Immunological evidence for interactions between the first, second, and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1 - PubMed (original) (raw)
Immunological evidence for interactions between the first, second, and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1
J P Moore et al. J Virol. 1994 Nov.
Abstract
We have used a combination of genetic and immunological techniques to explore how amino acid substitutions in the second conserved (C2) domain of gp120 from human immunodeficiency virus type 1 (HIV-1) affect the conformation of the protein. It was reported previously (R. L. Willey, E. K. Ross, A. J. Buckler-White, T. S. Theodore, and M. A. Martin. J. Viol. 63:3595-3600, 1989) that an asparagine-glutamine (N/Q) substitution at C2 residue 267 of HIV-1 NL4/3 reduced virus infectivity, but that infectivity was restored by a compensatory amino acid change (serine-glutamine; S/N) at residue 128 in the C1 domain. Here we show that the 267 N/Q substitution causes the abnormal exposure of a segment of C1 spanning residues 80 to 120, which compromises the integrity of the CD4-binding site. The reversion substitution at residue 128 restores the normal conformation of the C1 domain and recreates a high-affinity CD4-binding site. The gp120 structural perturbation caused by changes in C2 extends also to the C5 domain, and we show by immunological analysis that there is a close association between areas of the C1 and C5 domains. This association might be important for forming a complex binding site for gp41 (E. Helseth, U. Olshevsky, C. Furman, and J. Sodroski. J. Virol. 65:2119-2123, 1991). Segments of the C1 and C2 domains are predicted to form amphipathic alpha helices. We suggest that these helices might be packed together in the core of the folded gp120 molecule, that the 267 N/Q substitution disrupts this interdomain association, and that the 128 S/N reversion substitution restores it.
Similar articles
- Characterization of neutralizing monoclonal antibodies to linear and conformation-dependent epitopes within the first and second variable domains of human immunodeficiency virus type 1 gp120.
McKeating JA, Shotton C, Cordell J, Graham S, Balfe P, Sullivan N, Charles M, Page M, Bolmstedt A, Olofsson S, et al. McKeating JA, et al. J Virol. 1993 Aug;67(8):4932-44. doi: 10.1128/JVI.67.8.4932-4944.1993. J Virol. 1993. PMID: 7687306 Free PMC article. - A Highly Conserved gp120 Inner Domain Residue Modulates Env Conformation and Trimer Stability.
Ding S, Tolbert WD, Prévost J, Pacheco B, Coutu M, Debbeche O, Xiang SH, Pazgier M, Finzi A. Ding S, et al. J Virol. 2016 Sep 12;90(19):8395-409. doi: 10.1128/JVI.01068-16. Print 2016 Oct 1. J Virol. 2016. PMID: 27384653 Free PMC article. - Functional analysis of the disulfide-bonded loop/chain reversal region of human immunodeficiency virus type 1 gp41 reveals a critical role in gp120-gp41 association.
Maerz AL, Drummer HE, Wilson KA, Poumbourios P. Maerz AL, et al. J Virol. 2001 Jul;75(14):6635-44. doi: 10.1128/JVI.75.14.6635-6644.2001. J Virol. 2001. PMID: 11413331 Free PMC article. - Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies.
Moore JP, Sattentau QJ, Wyatt R, Sodroski J. Moore JP, et al. J Virol. 1994 Jan;68(1):469-84. doi: 10.1128/JVI.68.1.469-484.1994. J Virol. 1994. PMID: 7504741 Free PMC article.
Cited by
- Reconstruction of a polyclonal ADCC antibody repertoire from an HIV-1 non-transmitting mother.
Yaffe ZA, Ding S, Sung K, Chohan V, Marchitto L, Doepker L, Ralph D, Nduati R, Matsen FA 4th, Finzi A, Overbaugh J. Yaffe ZA, et al. iScience. 2023 Apr 26;26(5):106762. doi: 10.1016/j.isci.2023.106762. eCollection 2023 May 19. iScience. 2023. PMID: 37216090 Free PMC article. - A Structural Update of Neutralizing Epitopes on the HIV Envelope, a Moving Target.
Parker Miller E, Finkelstein MT, Erdman MC, Seth PC, Fera D. Parker Miller E, et al. Viruses. 2021 Sep 5;13(9):1774. doi: 10.3390/v13091774. Viruses. 2021. PMID: 34578355 Free PMC article. Review. - HIV-1 Envelope Glycosylation and the Signal Peptide.
Lambert GS, Upadhyay C. Lambert GS, et al. Vaccines (Basel). 2021 Feb 19;9(2):176. doi: 10.3390/vaccines9020176. Vaccines (Basel). 2021. PMID: 33669676 Free PMC article. Review. - HIV-1 Envelope Glycoprotein Amino Acids Signatures Associated with Clade B Transmitted/Founder and Recent Viruses.
Kafando A, Martineau C, El-Far M, Fournier E, Doualla-Bell F, Serhir B, Kazienga A, Sangaré MN, Sylla M, Chamberland A, Charest H, Tremblay CL. Kafando A, et al. Viruses. 2019 Nov 1;11(11):1012. doi: 10.3390/v11111012. Viruses. 2019. PMID: 31683782 Free PMC article. - A New Family of Small-Molecule CD4-Mimetic Compounds Contacts Highly Conserved Aspartic Acid 368 of HIV-1 gp120 and Mediates Antibody-Dependent Cellular Cytotoxicity.
Ding S, Grenier MC, Tolbert WD, Vézina D, Sherburn R, Richard J, Prévost J, Chapleau JP, Gendron-Lepage G, Medjahed H, Abrams C, Sodroski J, Pazgier M, Smith AB 3rd, Finzi A. Ding S, et al. J Virol. 2019 Nov 26;93(24):e01325-19. doi: 10.1128/JVI.01325-19. Print 2019 Dec 15. J Virol. 2019. PMID: 31554684 Free PMC article.
References
- Biophys J. 1968 Jan;8(1):29-39 - PubMed
- AIDS Res Hum Retroviruses. 1994 Apr;10(4):371-81 - PubMed
- J Mol Biol. 1984 Oct 15;179(1):125-42 - PubMed
- Science. 1986 Jan 24;231(4736):382-5 - PubMed
- Cell. 1986 Jun 6;45(5):637-48 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous