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Heat shock protein mediates cross-presentation of exogenous HIV antigen.

Vaccine Weekly

| October 06, 2004 | COPYRIGHT 2004 NewsRX. This material is published under license from the publisher through the Gale Group, Farmington Hills, Michigan.  All inquiries regarding rights should be directed to the Gale Group. (Hide copyright information)Copyright

2004 OCT 6 - (NewsRx.com & NewsRx.net) -- Heat shock protein mediates cross-presentation of exogenous HIV antigen on HLA class I and class II.

According to a study from the United States, "Strong CD4+ and CD8+ T cell responses are considered important immune components for controlling HIV infection, and their priming may be central to an effective HIV vaccine. We describe in this study an approach by which multiple CD4+ and CD8+ T cell epitopes are processed and presented from an exogenously added HIV-1 Gag-p 4 peptide of 32 aa complexed to heat shock protein (HSP) gp96. CD8+ T cell recognition of the HSP/peptide complex, but not the peptide alone, was inhibited by brefeldin A, suggesting an endoplasmic reticulum-dependent pathway."

"This is the first report to describe efficient processing and simultaneous presentation of overlapping class I- and class II-restricted epitopes from the same extracellularly added precursor peptide complexed to HSP," said Devi SenGupta and collaborators at Harvard University, Antigenics, Inc., and the University of Connecticut.

"Given previous reports of the strong immunogenicity of HSP/peptide complexes, the present data suggest that HSP-complexed ...

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Source: HighBeam Research, Heat shock protein mediates cross-presentation of exogenous HIV...

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