| Title: |
Shaping T cell - B cell collaboration in the response to human immunodeficiency virus type 1 envelope glycoprotein gp120 by peptide priming. |
| Authors: |
N Kalaya Steede; Blake J Rust; Mohammad M Hossain; Lucy C Freytag; James E Robinson; Samuel J Landry |
| Source: |
PLoS ONE, Vol 8, Iss 6, p e65748 (2013) |
| Publisher Information: |
Public Library of Science (PLoS) |
| Publication Year: |
2013 |
| Collection: |
Directory of Open Access Journals: DOAJ Articles |
| Subject Terms: |
Medicine; Science |
| Description: |
Prime-boost vaccination regimes have shown promise for obtaining protective immunity to HIV. Poorly understood mechanisms of cellular immunity could be responsible for improved humoral responses. Although CD4+ T-cell help promotes B-cell development, the relationship of CD4+ T-cell specificity to antibody specificity has not been systematically investigated. Here, protein and peptide-specific immune responses to HIV-1 gp120 were characterized in groups of ten mucosally immunized BALB/c mice. Protein and peptide reactivity of serum antibody was tested for correlation with cytokine secretion by splenocytes restimulated with individual gp120 peptides. Antibody titer for gp120 correlated poorly with the peptide-stimulated T-cell response. In contrast, titers for conformational epitopes, measured as crossreactivity or CD4-blocking, correlated with average interleukin-2 and interleukin-5 production in response to gp120 peptides. Antibodies specific for conformational epitopes and individual gp120 peptides typically correlated with T-cell responses to several peptides. In order to modify the specificity of immune responses, animals were primed with a gp120 peptide prior to immunization with protein. Priming induced distinct peptide-specific correlations of antibodies and T-cells. The majority of correlated antibodies were specific for the primed peptides or other peptides nearby in the gp120 sequence. These studies suggest that the dominant B-cell subsets recruit the dominant T-cell subsets and that T-B collaborations can be shaped by epitope-specific priming. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| Relation: |
http://europepmc.org/articles/PMC3679139?pdf=render; https://doaj.org/toc/1932-6203; https://doaj.org/article/57096469cdc04b25aa27a7ce200509a2 |
| DOI: |
10.1371/journal.pone.0065748 |
| Availability: |
https://doi.org/10.1371/journal.pone.0065748; https://doaj.org/article/57096469cdc04b25aa27a7ce200509a2 |
| Accession Number: |
edsbas.BABCDBB3 |
| Database: |
BASE |