Cited by 235HIV Research and TreatmentMonoclonal and Polyclonal Antibodies ResearchSARS-CoV-2 and COVID-19 Research

The DOI matches its Crossref record; 76 of the 77 references it cites were found in a registry or an index.

Mechanism of Neutralization by the Broadly Neutralizing HIV-1 Monoclonal Antibody VRC01

Open access

Li, Yuxing, O'Dell, Sijy, Walker, Laura M., Wu, Xueling, Guenaga, Javier, Feng, Yu, Schmidt, Stephen D., McKee, Krisha, Louder, Mark K., Ledgerwood, Julie E., Graham, Barney S., Haynes, Barton F., Burton, Dennis R., Wyatt, Richard T., Mascola, John R.·2011·Journal of Virology

DOI 10.1128/jvi.00754-11PMC PMC3165784

Open this paper in CoChat — free account Open PDF

Abstract

The structure of VRC01 in complex with the HIV-1 gp120 core reveals that this broadly neutralizing CD4 binding site (CD4bs) antibody partially mimics the interaction of the primary virus receptor, CD4, with gp120. Here, we extended the investigation of the VRC01-gp120 core interaction to the biologically relevant viral spike to better understand the mechanism of VRC01-mediated neutralization and to define viral elements associated with neutralization resistance. In contrast to the interaction of CD4 or the CD4bs monoclonal antibody (MAb) b12 with the HIV-1 envelope glycoprotein (Env), occlusion of the VRC01 epitope by quaternary constraints was not a major factor limiting neutralization. Mutagenesis studies indicated that VRC01 contacts within the gp120 loop D, the CD4 binding loop, and the V5 region were necessary for optimal VRC01 neutralization, as suggested by the crystal structure. In contrast to interactions with the soluble gp120 monomer, VRC01 interaction with the native viral spike did not occur in a CD4-like manner; VRC01 did not induce gp120 shedding from the Env spike or enhance gp41 membrane proximal external region (MPER)-directed antibody binding to the Env spike. Finally, VRC01 did not display significant reactivity with human antigens, boding well for potential in vivo applications. The data indicate that VRC01 interacts with gp120 in the context of the functional spike in a manner distinct from that of CD4. It achieves potent neutralization by precisely targeting the CD4bs without requiring alterations of Env spike configuration and by avoiding steric constraints imposed by the quaternary structure of the functional Env spike.

