NP_057856.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
69.7 kDa
NCBI Official Full Name
Envelope surface glycoprotein gp160
NCBI Protein Information
gp160; envelope glycoprotein
UniProt Protein Name
Envelope glycoprotein gp160
UniProt Synonym Protein Names
Env polyprotein
UniProt Synonym Gene Names
UniProt Entry Name
ENV_HV1H2
UniProt Comments for gp120
gp160: The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves
Protein type: Membrane protein, integral; Apoptosis
Product References and Citations for gp120 recombinant protein
Complete nucleotide sequences of functional clones of the AIDS virus.Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S., Gallo R.C., Wong-Staal F.AIDS Res. Hum. Retroviruses 3:57-69(1987)
Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S., Gallo R.C., Wong-Staal F.Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus.McCune J.M., Rabin L.B., Feinberg M.B., Lieberman M., Kosek J.C., Reyes G.R., Weissman I.L.Cell 53:55-67(1988)
Changes in the transmembrane region of the human immunodeficiency virus type 1 gp41 envelope glycoprotein affect membrane fusion.Helseth E., Olshevsky U., Gabuzda D., Ardman B., Haseltine W., Sodroski J.J. Virol. 64:6314-6318(1990)
Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160.Hallenberger S., Bosch V., Angliker H., Shaw E., Klenk H.D., Garten W.Nature 360:358-361(1992)
The immunosuppressive peptide of HIV-1
functional domains and immune response in AIDS patients.Denner J., Norley S., Kurth R.AIDS 8:1063-1072(1994)
The human and simian immunodeficiency virus envelope glycoprotein transmembrane subunits are palmitoylated.Yang C., Spies C.P., Compans R.W.Proc. Natl. Acad. Sci. U.S.A. 92:9871-9875(1995)
Human immunodeficiency virus type 1 infection of SK-N-MC cells
domains of gp120 involved in entry into a CD4-negative, galactosyl ceramide/3' sulfo-galactosyl ceramide-positive cell line.Harouse J.M., Collman R.G., Gonzalez-Scarano F.J. Virol. 69:7383-7390(1995)
Polarized human immunodeficiency virus budding in lymphocytes involves a tyrosine-based signal and favors cell-to-cell viral transmission.Deschambeault J., Lalonde J.P., Cervantes-Acosta G., Lodge R., Cohen E.A., Lemay G.J. Virol. 73:5010-5017(1999)
A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)
-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection.Bashirova A.A., Geijtenbeek T.B.H., van Duijnhoven G.C.F., van Vliet S.J., Eilering J.B.G., Martin M.P., Wu L., Martin T.D., Viebig N., Knolle P.A., Kewalramani V.N., van Kooyk Y., Carrington M.J. Exp. Med. 193:671-678(2001)
Pathogens target DC-SIGN to influence their fate DC-SIGN functions as a pathogen receptor with broad specificity.Geijtenbeek T.B., van Kooyk Y.APMIS 111:698-714(2003)
Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion.Barbouche R., Miquelis R., Jones I.M., Fenouillet E.J. Biol. Chem. 278:3131-3136(2003)
Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR.Lin G., Simmons G., Poehlmann S., Baribaud F., Ni H., Leslie G.J., Haggarty B.S., Bates P., Weissman D., Hoxie J.A., Doms R.W.J. Virol. 77:1337-1346(2003)
Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1.Yang X., Kurteva S., Ren X., Lee S., Sodroski J.J. Virol. 79:12132-12147(2005)
The HIV Env-mediated fusion reaction.Gallo S.A., Finnegan C.M., Viard M., Raviv Y., Dimitrov A., Rawat S.S., Puri A., Durell S., Blumenthal R.Biochim. Biophys. Acta 1614:36-50(2003)
Mechanisms of apoptosis induction by the HIV-1 envelope.Perfettini J.-L., Castedo M., Roumier T., Andreau K., Nardacci R., Piacentini M., Kroemer G.Cell Death Differ. 12:916-923(2005)
V3
HIV's switch-hitter.Hartley O., Klasse P.J., Sattentau Q.J., Moore J.P.AIDS Res. Hum. Retroviruses 21:171-189(2005)
Emerging drug targets for antiretroviral therapy.Reeves J.D., Piefer A.J.Drugs 65:1747-1766(2005)
HIV and the chemokine system
10 years later.Lusso P.EMBO J. 25:447-456(2006)
A conserved dileucine motif mediates clathrin and AP-2-dependent endocytosis of the HIV-1 envelope protein.Byland R., Vance P.J., Hoxie J.A., Marsh M.Mol. Biol. Cell 18:414-425(2007)
The membrane-proximal external region of the human immunodeficiency virus type 1 envelope
dominant site of antibody neutralization and target for vaccine design.Montero M., van Houten N.E., Wang X., Scott J.K.Microbiol. Mol. Biol. Rev. 72:54-84(2008)
The HIV-1 envelope glycoprotein gp120 features four heparan sulfate binding domains, including the co-receptor binding site.Crublet E., Andrieu J.P., Vives R.R., Lortat-Jacob H.J. Biol. Chem. 283:15193-15200(2008)
HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes.Miyauchi K., Kim Y., Latinovic O., Morozov V., Melikyan G.B.Cell 137:433-444(2009)
Modulation of cytokine release and gene expression by the immunosuppressive domain of gp41 of HIV-1.Denner J., Eschricht M., Lauck M., Semaan M., Schlaermann P., Ryu H., Akyuez L.PLoS ONE 8:E55199-E55199(2013)
