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

Dehua Luo | Zendy; Li Huang | Zendy; Vijay Singh Gondil | Zendy; Wanli Zhou | Zendy; Wan Yang | Zendy; Minghui Jia | Zendy; Shencai Hu | Zendy; Jin He | Zendy; Hang Yang | Zendy; Hongping Wei | Zendy

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

Author(s) -

Dehua Luo,

Li Huang,

Vijay Singh Gondil,

Wanli Zhou,

Wan Yang,

Minghui Jia,

Shencai Hu,

Jin He,

Hang Yang,

Hongping Wei

Publication year - 2020

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.00311-20

Subject(s) - lysin , microbiology and biotechnology , streptococcus pneumoniae , bacteriophage , biology , biochemistry , chemistry , antibiotics , escherichia coli , gene

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 theStreptococcus phage SPSL1 and the CHAP (cysteine, histidine-dependent amidohydrolase/peptidase) catalytic domain from the PlyC lysin.

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