Integrity signals

Registry

Crossref · 10.1128/jvi.00754-11

Cites

76 of 76 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

HIV-1 Entry Cofactor: Functional cDNA Cloning of a Seven-Transmembrane, G Protein-Coupled Receptor
Feng, Y. Y., Broder, C. C., Kennedy, P. E., & Berger, E. A. (1996) · Science · doi:10.1126/science.272.5263.872 · Cited by 4,169
Self-citation
Identification of a major co-receptor for primary isolates of HIV-1
Deng, H., Liu, R., Ellmeier, W., Choe, S. S., Unutmaz, D., Burkhart, M. D., Marzio, P. D., Marmon, S., Sutton, R. E., Hill, C. M., et al. (1996) · Nature · doi:10.1038/381661a0 · Cited by 3,640
The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus
Dalgleish, A. G., Beverley, P. C. L., Clapham, P. R., Crawford, D., Greaves, M. F., & Weiss, R. A. (1984) · Nature · doi:10.1038/312763a0 · Cited by 3,539
HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5
Dragic, T., Litwin, V., Allaway, G. P., Martin, S. R., Huang, Y., Nagashima, K. A., Cayanan, C. S., Maddon, P. J., Koup, R. A., Moore, J. P., et al. (1996) · Nature · doi:10.1038/381667a0 · Cited by 3,173
CC CKR5: A RANTES, MIP-1α, MIP-1β Receptor as a Fusion Cofactor for Macrophage-Tropic HIV-1
Alkhatib, G., Combadière, C., Broder, C. C., Feng, Y., Kennedy, P. E., Murphy, P. M., & Berger, E. A. (1996) · Science · doi:10.1126/science.272.5270.1955 · Cited by 2,703
Self-citation
T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV
Klatzmann, D., Champagne, É., Chamaret, S., Gruest, J., Guétard, D., Hercend, T., Gluckman, J. C., & Montagnier, L. (1984) · Nature · doi:10.1038/312767a0 · Cited by 2,435
Antibody neutralization and escape by HIV-1
Wei, X., Decker, J. M., Wang, S., Hui, H., Kappes, J. C., Wu, X., Salazar-Gonzalez, J. F., Salazar, M. G., Kilby, J. M., Saag, M. S., et al. (2003) · Nature · doi:10.1038/nature01470 · Cited by 2,421
Self-citation
The β-Chemokine Receptors CCR3 and CCR5 Facilitate Infection by Primary HIV-1 Isolates
Choe, H., Farzan, M., Sun, Y., Sullivan, N. J., Rollins, B. J., Ponath, P. D., Wu, L., Mackay, C. R., LaRosa, G. J., Newman, W., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81313-6 · Cited by 2,286
Core Structure of gp41 from the HIV Envelope Glycoprotein
Chan, D. C., Fass, D., Berger, J. M., & Kim, P. S. (1997) · Cell · doi:10.1016/s0092-8674(00)80205-6 · Cited by 2,000
Broad and Potent Neutralizing Antibodies from an African Donor Reveal a New HIV-1 Vaccine Target
Walker, L., Phogat, S., Chan-hui, P., Wagner, D., Pham, P., Goss, J. L., Wrin, T., Simek, M., Fling, S., Mitcham, J., et al. (2009) · Science · doi:10.1126/science.1178746 · Cited by 1,849
Self-citation
A Dual-Tropic Primary HIV-1 Isolate That Uses Fusin and the β-Chemokine Receptors CKR-5, CKR-3, and CKR-2b as Fusion Cofactors
Doranz, B. J., Rucker, J. B., Yi, Y., Smyth, R. J., Samson, M., Peiper, S. C., Parmentier, M., Collman, R. G., & Doms, R. W. (1996) · Cell · doi:10.1016/s0092-8674(00)81314-8 · Cited by 1,833
Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1
Wu, X., Yang, Z., Li, Y., Högerkorp, C., Schief, W. R., Seaman, M. S., Zhou, T., Schmidt, S. D., Wu, L., Xu, L., et al. (2010) · Science · doi:10.1126/science.1187659 · Cited by 1,724
Self-citation
Atomic structure of the ectodomain from HIV-1 gp41
Weissenhorn, W., Dessen, A., Harrison, S. C., Skehel, J. J., & Wiley, D. C. (1997) · Nature · doi:10.1038/387426a0 · Cited by 1,625
The HIV-1 Envelope Glycoproteins: Fusogens, Antigens, and Immunogens
Wyatt, R. T., & Sodroski, J. (1998) · Science · doi:10.1126/science.280.5371.1884 · Cited by 1,605
