Research articles

Crystal structure of cytotoxin protein suilysin from Streptococcus suis

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  • 1.National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China; 2.College of Biotechnology, Southwest University, Chongqing 400715, China;State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Communicable Disease Control and Prevention, Beijing 102200, China; 3.Protein Studies Program, Oklahoma Medical Research Foundation, 825 N.E. 13th street, Oklahoma City, OK 73104, USA; 4.State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Communicable Disease Control and Prevention, Beijing 102200, China;

Published date: 01 Jan 2010

Abstract

Cholesterol-dependent cytolysins (CDC) are pore forming toxins. A prototype of the CDC family members is perfringolysin O (PFO), which directly binds to cholesterol rich cell membrane and lyses the cell. However, as an exception of this general observation, Streptococcus intermedius intermedilysin (ILY) requires human CD59 as its receptor in addition to cholesterol when exhibiting hemolytic activity. It was attempted to explain this functional difference based on a conformational variation in the C-terminal domain of the two toxin proteins, particularly a highly conserved undecapeptide termed tryptophan rich motif. Here, we present the crystal structure of suilysin, a CDC toxin from the swine infectious pathogen Streptococcus suis. Like PFO, suilysin does not require a host receptor for hemolytic activity; yet in the suilysin crystal it shares a similar conformation in the tryptophan rich motif with ILY. This observation suggests that current views of structure-function relationship of CDC proteins in membrane association are still far from complete.

Cite this article

Lingfeng Xu, Bo Huang, Xuemei Li, Zihe Rao, Huamao Du, Xuejun C. Zhang, Jianguo Xu, . Crystal structure of cytotoxin protein suilysin from Streptococcus suis[J]. Protein & Cell, 2010 , 1(1) : 96 -105 . DOI: 10.1007/s13238-010-0012-3

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