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Journal of Virology, January 2000, p. 254-263, Vol. 74, No. 1
0022-538X/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Induction of Antibodies in Guinea Pigs and Rhesus Monkeys against the Human Immunodeficiency Virus Type 1 Envelope: Neutralization of Nonpathogenic and Pathogenic Primary Isolate Simian/Human Immunodeficiency Virus Strains

Hua-Xin Liao,1,2,* Bijan Etemad-Moghadam,3 David C. Montefiori,2,4 Ying Sun,3 Joseph Sodroski,3 Richard M. Scearce,1,2 Robert W. Doms,5 James R. Thomasch,1,2 Suzanne Robinson,6 Norman L. Letvin,6 and Barton F. Haynes1,2,*

Departments of Medicine1 and Surgery4 and Center for AIDS Research,2 Duke University Medical Center, Durham, North Carolina 27710; Dana Farber Cancer Institute3 and Beth Israel Deaconess Medical Center,6 Harvard Medical School, Boston, Massachusetts 02115; and Department of Pathology, University of Pennsylvania, Philadelphia, Pennsylvania 191045

Received 30 March 1999/Accepted 10 September 1999

We have compared the abilities of human immunodeficiency virus type 1 (HIV-1) envelope V3 peptides and recombinant gp120 to induce antibodies that neutralize simian/human immunodeficiency viruses (SHIVs). SHIV-89.6 is a nonpathogenic SHIV that expresses the envelope protein of primary HIV-1 isolate 89.6. SHIV-89.6P, clone KB9, is a pathogenic SHIV variant derived from SHIV-89.6. Infection of rhesus monkeys with these SHIVs rarely induces anti-V3 region antibodies. To determine the availability of the gp120 V3 loop for neutralizing antibody binding on SHIV-89.6 and KB9 virions, we have constructed immunogenic C4-V3 peptides from these SHIVs and induced anti-V3 antibodies in guinea pigs and rhesus monkeys. We found that both SHIV-89.6 and KB9 C4-V3 peptides induced antibodies that neutralized SHIV-89.6 but that only SHIV-KB9 C4-V3 peptide induced antibodies that neutralized SHIV-KB9. Immunoprecipitation assays demonstrated that SHIV-KB9 C4-V3 peptide-induced antibodies had a greater ability to bind SHIV-KB9 envelope proteins than did antibodies raised against SHIV-89.6 C4-V3 peptide. We have used a series of mutant HIV-1 envelope constructs to map the gp120 determinants that affect neutralization by anti-V3 antibodies. The residue change at position 305 of arginine (in SHIV-89.6) to glutamic acid (in SHIV-KB9) played a central role in determining the ability of peptide-induced anti-V3 antiserum to neutralize primary isolate SHIVs. Moreover, residue changes in the SHIV-89.6 V1/V2 loops also played roles in regulating the availability of the V3 neutralizing epitope on SHIV-89.6 and -KB9. Thus, SHIV-89.6 and -KB9 V3 region peptides are capable of inducing neutralizing antibodies against these primary isolate SHIVs, although the pathogenic SHIV-KB9 is less easily neutralized than its nonpathogenic variant SHIV-89.6. In contrast to natural infection with SHIV-89.6, in which few animals make anti-V3 antibodies, C4-V3 peptides frequently induced anti-V3 antibodies that neutralized primary isolate SHIV strains.

* Corresponding author. Mailing address: Duke University Medical Center, Box 3258, Durham, NC 27710. Phone: (919) 684-5858. Fax: (919) 684-5230. E-mail for Hua-Xin Liao: hliao{at}acpub.duke.edu. E-mail for Barton F. Haynes: hayne002{at}mc.duke.edu.

Journal of Virology, January 2000, p. 254-263, Vol. 74, No. 1
0022-538X/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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