Self-citation
Rapid evolution of the neutralizing antibody response to HIV type 1 infection
Richman, D. D., Wrin, T., Little, S. J., & Petropoulos, C. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0630530100 · Cited by 1,196
CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5
Wu, L., Gerard, N. P., Wyatt, R. T., Choe, H., Parolin, C., Ruffing, N., Borsetti, A., Cardoso, A. A., Desjardin, E., Newman, W., et al. (1996) · Nature · doi:10.1038/384179a0 · Cited by 1,168
Self-citation
Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01
Zhou, T., Georgiev, I. S., Wu, X., Yang, Z., Dai, K., Finzi, A., Kwon, Y. D., Scheid, J. F., Shi, W., Xu, L., et al. (2010) · Science · doi:10.1126/science.1192819 · Cited by 1,123
Self-citation
Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1
Trkola, A., Purtscher, M., Muster, T., Ballaun, C., Buchacher, A., Sullivan, N. J., Srinivasan, K., Sodroski, J., Moore, J. P., & Katinger, H. W. D. (1996) · Journal of Virology · doi:10.1128/jvi.70.2.1100-1108.1996 · Cited by 1,115
Efficient Neutralization of Primary Isolates of HIV-1 by a Recombinant Human Monoclonal Antibody
Burton, D. R., Pyati, J., Koduri, R. K., Sharp, S. J., Thornton, G. B., Parren, P. W. H. I., Sawyer, L. S. W., Hendry, R. M., Dunlop, N. M., Nara, P. L., et al. (1994) · Science · doi:10.1126/science.7973652 · Cited by 1,100
Self-citation
Human Immunodeficiency Virus Type 1 env Clones from Acute and Early Subtype B Infections for Standardized Assessments of Vaccine-Elicited Neutralizing Antibodies
Li, M., Gao, F., Mascola, J. R., Stamatatos, L., Polonis, V. R., Koutsoukos, M., Voss, G., Goepfert, P., Gilbert, P. B., Greene, K., et al. (2005) · Journal of Virology · doi:10.1128/jvi.79.16.10108-10125.2005 · Cited by 1,077
Self-citation
CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5
Trkola, A., Dragic, T., Arthos, J. A., Binley, J. Μ., Olson, W. C., Allaway, G. P., Cheng‐Mayer, C., Robinson, J. E., Maddon, P. J., & Moore, J. P. (1996) · Nature · doi:10.1038/384184a0 · Cited by 1,034
Binding of HTLV-III/LAV to T4 + T Cells by a Complex of the 110K Viral Protein and the T4 Molecule
McDougal, J. S., Kennedy, M. S., Sligh, J. M., Cort, S. P., Mawle, A. C., & Nicholson, J. K. A. (1986) · Science · doi:10.1126/science.3001934 · Cited by 989
HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites
Kwong, P. D., Doyle, M. L., Casper, D. J., Cicala, C., Leavitt, S. A., Majeed, S., Steenbeke, T. D., Venturi, M., CHAIKEN, I. M., Fung, M. S. C., et al. (2002) · Nature · doi:10.1038/nature01188 · Cited by 889
Self-citation
Molecular architecture of native HIV-1 gp120 trimers
Liu, J., Bartesaghi, A., Borgnia, M. J., Sapiro, G., & Subramaniam, S. (2008) · Nature · doi:10.1038/nature07159 · Cited by 815
Broadly Neutralizing Antibodies Targeted to the Membrane-Proximal External Region of Human Immunodeficiency Virus Type 1 Glycoprotein gp41
Zwick, M. B., Labrijn, A. F., Wang, M., Spenlehauer, C., Saphire, E. O., Binley, J. Μ., Moore, J. P., Stiegler, G. M., Katinger, H. W. D., Burton, D. R., et al. (2001) · Journal of Virology · doi:10.1128/jvi.75.22.10892-10905.2001 · Cited by 797
Self-citation
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., et al. (2007) · Nature · doi:10.1038/nature05580 · Cited by 770
Self-citation
Cardiolipin Polyspecific Autoreactivity in Two Broadly Neutralizing HIV-1 Antibodies
Haynes, B. F., Fleming, J., Clair, E. W. S., Katinger, H., Stiegler, G. M., Kunert, R., Robinson, J. E., Scearce, R. M., Plonk, K., Staats, H. F., et al. (2005) · Science · doi:10.1126/science.1111781 · Cited by 746