Core structure of gp41 from the HIV envelope glycoprotein.Chan D.C., Fass D., Berger J.M., Kim P.S.Cell 89:263-273(1997)
Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody.Kwong P.D., Wyatt R., Robinson J., Sweet R.W., Sodroski J., Hendrickson W.A.Nature 393:648-659(1998)
Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides.Shu W., Liu J., Ji H., Radigen L., Jiang S., Lu M.Biochemistry 39:1634-1642(2000)
Interactions between HIV-1 gp41 core and detergents and their implications for membrane fusion.Shu W., Ji H., Lu M.J. Biol. Chem. 275:1839-1845(2000)
Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates.Kwong P.D., Wyatt R., Majeed S., Robinson J., Sweet R.W., Sodroski J., Hendrickson W.A.Structure 8:1329-1339(2000)
Interhelical interactions in the gp41 core
implications for activation of HIV-1 membrane fusion.Wang S., York J., Shu W., Stoller M.O., Nunberg J.H., Lu M.Biochemistry 41:7283-7292(2002)
Short constrained peptides that inhibit HIV-1 entry.Sia S.K., Carr P.A., Cochran A.G., Malashkevich V.N., Kim P.S.Proc. Natl. Acad. Sci. U.S.A. 99:14664-14669(2002)
Structural analysis of the epitope of the anti-HIV antibody 2F5 sheds light into its mechanism of neutralization and HIV fusion.Barbato G., Bianchi E., Ingallinella P., Hurni W.H., Miller M.D., Ciliberto G., Cortese R., Bazzo R., Shiver J.W., Pessi A.J. Mol. Biol. 330:1101-1115(2003)
Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120.Huang C.C., Venturi M., Majeed S., Moore M.J., Phogat S., Zhang M.Y., Dimitrov D.S., Hendrickson W.A., Robinson J., Sodroski J., Wyatt R., Choe H., Farzan M., Kwong P.D.Proc. Natl. Acad. Sci. U.S.A. 101:2706-2711(2004)
Structural definition of a conserved neutralization epitope on HIV-1 gp120.Zhou T., Xu L., Dey B., Hessell A.J., Van Ryk D., Xiang S.H., Yang X., Zhang M.Y., Zwick M.B., Arthos J., Burton D.R., Dimitrov D.S., Sodroski J., Wyatt R., Nabel G.J., Kwong P.D.Nature 445:732-737(2007)
HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane.Sun Z.Y., Oh K.J., Kim M., Yu J., Brusic V., Song L., Qiao Z., Wang J.H., Wagner G., Reinherz E.L.Immunity 28:52-63(2008)
Structural details of HIV-1 recognition by the broadly neutralizing monoclonal antibody 2F5
epitope conformation, antigen-recognition loop mobility, and anion-binding site.Julien J.P., Bryson S., Nieva J.L., Pai E.F.J. Mol. Biol. 384:377-392(2008)
Molecular architecture of native HIV-1 gp120 trimers.Liu J., Bartesaghi A., Borgnia M.J., Sapiro G., Subramaniam S.Nature 455:109-113(2008)
Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120.Chen L., Kwon Y.D., Zhou T., Wu X., O'Dell S., Cavacini L., Hessell A.J., Pancera M., Tang M., Xu L., Yang Z.Y., Zhang M.Y., Arthos J., Burton D.R., Dimitrov D.S., Nabel G.J., Posner M.R., Sodroski J., Wyatt R., Mascola J.R., Kwong P.D.Science 326:1123-1127(2009)
Crystal structure and size-dependent neutralization properties of HK20, a human monoclonal antibody binding to the highly conserved heptad repeat 1 of gp41.Sabin C., Corti D., Buzon V., Seaman M.S., Lutje Hulsik D., Hinz A., Vanzetta F., Agatic G., Silacci C., Mainetti L., Scarlatti G., Sallusto F., Weiss R., Lanzavecchia A., Weissenhorn W.PLoS Pathog. 6:E1001195-E1001195(2010)
A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield.Pejchal R., Doores K.J., Walker L.M., Khayat R., Huang P.S., Wang S.K., Stanfield R.L., Julien J.P., Ramos A., Crispin M., Depetris R., Katpally U., Marozsan A., Cupo A., Maloveste S., Liu Y., McBride R., Ito Y., Sanders R.W., Ogohara C., Paulson J.C., Feizi T., Scanlan C.N., Wong C.H., Moore J.P., Olson W.C., Ward A.B., Poignard P., Schief W.R., Burton D.R., Wilson I.A.Science 334:1097-1103(2011)
Broad antiviral activity and crystal structure of HIV-1 fusion inhibitor sifuvirtide.Yao X., Chong H., Zhang C., Waltersperger S., Wang M., Cui S., He Y.J. Biol. Chem. 287:6788-6796(2012)
Rational HIV immunogen design to target specific germline B cell receptors.Jardine J., Julien J.P., Menis S., Ota T., Kalyuzhniy O., McGuire A., Sok D., Huang P.S., MacPherson S., Jones M., Nieusma T., Mathison J., Baker D., Ward A.B., Burton D.R., Stamatatos L., Nemazee D., Wilson I.A., Schief W.R.Science 340:711-716(2013)
Disruption of helix-capping residues 671 and 674 reveals a role in HIV-1 entry for a specialized hinge segment of the membrane proximal external region of gp41.Sun Z.Y., Cheng Y., Kim M., Song L., Choi J., Kudahl U.J., Brusic V., Chowdhury B., Yu L., Seaman M.S., Bellot G., Shih W.M., Wagner G., Reinherz E.L.J. Mol. Biol. 426:1095-1108(2014)
+Additional computationally mapped references.<p>Provides general information on the entry.
Research Articles on gp120
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Pathways associated with gp120 recombinant protein
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