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Confirmation of cross-reactivity between Lyme antibody H9724 and human heat shock protein 60 by a combinatorial approach.

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Abstract


A library of Ac-XXXXXPAPRM decapeptides was prepared on a TentaGel solid support using the approach of split synthesis and the strategy of partial chain termination. Epitope screening of the library (17(5) approximately 1.4 x 10(6) decapeptides) with a
Lyme monoclonal antibody (H9724) and subsequent MALDI-MS analysis of candidate peptides from colored beads revealed a consensus structure of Xi-DLSXj (Xi = V, L, Y; Xj = G, R). These identified sequences presented no homology to the natural epitope from Borrelia burgdorferi flagellin. However, they were found to resemble a fragment at the N-terminus of human heat shock protein (Hsp60). Our results confirmed that H9724 cross-reacts between bacterial and human proteins and provided support for an autoimmunity mechanism of
Lyme disease.

Anal Chem. 1997 Nov 15;69(22):4515-8. Research Support, Non-U.S. Gov’t

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