Self-citation
A trimeric structural domain of the HIV-1 transmembrane glycoprotein
Lu, M., Blacklow, S. C., & Kim, P. S. (1995) · Nature Structural & Molecular Biology · doi:10.1038/nsb1295-1075 · Cited by 702
The Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 Antibody 2G12 Recognizes a Cluster of α1→2 Mannose Residues on the Outer Face of gp120
Scanlan, C. N., Pantophlet, R. A., Wormald, M. R., Saphire, E. O., Stanfield, R. L., Wilson, I. A., Katinger, H. W. D., Dwek, R. A., Rudd, P. M., & Burton, D. R. (2002) · Journal of Virology · doi:10.1128/jvi.76.14.7306-7321.2002 · Cited by 665
Self-citation
Dissociation of gp120 from HIV-1 virions induced by soluble CD4.
Moore, J., McKeating, J., Weiss, R., & Sattentau, Q. (1990) · Science · doi:10.1126/science.2251501 · Cited by 625
Human Immunodeficiency Virus Type 1 Elite Neutralizers: Individuals with Broad and Potent Neutralizing Activity Identified by Using a High-Throughput Neutralization Assay together with an Analytical Selection Algorithm
Simek, M. D., RIDA, W. N., Priddy, F. H., Pung, P., Carrow, E. W., Laufer, D. S., Lehrman, J. K., Boaz, M. J., Tarragona-Fiol, T., Miiro, G., et al. (2009) · Journal of Virology · doi:10.1128/jvi.00110-09 · Cited by 605
Self-citation
The Mannose-Dependent Epitope for Neutralizing Antibody 2G12 on Human Immunodeficiency Virus Type 1 Glycoprotein gp120
Sanders, R. W., Venturi, M., Schiffner, L., Kalyanaraman, R., Katinger, H. W. D., Lloyd, K. O., Kwong, P. D., & Moore, J. P. (2002) · Journal of Virology · doi:10.1128/jvi.76.14.7293-7305.2002 · Cited by 553
Generation of Human Monoclonal Antibodies against HIV-1 Proteins; Electrofusion and Epstein-Barr Virus Transformation for Peripheral Blood Lymphocyte Immortalization
Buchacher, A., PREDL, R., Strutzenberger, K., Steinfellner, W., Trkola, A., Purtscher, M., Grüber, G., Tauer, C., Steindl, F., Jungbauer, A., et al. (1994) · AIDS Research and Human Retroviruses · doi:10.1089/aid.1994.10.359 · Cited by 529
Factors Associated with the Development of Cross-Reactive Neutralizing Antibodies during Human Immunodeficiency Virus Type 1 Infection
Sather, D. N., Armann, J. P., Ching, L. K., Mavrantoni, A., Sellhorn, G., Caldwell, Z., Yu, X., Wood, B., Self, S. G., Kalams, S. A., et al. (2008) · Journal of Virology · doi:10.1128/jvi.02036-08 · Cited by 528
Capture of an early fusion-active conformation of HIV-1 gp41
Furuta, R. A., Wild, C. T., Weng, Y., & Weiss, C. D. (1998) · Nature Structural Biology · doi:10.1038/nsb0498-276 · Cited by 488
GP120: Target for Neutralizing HIV-1 Antibodies
Pantophlet, R. A., & Burton, D. R. (2006) · Annual Review of Immunology · doi:10.1146/annurev.immunol.24.021605.090557 · Cited by 440
Self-citation
Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine?
Stamatatos, L., Morris, L., Burton, D. R., & Mascola, J. R. (2009) · Nature Medicine · doi:10.1038/nm.1949 · Cited by 430
Self-citation
Energetics of the HIV gp120-CD4 binding reaction
Myszka, D. G., Sweet, R. W., Hensley, P., Brigham-Burke, M. R., Kwong, P. D., Hendrickson, W. A., Wyatt, R. T., Sodroski, J., & Doyle, M. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.16.9026 · Cited by 422
Self-citation
Broad HIV-1 neutralization mediated by CD4-binding site antibodies
Li, Y., Migueles, S. A., Welcher, B. C., Svehla, K., Phogat, A., Louder, M. K., Wu, X., Shaw, G. M., Connors, M., Wyatt, R. T., et al. (2007) · Nature Medicine · doi:10.1038/nm1624 · Cited by 382
Self-citation
The Role of Antibodies in HIV Vaccines
