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Originally published In Press as doi:10.1074/jbc.M107624200 on October 22, 2001

J. Biol. Chem., Vol. 277, Issue 1, 155-160, January 4, 2002
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Proteolytic Sensitivity and Helper T-cell Epitope Immunodominance Associated with the Mobile Loop in Hsp10s*

Stephanie Carmicle, Guixiang Dai, N. Kalaya Steede, and Samuel J. LandryDagger

From the Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, Louisiana 70112-2699

Antigen three-dimensional structure potentially limits antigen processing and presentation to helper T-cell epitopes. The association of helper T-cell epitopes with the mobile loop in Hsp10s from mycobacteria and bacteriophage T4 suggests that the mobile loop facilitates proteolytic processing and presentation of adjacent sequences. Sites of initial proteolytic cleavage were mapped in divergent Hsp10s after treatment with a variety of proteases including cathepsin S. Each protease preferentially cleaved the Hsp10s in the mobile loop. Flexibility in the 22-residue mobile loop most probably allows it to conform to protease active sites. Three variants of the bacteriophage T4 Hsp10 were constructed with deletions in the mobile loop to test the hypothesis that shorter loops would be less sensitive to proteolysis. The two largest deletions effectively inhibited proteolysis by several proteases. Circular dichroism spectra and chemical cross-linking of the deletion variants indicate that the secondary and quaternary structures of the variants are native-like, and all three variants were more thermostable than the wild-type Hsp10. Local structural flexibility appears to be a general requirement for proteolytic sensitivity, and thus, it could be an important factor in antigen processing and helper T-cell epitope immunogenicity.

* This work was supported by National Institutes of Health Grant R01-AI42350.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Biochemistry, Tulane University Health Sciences Center, 1430 Tulane Ave., New Orleans, LA 70112-2699. Tel.: 504-586-3990; Fax: 504-584-2739; E-mail: landry@tulane.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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