Home LiteratureArticle Details
PMID: 7514319 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Antibody responses to HIV-1 envelope and gag epitopes in HIV-1 seroconverters with rapid versus slow disease progression.

Virology ·Vol. 201 ·No. 2 ·1994-06-00 ·Pages 285-93

Zwart G, van der Hoek L, Valk M, Cornelissen MT, Baan E, Dekker J, Koot M, Kuiken CL, Goudsmit J

Abstract

We studied the relationship between the rate of disease progression after HIV-1 seroconversion and the level of IgG antibody response to HIV-1 envelope and core epitopes. This was done by comparing a group of fast-progressing individuals and a group of slow-progressing individuals for serum IgG titers to peptides from the gp120-V3 neutralization domain, to a peptide from the immunodominant gp41 epitope (residues 590 to 607), and to recombinant gp120 and p24. The two groups displayed a large overlap in titers to the envelope epitopes, which precluded their differentiation at most time points after seroconversion. Low responsiveness to envelope antigens was not only found in a few fast-progressors but also in one individual who remained asymptomatic for at least 92 months after seroconversion. The only significant differences between the groups were found in the first months after seroconversion when the responses to the V3 domain and the gp41 epitope were more vigorous in the group of fast-progressors. Furthermore, on evaluating ratios of anti-V3 antibody titers to anti-gp120 antibody titers we found no indication that fast disease progression was associated with a restriction in antibody response to the V3 epitope. We did confirm the finding that fast disease progression is associated with low levels of p24-directed antibodies, both early after seroconversion and at later stages. These data demonstrate that levels of IgG antibodies to envelope epitopes are poor predictors of rapid disease progression and suggest that the role of V3-directed neutralizing antibodies in preventing subversion of the immune system is not decisive in natural HIV-1 infection.

MeSH Terms
Adult Amino Acid Sequence Animals CHO Cells Cohort Studies Cricetinae Enzyme-Linked Immunosorbent Assay Epitopes/immunology HIV Antibodies/biosynthesis,immunology HIV Core Protein p24/immunology HIV Envelope Protein gp120/immunology HIV Envelope Protein gp41/immunology HIV Seropositivity/immunology,physiopathology HIV-1/immunology Humans Male Molecular Sequence Data Peptide Fragments/immunology Recombinant Proteins/immunology Sequence Homology, Amino Acid
Chemicals
Epitopes HIV Antibodies HIV Core Protein p24 HIV Envelope Protein gp120 HIV Envelope Protein gp41 HIV envelope protein gp120 (305-321) Peptide Fragments Recombinant Proteins
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Zwart G
Department of Virology, Academic Medical Center, University of Amsterdam, The Netherlands.
van der Hoek L
Valk M
Cornelissen M T
Baan E
Dekker J
Koot M
Kuiken C L
Goudsmit J
Article Info
Journal
Virology
Abbr.
Virology
ISSN
0042-6822
Published
1994-06-00
Pages
285-93
Language
English
Region
United States
NLM ID
0110674
Subset
IM
Databases
GENBANK
U05786, U05787, U05788, U05789, U05790, U05791, U05792, U05793, U05794, U05795, U05796, U05797, U05798, U05799, U05800, U05801, U05802, U05803, U05804, U05805, U05806, U05807, U05808
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com