Crystal structure of the choline-binding protein CbpJ from Streptococcus pneumoniae

Qian Xu; Jun-Wei Zhang; Yuxing Chen; Qiong Li; Yong-Liang Jiang

doi:10.1016/j.bbrc.2019.05.053

Crystal structure of the choline-binding protein CbpJ from Streptococcus pneumoniae

Biochem Biophys Res Commun. 2019 Jul 5;514(4):1192-1197. doi: 10.1016/j.bbrc.2019.05.053. Epub 2019 May 16.

Authors

Qian Xu¹, Jun-Wei Zhang¹, Yuxing Chen¹, Qiong Li², Yong-Liang Jiang³

Affiliations

¹ Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, China.
² Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, China. Electronic address: liqiong@ustc.edu.cn.
³ Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, China. Electronic address: jyl@ustc.edu.cn.

PMID: 31104766
DOI: 10.1016/j.bbrc.2019.05.053

Abstract

The choline-binding proteins play essential roles in pneumococcal colonization and virulence. It has been suggested that the choline-binding protein J (termed CbpJ; encoded by the gene sp_0378) from Streptococcus pneumoniae TIGR4 involves in the colonization in host and contributes to evasion of neutrophil killing. Here we report the 2.0 Å crystal structure of CbpJ in complex with choline. CbpJ consists of an N-terminal putative functional domain (N-domain) followed by a C-terminal choline-binding domain (CBD). The N-domain harbors four degenerated choline-binding repeats (CBRs) that lose the capacity of binding to choline, whereas the CBD is composed of seven typical CBRs. Further functional assays showed that the CBD contributes to the pneumococcal adhesion to human lung epithelial cell A549. These findings provide insights into the pneumococcal pathogenesis and broaden our understanding on the functions of choline-binding proteins.

Keywords: Adhesion; Choline-binding proteins; Crystal structure; Streptococcus pneumoniae.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

A549 Cells
Adhesins, Bacterial / chemistry*
Bacterial Adhesion
Cell Adhesion
Choline / chemistry
Choline / metabolism
Crystallography, X-Ray
Humans
Models, Molecular
Streptococcus pneumoniae / chemistry*
Streptococcus pneumoniae / metabolism

Substances

Adhesins, Bacterial
choline-binding protein J, Streptococcus pneumoniae
Choline