability to reverse transcription in with the RNA from produced in cells M. Cen S. Carlson B.A. Kleiman L. Yu X.F. J. Virol. 2000; 74: 8938-8945Crossref PubMed Scopus (104) Google Scholar). this the presence in non-permissive cells of other anti-HIV-1 to