Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain

Gene

Volumn 443, Issue 1-2, 2009, Pages 32-41

  Becker, Stephen C ^a   Foster Frey, Juli ^a   Stodola, Angeline J ^a   Anacker, Daniel ^a   Donovan, David M ^a  

^a AGRICULTURAL RESEARCH SERVICE   (United States)

Author keywords

Autolysin; Bacteriophage endolysin; Peptidoglycan hydrolase; Phage introns; Staphylococcus aureus; Streptococcus uberis

Indexed keywords

BACTERIOCIN; PROTEIN SH3; PROTEIN SH3B 5; PROTEINASE; UNCLASSIFIED DRUG;

ANTIMICROBIAL ACTIVITY; ARTICLE; BACTERIAL CELL WALL; BACTERIOLYSIS; BACTERIOPHAGE; CONTROLLED STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROPHAGE; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SEQUENCE DATABASE; STAPHYLOCOCCUS AUREUS; STREPTOCOCCUS AGALACTIAE; STREPTOCOCCUS UBERIS; UNINDEXED SEQUENCE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BACTERIOPHAGES; ENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; STAPHYLOCOCCUS; STREPTOCOCCUS;

STAPHYLOCOCCUS AUREUS; STREPTOCOCCUS UBERIS;

EID: 67549109077     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2009.04.023     Document Type: Article

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