Mascola, J. R., & Montefiori, D. C. (2010) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101256 · Cited by 382
Self-citation
Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein.
Earl, P. L., Doms, R. W., & Moss, B. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.2.648 · Cited by 365
Profiling the Specificity of Neutralizing Antibodies in a Large Panel of Plasmas from Patients Chronically Infected with Human Immunodeficiency Virus Type 1 Subtypes B and C
Binley, J. Μ., Lybarger, E. A., Crooks, E. T., Seaman, M. S., Gray, E. S., Davis, K. L., Decker, J. M., Wycuff, D. L., Harris, L. J., Hawkins, N. R., et al. (2008) · Journal of Virology · doi:10.1128/jvi.01762-08 · Cited by 355
Self-citation
Breadth of Human Immunodeficiency Virus-Specific Neutralizing Activity in Sera: Clustering Analysis and Association with Clinical Variables
Doria‐Rose, N. A., Klein, R. M., Daniels, M., O'Dell, S. J., Nason, M., Lapedes, A. S., Tanmoy Bhattacharya, A., Migueles, S. A., Wyatt, R. T., Korber, B., et al. (2009) · Journal of Virology · doi:10.1128/jvi.01482-09 · Cited by 336
Self-citation
Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein
Moore, J. P., & Sodroski, J. (1996) · Journal of Virology · doi:10.1128/jvi.70.3.1863-1872.1996 · Cited by 304
Neutralizing Antibody Responses in Acute Human Immunodeficiency Virus Type 1 Subtype C Infection
Gray, E. S., Moore, P. L., Choge, I., Decker, J. M., Bibollet‐Ruche, F., Li, H., Leseka, N., Treurnicht, F. K., Mlisana, K. P., Shaw, G. M., et al. (2007) · Journal of Virology · doi:10.1128/jvi.00239-07 · Cited by 299
Dissection of the carbohydrate specificity of the broadly neutralizing anti-HIV-1 antibody 2G12
Calarese, D. A., Lee, H., Huang, C., Best, M. D., Astronomo, R. D., Stanfield, R. L., Katinger, H. W. D., Burton, D. R., Wong, C., & Wilson, I. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505763102 · Cited by 293
Self-citation
Oligomeric structure of gp41, the transmembrane protein of human immunodeficiency virus type 1
Pinter, A., Honnen, W. J., TILLEY, S. A., Bona, C. A., Zaghouani, H., Górny, M. K., & Zolla‐Pazner, S. (1989) · Journal of Virology · doi:10.1128/jvi.63.6.2674-2679.1989 · Cited by 291
Anti-Human Immunodeficiency Virus Type 1 (HIV-1) Antibodies 2F5 and 4E10 Require Surprisingly Few Crucial Residues in the Membrane-Proximal External Region of Glycoprotein gp41 To Neutralize HIV-1
Zwick, M. B., Jensen, R., Church, S., Wang, M., Stiegler, G. M., Kunert, R., Katinger, H. W. D., & Burton, D. R. (2004) · Journal of Virology · doi:10.1128/jvi.79.2.1252-1261.2005 · Cited by 278
Self-citation
Analysis of Neutralization Specificities in Polyclonal Sera Derived from Human Immunodeficiency Virus Type 1-Infected Individuals
Li, Y., Svehla, K., Louder, M. K., Wycuff, D. L., Phogat, S. K., Tang, M., Migueles, S. A., Wu, X., Phogat, A., Shaw, G. M., et al. (2008) · Journal of Virology · doi:10.1128/jvi.01992-08 · Cited by 259
Self-citation
Small-molecule inhibitors of HIV-1 entry block receptor-induced conformational changes in the viral envelope glycoproteins
Si, Z., Madani, N., Cox, J. M., Chruma, J. J., Klein, J. C., Schön, A., Phan, N. M. H., Wang, L., Biorn, A. C., Cocklin, S., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307953101 · Cited by 248
Fine Mapping of the Interaction of Neutralizing and Nonneutralizing Monoclonal Antibodies with the CD4 Binding Site of Human Immunodeficiency Virus Type 1 gp120
Pantophlet, R. A., Saphire, E. O., Poignard, P., Parren, P. W. H. I., Wilson, I. A., & Burton, D. R. (2002) · Journal of Virology · doi:10.1128/jvi.77.1.642-658.2003 · Cited by 244
