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Journal of Virology, August 2007, p. 8809-8813, Vol. 81, No. 16
0022-538X/07/$08.00+0     doi:10.1128/JVI.00394-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Antibody Binding in Proximity to the Receptor/Glycoprotein Complex Leads to a Basal Level of Virus Neutralization{triangledown}

Xinzhen Yang,1,2,3,4* Inna Lipchina,4 Michelle Lifton,1 Liping Wang,4 and Joseph Sodroski3,4,5

Division of Viral Pathogenesis, Beth Israel Deaconess Medical Center,1 Department of Medicine,2 Department of Pathology, Division of AIDS, Harvard Medical School,3 Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute,4 Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, Massachusetts 022155

Received 23 February 2007/ Accepted 22 May 2007

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.

* Corresponding author. Mailing address: R.E 213A, 330 Brookline Avenue, Boston, MA 02215. Phone: (617) 667-2052. Fax: (617) 667-8210. E-mail: xyang1{at}bidmc.harvard.edu

{triangledown} Published ahead of print on 30 May 2007.

Journal of Virology, August 2007, p. 8809-8813, Vol. 81, No. 16
0022-538X/07/$08.00+0     doi:10.1128/JVI.00394-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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