Retrocyclins neutralize bacterial toxins by potentiating their unfolding

Author:

Kudryashova Elena1,Seveau Stephanie23,Lu Wuyuan4,Kudryashov Dmitri S.156

Affiliation:

1. Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, U.S.A.

2. Department of Microbiology, The Ohio State University, Columbus, OH 43210, U.S.A.

3. Department of Microbial Infection and Immunity, The Ohio State University, Columbus, OH 43210, U.S.A.

4. Institute of Human Virology and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, U.S.A.

5. Center for Microbial Interface Biology, The Ohio State University, Columbus, OH 43210, U.S.A.

6. Public Health Preparedness for Infectious Diseases Program, The Ohio State University, Columbus, OH 43210, U.S.A.

Abstract

We demonstrate that retrocyclins (RCs), promising therapeutic peptides, neutralize bacterial toxins by inducing their unfolding and exposing hydrophobic regions, normally buried in the molecule interior, to solvents. RC-induced toxin unfolding leads to toxin precipitation, proneness to proteolytic degradation and abrogated activity.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference56 articles.

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4. Theta-defensins prevent HIV-1 Env-mediated fusion by binding gp41 and blocking 6-helix bundle formation;Gallo;J. Biol. Chem.,2006

5. The theta-defensin, retrocyclin, inhibits HIV-1 entry;Munk;AIDS Res. Hum. Retroviruses,2003

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