The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Access of Antibody Molecules to the Conserved Coreceptor Binding Site on Glycoprotein gp120 Is Sterically Restricted on Primary Human Immunodeficiency Virus Type 1
Open accessAbstract
Anti-human immunodeficiency virus type 1 (HIV-1) antibodies whose binding to gp120 is enhanced by CD4 binding (CD4i antibodies) are generally considered nonneutralizing for primary HIV-1 isolates. However, a novel CD4i-specific Fab fragment, X5, has recently been found to neutralize a wide range of primary isolates. To investigate the precise nature of the extraordinary neutralizing ability of Fab X5, we evaluated the abilities of different forms (immunoglobulin G [IgG], Fab, and single-chain Fv) of X5 and other CD4i monoclonal antibodies to neutralize a range of primary HIV-1 isolates. Our results show that, for a number of isolates, the size of the neutralizing agent is inversely correlated with its ability to neutralize. Thus, the poor ability of CD4i-specific antibodies to neutralize primary isolates is due, at least in part, to steric factors that limit antibody access to the gp120 epitopes. Studies of temperature-regulated neutralization or fusion-arrested intermediates suggest that the steric effects are important in limiting the binding of IgG to the viral envelope glycoproteins after HIV-1 has engaged CD4 on the target cell membrane. The results identify hurdles in using CD4i epitopes as targets for antibody-mediated neutralization in vaccine design but also indicate that the CD4i regions could be efficiently targeted by small molecule entry inhibitors.
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Cites
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Cited by
3D visualization of HIV transfer at the virological synapse between dendritic cells and T cells
Felts, R. L., Narayan, K., Estes, J. D., Shi, D., Trubey, C. M., Fu, J., Hartnell, L. M., Ruthel, G. T., Schneider, D. K., Nagashima, K., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003040107 · Cited by 184
Sequencing the biology of entry: the retroviral Env gene
Swanstrom, R., Graham, W. D., & Zhou, S. (2017) · Current Topics in Microbiology and Immunology · doi:10.1007/82_2017_35 · Cited by 24
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Metadata
- Authors
- Labrijn, A. F., Poignard, P., Raja, A., Zwick, M. B., Delgado, K., Franti, M., Binley, J., Vivona, V., Grundner, C., Huang, C.-C., Venturi, M., Petropoulos, C. J., Wrin, T., Dimitrov, D. S., Robinson, J., Kwong, P. D., Wyatt, R. T., Sodroski, J., & Burton, D. R.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2003-10
- Volume
- 77
- Issue
- 19
- Pages
- 10557-10565
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- OpenAlex
- W2126977955
- Cited by
- 357
- References
- 59
- FWCI
- 6.56
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Access of Antibody Molecules to the Conserved Coreceptor Binding Site on Glycoprotein gp120 Is Sterically Restricted on Primary Human Immunodeficiency Virus Type 1. https://app.cochat.ai/papers/10.1128/jvi.77.19.10557-10565.2003
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- Labrijn, A. F., Poignard, P., Raja, A., Zwick, M. B., Delgado, K., Franti, M., Binley, J., Vivona, V., Grundner, C., Huang, C.-C., Venturi, M., Petropoulos, C. J., Wrin, T., Dimitrov, D. S., Robinson, J., Kwong, P. D., Wyatt, R. T., Sodroski, J., & Burton, D. R. (2003). Access of Antibody Molecules to the Conserved Coreceptor Binding Site on Glycoprotein gp120 Is Sterically Restricted on Primary Human Immunodeficiency Virus Type 1. Journal of Virology. https://doi.org/10.1128/jvi.77.19.10557-10565.2003
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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