Self-citation
Variable Loop Glycan Dependency of the Broad and Potent HIV-1-Neutralizing Antibodies PG9 and PG16
Doores, K. J., & Burton, D. R. (2010) · Journal of Virology · doi:10.1128/jvi.00552-10 · Cited by 235
Self-citation
Autologous and heterologous neutralizing antibody responses following initial seroconversion in human immunodeficiency virus type 1-infected individuals
Moog, C., Fleury, H. J., Pellegrin, I., Kirn, A., & Aubertin, A.-M. (1997) · Journal of Virology · doi:10.1128/jvi.71.5.3734-3741.1997 · Cited by 232
Native oligomeric human immunodeficiency virus type 1 envelope glycoprotein elicits diverse monoclonal antibody reactivities
Earl, P. L., Broder, C. C., Long, D., Lee, S. A., Peterson, J., Chakrabarti, S., Doms, R. W., & Moss, B. (1994) · Journal of Virology · doi:10.1128/jvi.68.5.3015-3026.1994 · Cited by 215
Binding of soluble CD4 proteins to human immunodeficiency virus type 1 and infected cells induces release of envelope glycoprotein gp120.
Hart, T. K., Kirsh, R. L., Ellens, H. M., Sweet, R. W., Lambert, D. M., Petteway, S. R., Leary, J. F., & Bugelski, P. J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.6.2189 · Cited by 204
Dissecting the Neutralizing Antibody Specificities of Broadly Neutralizing Sera from Human Immunodeficiency Virus Type 1-Infected Donors
Dhillon, A. K., Donners, H., Pantophlet, R. A., Johnson, W. E., Decker, J. M., Shaw, G. M., Lee, F.-H., Richman, D. D., Doms, R. W., Vanham, G., et al. (2007) · Journal of Virology · doi:10.1128/jvi.02749-06 · Cited by 192
Self-citation
Antibody Specificities Associated with Neutralization Breadth in Plasma from Human Immunodeficiency Virus Type 1 Subtype C-Infected Blood Donors
Gray, E. S., Taylor, N., Wycuff, D. L., Moore, P. L., Tomaras, G. D., Wibmer, C. K., Puren, A. J., deCamp, A. C., Gilbert, P. B., Wood, B., et al. (2009) · Journal of Virology · doi:10.1128/jvi.00758-09 · Cited by 182
Self-citation
Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition
Koch, M., Pancera, M., Kwong, P. D., Kolchinsky, P., Grundner, C., Wang, L., Hendrickson, W. A., Sodroski, J., & Wyatt, R. T. (2003) · Virology · doi:10.1016/s0042-6822(03)00294-0 · Cited by 175
Self-citation
Direct measurement of soluble CD4 binding to human immunodeficiency virus type 1 virions: gp120 dissociation and its implications for virus-cell binding and fusion reactions and their neutralization by soluble CD4
Moore, J. P., McKeating, J. A., Norton, W. A., & Sattentau, Q. J. (1991) · Journal of Virology · doi:10.1128/jvi.65.3.1133-1140.1991 · Cited by 173
Increased Neutralization Sensitivity of CD4-Independent Human Immunodeficiency Virus Variants
Kolchinsky, P., Kiprilov, E., & Sodroski, J. (2001) · Journal of Virology · doi:10.1128/jvi.75.5.2041-2050.2001 · Cited by 172
Removal of a Single N-Linked Glycan in Human Immunodeficiency Virus Type 1 gp120 Results in an Enhanced Ability To Induce Neutralizing Antibody Responses
Li, Y., Cleveland, B., Klots, I. N., Travis, B. M., Richardson, B. A., Anderson, D., Montefiori, D. C., Polacino, P. S., & Hu, S.-L. (2007) · Journal of Virology · doi:10.1128/jvi.01691-07 · Cited by 164
Self-citation
Antibody polyspecificity and neutralization of HIV-1: A hypothesis
Haynes, B. F., Moody, M. A., Verkoczy, L. K., Kelsoe, G. H., & Alam, S. M. (2006) · Human Antibodies · doi:10.3233/hab-2005-143-402 · Cited by 163
Self-citation
Oligomeric organization of gp120 on infectious human immunodeficiency virus type 1 particles
