期刊
JOURNAL OF VIROLOGY
卷 75, 期 2, 页码 645-653出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.75.2.645-653.2001
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资金
- NCI NIH HHS [N01CO56000] Funding Source: Medline
- NIAID NIH HHS [AI85343] Funding Source: Medline
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [Z01AI000416, N01AI085343] Funding Source: NIH RePORTER
- OFFICE OF THE DIRECTOR, NCI [N01CO056000] Funding Source: NIH RePORTER
The biologically active form of the human immunodeficiency virus type 1 (HIV-1) envelope (Env) glycoprotein is oligomeric. We previously described a soluble HIV-1 IIIB Env protein, gp140, with a stable oligomeric structure composed of uncleaved gp120 linked to the ectodomain of gp41 (P. L. Earl, C. C. Broder, D. Long, S. A. Lee, J. Peterson, S. Chakrabarti, R W Doms, and B. Moss, J, Virol. 68:3015-3026, 1994). Here we compared the antibody responses of rabbits to gp120 and gp140 that had been produced and purified in an identical manner. The gp140 antisera exhibited enhanced cross-reactivity with heterologous Env proteins as well as greater neutralization of HIV-1 compared to the gp120 antisera. To examine both immunogenicity and protective efficacy, we immunized rhesus macaques with oligomeric gp140. Strong neutralizing antibodies against a homologous virus and modest neutralization of heterologous laboratory-adapted isolates were elicited. No neutralization of primary isolates was observed. However, a substantial fraction of the neutralizing activity could not be blocked by a V3 loop peptide. After intravenous challenge with simian-HIV virus SHN-HXB2, three of the four vaccinated macaques exhibited no evidence of virus replication.
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