Molecular dissection of phage lysin PlySs2: integrity of the catalytic and cell wall binding domains is essential for its broad lytic activity

Virologica Sinica

Volumn 30, Issue 1, 2015, Pages 45-51

  Huang, Yanling ^a   Yang, Hang ^a   Yu, Junping ^a   Wei, Hongping ^a  

^a WUHAN INSTITUTE OF VIROLOGY   (China)

Author keywords

bacterial resistance; catalytic domain; cell wall binding domain; lysin; streptococci

Indexed keywords

ENHANCED GREEN FLUORESCENT PROTEIN; VIRUS PROTEIN;

ARTICLE; BACTERIAL STRAIN; BACTERIOPHAGE; BINDING AFFINITY; CATALYSIS; CELL WALL; DONOR; ENTEROCOCCUS FAECIUM; ENZYME ACTIVE SITE; NONHUMAN; PHAGE LYSIN PLYSS2; STAPHYLOCOCCUS; STREPTOCOCCUS; STREPTOCOCCUS AGALACTIAE; STREPTOCOCCUS DYSGALACTIAE; STREPTOCOCCUS SUIS; CHEMISTRY; GENETICS; HOST RANGE; METABOLISM; PROTEIN TERTIARY STRUCTURE; VIROLOGY;

BACTERIA (MICROORGANISMS); LISTERIA; STAPHYLOCOCCUS;

BACTERIOPHAGES; CELL WALL; HOST SPECIFICITY; PROTEIN STRUCTURE, TERTIARY; STREPTOCOCCUS; VIRAL PROTEINS;

EID: 84923198695     PISSN: 16740769     EISSN: 1995820X     Source Type: Journal    
DOI: 10.1007/s12250-014-3535-6     Document Type: Article

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