Biochemical Society Focused Meeting
Heat shock proteins (HSPs) play essential roles in protein folding and membrane translocation. In the last few years it has become clear that in addition to the well-characterised chaperone activity, HSPs are potent stimulators of adaptive immune responses. HSPs can efficiently introduce antigen into both MHC class I and MHC class II processing pathways following receptor-mediated uptake of HSP-antigen complexes. Moreover HSPs also stimulate maturation of dendritic cells and production of chemokines and cytokines. They therefore form a link between innate and adaptive immunity. These novel properties of HSPs are being exploited in the development of new approaches to vaccination and cancer therapy.
Significant developments have come from determination of the 3-D structures of a number of HSPs, and the determination of the basis of interaction with substrate and definition of cellular receptors that mediate endocytosis and chemokine or cytokine production. This one day meeting is therefore timely and will bring together leading workers in these areas.
Proceedings will be published in Biochemical Society Transactions
Note: Early Registration Deadline 16 March 2004
Register early to avoid disappointment.
Poster Abstracts will be available to view on-line 2 weeks before the meeting.
Image of 'Surface representation of an unliganded section of GroEL', kindly supplied by Helen Saibil (Birkbeck College, London, UK). "Reprinted from CELL, Vol 107, 869-878, figure 3a. N.A. Ranson et al (2001) ATP-bound states of GroEL captured by cryo-electron microscopy, with permission from Elsevier."
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