Linker Editing of Pneumococcal Lysin ClyJ Conveys Improved Bactericidal Activity

Author:

Yang Hang12,Luo Dehua3,Etobayeva Irina24,Li Xiaohong1,Gong Yujing3,Wang Shujuan1,Li Qiong5,Xu Poshi67,Yin Wen3,He Jin3,Nelson Daniel C.24ORCID,Wei Hongping1

Affiliation:

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

2. Institute for Bioscience and Biotechnology Research, University of Maryland, Rockville, Maryland, USA

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

4. Department of Veterinary Medicine, University of Maryland, College Park, Maryland, USA

5. Wuhan Polytechnic University, Wuhan, China

6. Henan Provincial People's Hospital, Fuwai Central China Cardiovascular Hospital, Zhengzhou, Henan, China

7. School of Clinical Medicine, Henan University, Zhengzhou, Henan, China

Abstract

Streptococcus pneumoniae is a leading human pathogen uniquely characterized by choline moieties on the bacterial surface. Our previous work reported a pneumococcus-specific chimeric lysin, ClyJ, which combines the CHAP (cysteine, histidine-dependent amidohydrolase/peptidase) enzymatically active domain (EAD) from the PlyC lysin and the cell wall binding domain (CBD) from the phage SPSL1 lysin, which imparts choline binding specificity.

Funder

Open Research Fund Program of National Bio-Safety Laboratory, Wuhan

Youth Innovation Promotion Association of the Chinese Academy of Sciences

Natural Science Foundation of Henan Province

National Natural Science Foundation of China

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

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