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Journal of Virology, October 2000, p. 9749-9754, Vol. 74, No. 20
Laboratory of Molecular Microbiology,
National Institute of Allergy and Infectious Diseases, National
Institutes of Health, Bethesda, Maryland 208921;
Department of Microbiology, Meharry Medical College,
Nashville, Tennessee 372082; and
Department of Surgery, Duke University Medical Center, Durham,
North Carolina 277103
Received 17 May 2000/Accepted 18 July 2000
We have previously reported that a chimpanzee infected with a
primary human immunodeficiency virus type 1 (HIV-1) isolate (HIV-1DH12) developed an extremely potent
virus-neutralizing antibody. Immunoglobulin G purified from this animal
conferred sterilizing immunity following passive transfer to macaques
which were subsequently challenged with simian immunodeficiency
virus/HIV-1 chimeric virus strain DH12. In addition to being highly
strain specific, the chimpanzee antiserum did not bind to the V3 loop
peptide of HIV-1DH12, nor did it block the interaction of
gp120 with the CD4 receptor. When neutralization was examined in the
context of virus particles carrying chimeric envelope glycoproteins,
the presence of all five hypervariable regions (V1 to V5) was required
for optimal neutralization. Virions bearing chimeric gp120 containing
the V1-V2 and V4 regions of HIV-1DH12 could also be
neutralized, but larger quantities of the chimpanzee antiserum were
needed to block infection. These results indicate that the HIV-1 gp120
epitope(s) targeted by the chimpanzee antiserum is highly
conformational, involving surface elements contributed by all of the
hypervariable domains of the envelope glycoprotein.
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Identification of gp120 Regions Targeted by a Highly Potent
Neutralizing Antiserum Elicited in a Chimpanzee Inoculated with a
Primary Human Immunodeficiency Virus Type 1 Isolate

*
Corresponding author. Mailing address: Laboratory of
Molecular Microbiology, NIH, NIAID, 9000 Rockville Pike, Bldg. 4, Rm. 339, Bethesda, MD 20892-0460. Phone: (301) 496-0576. Fax: (301) 402-0226. E-mail: mcho{at}nih.gov.
Present address: Protein Engineering Laboratory, Korea Research
Institute of Bioscience and Biotechnology, Yusong, Taejon 305-600, Republic of Korea.
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