Antibody Binding in Proximity to the Receptor/Glycoprotein Complex Leads to a Basal Level of Virus Neutralization.
From: Division of Viral Pathogenesis, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215, USA. xyang1@bidmc.harvard.edu
Journal of virology
- Publish Date: Aug 2007
- ISSN: 0022-538X
- Volume: 81
- Issue: 16
- Pages: 8809-13
- Medium: Print
- Language: English
- Citation (JAMA): Yang Xinzhen, Lipchina Inna, Lifton Michelle, et al. Antibody Binding in Proximity to the Receptor/Glycoprotein Complex Leads to a Basal Level of Virus Neutralization.. J. Virol. Aug 2007;81:8809-13
Abstract
Hypothetically, antibodies may neutralize enveloped viruses by diverse mechanisms, such as disruption of receptor binding, interference with conformational changes required for virus entry, steric hindrance, or virus aggregation. Here, we demonstrate that retroviral infection mediated by the avian sarcoma-leukosis virus (ASLV-A) envelope glycoproteins can be neutralized by an antibody directed against a functionally unimportant component of a chimeric receptor protein. Thus, the binding of an antibody in proximity to the retroviral envelope glycoprotein-receptor complex, without binding to the entry machinery itself, results in neutralization. This finding provides additional support for the hypothesis that steric hindrance is sufficient for antibody-mediated neutralization of retroviruses.
Mesh Headings (Keywords): Animals, Antibodies, Monoclonal, Antibodies, Viral, Antigen-Antibody Reactions, Avian Sarcoma Viruses, Cells, Cultured, Glycoproteins, Humans, Ligands, Receptors, CCR5, Receptors, Virus, Viral Envelope Proteins, Virus Internalization
Check for Full Text / PubMed Unique Identifier (PMID): 17537847
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