Weiss, C. D., Levy, J. A., & White, J. M. (1990) · Journal of Virology · doi:10.1128/jvi.64.11.5674-5677.1990 · Cited by 161
Fine Definition of the Epitope on the gp41 Glycoprotein of Human Immunodeficiency Virus Type 1 for the Neutralizing Monoclonal Antibody 2F5
Parker, C. E., Deterding, L. J., Hager‐Braun, C., Binley, J. Μ., Schülke, N., Katinger, H. W. D., Moore, J. P., & Tomer, K. B. (2001) · Journal of Virology · doi:10.1128/jvi.75.22.10906-10911.2001 · Cited by 159
Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage
Pancera, M., & Wyatt, R. T. (2004) · Virology · doi:10.1016/j.virol.2004.10.042 · Cited by 151
Self-citation
Role of Complex Carbohydrates in Human Immunodeficiency Virus Type 1 Infection and Resistance to Antibody Neutralization
Binley, J. Μ., Ban, Y. A., Crooks, E. T., Eggink, D., Osawa, K., Schief, W. R., & Sanders, R. W. (2010) · Journal of Virology · doi:10.1128/jvi.00105-10 · Cited by 144
Peptides Trap the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Fusion Intermediate at Two Sites
He, Y., Vassell, R. A., Zaitseva, M. B., Nguyen, N. Y., Yang, Z., Weng, Y., & Weiss, C. D. (2003) · Journal of Virology · doi:10.1128/jvi.77.3.1666-1671.2003 · Cited by 130
The Prefusogenic Intermediate of HIV-1 gp41 Contains Exposed C-peptide Regions
Koshiba, T., & Chan, D. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211154200 · Cited by 116
Enhancing Exposure of HIV-1 Neutralization Epitopes through Mutations in gp41
Blish, C. A., Nguyen, M.-A., & Overbaugh, J. M. (2007) · PLoS Medicine · doi:10.1371/journal.pmed.0050009 · Cited by 98
Mechanism of Human Immunodeficiency Virus Type 1 Resistance to Monoclonal Antibody b12 That Effectively Targets the Site of CD4 Attachment
Wu, X., Zhou, T., O'Dell, S. J., Wyatt, R. T., Kwong, P. D., & Mascola, J. R. (2009) · Journal of Virology · doi:10.1128/jvi.01142-09 · Cited by 94
Self-citation
Two mechanisms of soluble CD4 (sCD4)-mediated inhibition of human immunodeficiency virus type 1 (HIV-1) infectivity and their relation to primary HIV-1 isolates with reduced sensitivity to sCD4
Orloff, S. L., Kennedy, M. S., Belperron, A. A., Maddon, P. J., & McDougal, J. S. (1993) · Journal of Virology · doi:10.1128/jvi.67.3.1461-1471.1993 · Cited by 93
Structure of a clade C HIV-1 gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity
Diskin, R., Marcovecchio, P., & Björkman, P. J. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1796 · Cited by 91
Inhibition of Mammalian Glycan Biosynthesis Produces Non-self Antigens for a Broadly Neutralising, HIV-1 Specific Antibody
Scanlan, C. N., Ritchie, G. E., Baruah, K., Crispin, M., Harvey, D. J., Singer, B. B., Lucka, L., Wormald, M. R., Wentworth, P., Zitzmann, N., et al. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.06.027 · Cited by 68
Self-citation
HIV Type 1 Env Precursor Cleavage State Affects Recognition by Both Neutralizing and Nonneutralizing gp41 Antibodies
Chakrabarti, B. K., Pancera, M., Phogat, S. K., O'Dell, S. J., McKee, K., Guenaga, J., Robinson, J. E., Mascola, J. R., & Wyatt, R. T. (2010) · AIDS Research and Human Retroviruses · doi:10.1089/aid.2010.0281 · Cited by 56
Self-citation
Soluble CD4 and dextran sulfate mediate release of gp120 from HIV-1: implications for clinical trials.
Pj, B., Ellens, H. M., Tk, H., & Kirsh, R. L. (1991) · PubMed · Cited by 35
The effect of sCD4 on the binding and accessibility of HIV-1 gp41 MPER epitopes to human monoclonal antibodies
Peachman, K. K., Wieczorek, L., Polonis, V. R., Alving, C. R., & Rao, M. (2010) · Virology · doi:10.1016/j.virol.2010.09.029 · Cited by 13

