The human antimicrobial peptide LL-37 binds directly to CsrS, a sensor histidine kinase of group a streptococcus, to activate expression of virulence factors

Journal of Biological Chemistry

Volumn 289, Issue 52, 2014, Pages 36315-36324

  Velarde, Jorge J ^a   Ashbaugh, Melissa ^a   Wessels, Michael R ^a  

^a BOSTON CHILDREN S HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; CELL MEMBRANES; CYTOLOGY; MICROORGANISMS; PEPTIDES; SIGNAL TRANSDUCTION; SIGNALING;

ANTI-MICROBIAL ACTIVITY; ANTIMICROBIAL PEPTIDE; BINDING INTERACTION; DIRECT INTERACTIONS; EXTRACELLULAR DOMAINS; SIGNALING MECHANISMS; TWO COMPONENT SYSTEMS; VIRULENCE FACTORS;

CELL SIGNALING;

CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; PROTEIN HISTIDINE KINASE; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; CATHELICIDIN; CATHELICIDIN ANTIMICROBIAL PEPTIDE; CSRS PROTEIN, BACTERIA; PROTEIN BINDING; PROTEIN KINASE; VIRULENCE FACTOR;

ANTIMICROBIAL ACTIVITY; ARTICLE; BACTERIAL MEMBRANE; BACTERIAL STRAIN; BACTERIAL VIRULENCE; BINDING AFFINITY; BINDING KINETICS; CELLULAR STRESS RESPONSE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; IN VITRO STUDY; MEMBRANE DAMAGE; MINIMUM BACTERICIDAL CONCENTRATION; NONHUMAN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; STREPTOCOCCUS GROUP A; UPREGULATION; AMINO ACID SEQUENCE; BIOSYNTHESIS; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; HUMAN; METABOLISM; MICROBIAL SENSITIVITY TEST; MOLECULAR GENETICS; PHYSIOLOGY; STREPTOCOCCUS PYOGENES; TRANSCRIPTION INITIATION;

BACTERIA (MICROORGANISMS); STREPTOCOCCUS SP. 'GROUP A';

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; CATHELICIDINS; GENE EXPRESSION REGULATION, BACTERIAL; HUMANS; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN KINASES; STREPTOCOCCUS PYOGENES; TRANSCRIPTIONAL ACTIVATION; UP-REGULATION; VIRULENCE FACTORS;

EID: 84919784538     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.605394     Document Type: Article

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