T cell epitope 'hotspots' on the HIV Type 1 gp120 envelope protein overlap with tryptic fragments displayed by mass spectrometry
| Autor: | Clive A. Slaughter, Karen S. Slobod, Amy Zirkel, Scott A. Brown, Timothy D. Lockey, Peter C. Doherty, Ashutosh Mishra, Sherri L. Surman, Julia L. Hurwitz, Chris Coleclough, Vishwajeeth Pagala |
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| Rok vydání: | 2005 |
| Předmět: |
T cell
Immunology Antigen presentation Molecular Sequence Data Epitopes T-Lymphocyte Peptide Biology HIV Envelope Protein gp120 Epitope Mass Spectrometry Mice Virology medicine Animals Trypsin Amino Acid Sequence Peptide sequence chemistry.chemical_classification AIDS Vaccines Mice Inbred BALB C Antigen processing Immunodominant Epitopes T lymphocyte HIV envelope protein Molecular biology Peptide Fragments Mice Inbred C57BL Infectious Diseases medicine.anatomical_structure chemistry |
| Zdroj: | AIDS research and human retroviruses. 21(2) |
| ISSN: | 0889-2229 |
| Popis: | Our previous work has shown that immunodominant T-helper cell epitopes cluster within distinct fragments on a single face of the HIV envelope gp120 protein. We show in this report that the general positions of immunodominant epitopes are shared by T cells derived from BALB/c, C57BL/6, and CB6F1 mice, yet the precise peptides recognized by the responding T cell populations may differ. In addition, we find that gp120 peptides displayed by tryptic digestion and mass spectrometry of a purified HIV envelope protein share location with peptides defined as immunodominant T cell targets. Results are consistent with the suggestion that gp120 peptide location influences antigen processing, which, in turn, influences the specificity of immunodominant T cells. |
| Databáze: | OpenAIRE |
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