Flagged first, then by citations

1 of the 77 references couldn’t be matched to a known paper.

Sorted by citations

mRNA vaccines for infectious diseases: principles, delivery and clinical translation
Chaudhary, N., Weissman, D., & Whitehead, K. A. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00283-5 · Cited by 1,555
HIV ‐1 neutralizing antibodies: understanding nature's pathways
Mascola, J. R., & Haynes, B. F. (2013) · Immunological Reviews · doi:10.1111/imr.12075 · Cited by 476
Self-citation
Virologic effects of broadly neutralizing antibody VRC01 administration during chronic HIV-1 infection
Lynch, R. M., Boritz, E., Coates, E. E., DeZure, A. D., Madden, P. J., Costner, P. J. M., Enama, M. E., Plummer, S. H., Holman, L. A., Hendel, C. S., et al. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aad5752 · Cited by 464
Self-citation
Increasing the Potency and Breadth of an HIV Antibody by Using Structure-Based Rational Design
Diskin, R., Scheid, J. F., Marcovecchio, P., West, A. P., Klein, F., Gao, H., Gnanapragasam, P. N. P., Abadir, A., Seaman, M. S., Nussenzweig, M. C., et al. (2011) · Science · doi:10.1126/science.1213782 · Cited by 376
Identification of a CD4-Binding-Site Antibody to HIV that Evolved Near-Pan Neutralization Breadth
Huang, J., Kang, B. H., Ishida, E., Zhou, T., Griesman, T., Sheng, Z., Wu, F., Doria‐Rose, N. A., Zhang, B., McKee, K., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.10.027 · Cited by 368
Self-citation

See all 235

Authors: Li, Y., O'Dell, S., Walker, L. M., Wu, X., Guenaga, J., Feng, Y., Schmidt, S. D., McKee, K., Louder, M. K., Ledgerwood, J. E., Graham, B. S., Haynes, B. F., Burton, D. R., Wyatt, R. T., & Mascola, J. R.
Affiliations: National Institutes of Health (US)
Scripps Research Institute (US)
Duke Medical Center (US)
ORCID: Li, Yuxing
O'Dell, Sijy
Walker, Laura M.
Wu, Xueling
Guenaga, Javier
Feng, Yu
Schmidt, Stephen D.
Louder, Mark K.
Ledgerwood, Julie E.
Graham, Barney S.
Haynes, Barton F.
Burton, Dennis R.
Wyatt, Richard T.
Mascola, John R.
Venue: Journal of Virology
Publisher: American Society for Microbiology
Published: 2011-09
Volume: 85
Issue: 17
Pages: 8954-8967
ISSN: 0022-538X (ISSN-L)
1098-5514
DOI: 10.1128/jvi.00754-11
PMC: PMC3165784
OpenAlex: W2165692875
Cited by: 235
References: 77
Citations by year: 2026: 9 · 2025: 11 · 2024: 5 · 2023: 5 · 2022: 10 · 2021: 14 · 2020: 8 · 2019: 17 · 2018: 18 · 2017: 19 · 2016: 23 · 2015: 22 · 2014: 16 · 2013: 21 · 2012: 30
FWCI: 9.24
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Virology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of Allergy and Infectious Diseases (R01AI033292)
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
Keywords: VRC01, broadly neutralizing antibodies, HIV-1, CD4 binding site, gp120, CD4 receptor, neutralization resistance, steric constraints
MeSH terms: Antibodies, Monoclonal, Binding Sites, Enzyme-Linked Immunosorbent Assay, Humans, Models, Molecular, Neutralization Tests, Protein Binding, HIV-1, HIV Envelope Protein gp120, Mutagenesis, Site-Directed, Mutant Proteins, Antibodies, Neutralizing

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Mechanism of Neutralization by the Broadly Neutralizing HIV-1 Monoclonal Antibody VRC01

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks