A Choline-Recognizing Monomeric Lysin, ClyJ-3m, Shows Elevated Activity against Streptococcus pneumoniae

Author:

Luo Dehua1,Huang Li2,Gondil Vijay Singh3,Zhou Wanli3,Yang Wan1,Jia Minghui1,Hu Shencai2,He Jin1,Yang Hang34,Wei Hongping34ORCID

Affiliation:

1. State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China

2. School of Biological and Pharmaceutical Engineering, Wuhan Polytechnic University, Wuhan, China

3. CAS Key Laboratory of Special Pathogens and Biosafety, Center for Emerging Infectious Diseases, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, China

4. University of the Chinese Academy of Sciences, Beijing, China

Abstract

Streptococcus pneumoniae is a leading pathogen for bacterial pneumonia, which can be treated with bacteriophage lysins harboring a conserved choline binding module (CBM). Such lysins regularly function as choline-recognizing dimers. Previously, we reported a pneumococcus-specific lysin ClyJ comprising the binding domain from the putative endolysin gp20 from the Streptococcus phage SPSL1 and the CHAP (cysteine, histidine-dependent amidohydrolase/peptidase) catalytic domain from the PlyC lysin.

Funder

Youth Innovation Promotion Association of the Chinese Academy of Sciences

National Natural Science Foundation of China

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

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