Effects on CD4 binding of anti-peptide sera to the fourth and fifth conserved domains of HIV-1 gp120 - PubMed (original) (raw)
Affiliations
- PMID: 2304000
Effects on CD4 binding of anti-peptide sera to the fourth and fifth conserved domains of HIV-1 gp120
B Ardman et al. J Acquir Immune Defic Syndr (1988). 1990.
Abstract
Antisera to peptides that represent regions within the fourth and fifth conserved domains of the human immunodeficiency virus type 1 (HIV-1) gp120 were tested for recognition of the gp120 glycoprotein and for the ability to interfere with gp120 binding to the CD4 receptor molecule. Antisera to both peptides contained equivalent antibody titers, showed equivalent reactions with denatured gp120 on Western blot, and had group-specific reactivity. Preincubation of gp120 with either anti-peptide sera prebound to a solid phase substantially blocked soluble CD4 binding to gp120. Similarly, preincubation of gp120 with CD4-positive cells substantially diminished recognition of gp120 by both anti-peptide antisera. These results provide serologic evidence that regions near or within the fourth and fifth conserved domains of gp120 are involved in CD4 binding. However, neither anti-peptide sera could block soluble gp120 from binding to CD4-positive cells nor inhibited HIV-1 envelope-mediated syncytium formation or virus infection. These results demonstrate that antisera to regions proximal to the CD4 binding site of gp120 may compete poorly with CD4 for gp120 binding.
Similar articles
- Synthetic peptides representing discontinuous CD4 binding epitopes of HIV-1 gp120 that induce T cell apoptosis and block cell death induced by gp120.
Howie SE, Cotton GJ, Heslop I, Martin NJ, Harrison DJ, Ramage R. Howie SE, et al. FASEB J. 1998 Aug;12(11):991-8. doi: 10.1096/fasebj.12.11.991. FASEB J. 1998. PMID: 9707171 - Multiple effects of CD4 CDR3-related peptide derivatives showing anti-HIV-1 activity on HIV-1 gp120 functions.
Ohki K, Kimura T, Jones IM, Morita F, Ikuta K. Ohki K, et al. Vaccine. 1994 Mar;12(4):343-50. doi: 10.1016/0264-410x(94)90099-x. Vaccine. 1994. PMID: 8178557 - Enzyme immunoassay (ELISA) for the evaluation of antibodies directed to the CD4 receptor-binding site of the HIV gp120 molecule.
Hinkula J, Gidlund M, Persson C, Osterhaus A, Wahren B. Hinkula J, et al. J Immunol Methods. 1994 Sep 30;175(1):37-46. doi: 10.1016/0022-1759(94)90329-8. J Immunol Methods. 1994. PMID: 7523525 - [Peptides from the principal neutralizing and CD4-binding domain: similar immunoreactive properties and structure pattern].
Meshcheriakova DV, Andreev SM, Sidorova MV, Vafina MG, Az'muko AA, Petrukhina AO, Khaitov RM. Meshcheriakova DV, et al. Vestn Ross Akad Med Nauk. 1992;(9-10):47-52. Vestn Ross Akad Med Nauk. 1992. PMID: 1283721 Review. Russian.
Cited by
- Envelope glycoproteins of human immunodeficiency virus type 1: profound influences on immune functions.
Chirmule N, Pahwa S. Chirmule N, et al. Microbiol Rev. 1996 Jun;60(2):386-406. doi: 10.1128/mr.60.2.386-406.1996. Microbiol Rev. 1996. PMID: 8801439 Free PMC article. Review. - Diversity of the envelope glycoprotein among human immunodeficiency virus type 1 isolates of clade E from Asia and Africa.
McCutchan FE, Artenstein AW, Sanders-Buell E, Salminen MO, Carr JK, Mascola JR, Yu XF, Nelson KE, Khamboonruang C, Schmitt D, Kieny MP, McNeil JG, Burke DS. McCutchan FE, et al. J Virol. 1996 Jun;70(6):3331-8. doi: 10.1128/JVI.70.6.3331-3338.1996. J Virol. 1996. PMID: 8648662 Free PMC article. - gp120-independent fusion mediated by the human immunodeficiency virus type 1 gp41 envelope glycoprotein: a reassessment.
Marcon L, Sodroski J. Marcon L, et al. J Virol. 1994 Mar;68(3):1977-82. doi: 10.1128/JVI.68.3.1977-1982.1994. J Virol. 1994. PMID: 8107258 Free PMC article. - Analysis of the cross-reactive anti-gp120 antibody population in human immunodeficiency virus-infected asymptomatic individuals.
Hariharan K, Nara PL, Caralli VM, Norton FL, Haigwood N, Kang CY. Hariharan K, et al. J Virol. 1993 Feb;67(2):953-60. doi: 10.1128/JVI.67.2.953-960.1993. J Virol. 1993. PMID: 7678311 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials