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Localization of CD4+ T cell epitope hotspots to exposed strands of HIV envelope glycoprotein suggests structural influences on antigen processing
- Publication Year :
- 2001
- Publisher :
- National Academy of Sciences, 2001.
-
Abstract
- The spectrum of immunogenic epitopes presented by the H2-IAbMHC class II molecule to CD4+T cells has been defined for two different (clade B and clade D) HIV envelope (gp140) glycoproteins. Hybridoma T cell lines were generated from mice immunized by a sequential prime and boost regime with DNA, recombinant vaccinia viruses, and protein. The epitopes recognized by reactive T cell hybridomas then were characterized with overlapping peptides synthesized to span the entire gp140 sequence. Evidence of clonality also was assessed with antibodies to T cell receptor Vα and Vβ chains. A total of 80 unique clonotypes were characterized from six individual mice. Immunogenic peptides were identified within only four regions of the HIV envelope. These epitope hotspots comprised relatively short sequences (≈20–80 aa in length) that were generally bordered by regions of heavy glycosylation. Analysis in the context of the gp120 crystal structure showed a pattern of uniform distribution to exposed, nonhelical strands of the protein. A likely explanation is that the physical location of the peptide within the native protein leads to differential antigen processing and consequent epitope selection.
- Subjects :
- CD4-Positive T-Lymphocytes
Models, Molecular
HIV Antigens
T cell
Molecular Sequence Data
Epitope
Epitopes
Mice
medicine
Animals
Amino Acid Sequence
Peptide sequence
B cell
chemistry.chemical_classification
Multidisciplinary
biology
Sequence Homology, Amino Acid
Antigen processing
T-cell receptor
env Gene Products, Human Immunodeficiency Virus
Gene Products, env
Biological Sciences
Virology
Molecular biology
Mice, Inbred C57BL
medicine.anatomical_structure
chemistry
biology.protein
Female
Antibody
Glycoprotein
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....7a900ed6d0a60acd8b3a868df96de66a