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Localization of CD4+ T Cell Epitope Hotspots to Exposed Strands of HIV Envelope Glycoprotein Suggests Structural Influences on Antigen Processing

Sherri Surman, Timothy D. Lockey, Karen S. Slobod, Bart Jones, Janice M. Riberdy, Stephen W. White, Peter C. Doherty and Julia L. Hurwitz
Proceedings of the National Academy of Sciences of the United States of America
Vol. 98, No. 8 (Apr. 10, 2001), pp. 4587-4592
Stable URL: http://www.jstor.org/stable/3055473
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Localization of CD4+ T Cell Epitope Hotspots to Exposed Strands of HIV Envelope Glycoprotein Suggests Structural Influences on Antigen Processing
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Abstract

The spectrum of immunogenic epitopes presented by the H2-IAb MHC 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.

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