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Science 26 February 1988:
Vol. 239. no. 4843, pp. 1021 - 1023
DOI: 10.1126/science.2830667
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Articles

Science, Vol 239, Issue 4843, 1021-1023
Copyright © 1988 by American Association for the Advancement of Science

articles

Second conserved domain of gp120 is important for HIV infectivity and antibody neutralization

DD Ho, JC Kaplan, IE Rackauskas, and ME Gurney

Division of Infectious Diseases, Cedars-Sinai Medical Center, Los Angeles, CA.

Rabbit antisera were raised against three overlapping synthetic peptides with sequence homology to the second conserved domain of the external envelope glycoprotein (gp120) of the human immunodeficiency virus (HIV). All of the antisera immunoprecipitated the envelope glycoprotein. In particular, an antiserum directed against amino acids 254 to 274 of env was efficient in neutralizing three different isolates of HIV in vitro, without affecting the binding of the virus to CD4-positive cells. Therefore, this conserved region of gp120 appears to be critical in a postbinding event during virus penetration and may represent a target for antibody neutralization of HIV. These findings may be applicable in the design of a vaccine for the acquired immunodeficiency syndrome.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Immunopathogenic Mechanisms in Human Immunodeficiency Virus (HIV) Infection.
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Markers of HIV Infection Prior to IgG Antibody Seropositivity.
S. L. Stramer, J. S. Heller, R. W. Coombs, J. V. Parry, D. D. Ho, and J.-P. Allain (1989)
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Prospects for Prevention of and Early Intervention Against HIV.
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High rate of HTLV-II infection in seropositive i.v. drug abusers in New Orleans.
H Lee, P Swanson, V. Shorty, J. Zack, J. Rosenblatt, and I. Chen (1989)
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Development and Evaluation of a Vaccine for Human Immunodeficiency Virus (HIV) Infection.
A. S. Fauci, R. C. Gallo, S. Koenig, J. Salk, and R. H. Purcell (1989)
Ann Intern Med 110, 373-385
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Development and testing of AIDS vaccines.
W. Koff and D. Hoth (1988)
Science 241, 426-432
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