Enhancement of the enterocin CRL35 activity by a synthetic peptide derived from the NH2-terminal sequence.
The enterocin CRL35 biosynthetic gene cluster was cloned and sequenced. The sequence was revealed to be highly identical to that of the mundticin KS gene cluster (S. Kawamoto, J. Shima, R. Sato, T. Eguchi, S. Ohmomo, J. Shibato, N. Horikoshi, K. Takeshita, and T. Sameshima, Appl. Environ. Microbiol. 68:3830-3840, 2002). Short synthetic peptides were designed based on the bacteriocin sequence and were evaluated in antimicrobial competitive assays. The peptide KYYGNGVSCNKKGCS produced an enhancement of enterocin CRL35 antimicrobial activity in a buffer system.
Saavedra
Lucila
L
Centro de Referencia para Lactobacilos (CERELA-CONICET), S.M. de Tucumán (4000), Chacabuco 145, Tucumán, Argentina.
Minahk
Carlos
C
de Ruiz Holgado
Aída P
AP
Sesma
Fernando
F
D000595:Amino Acid Sequence; D001430:Bacteriocins / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology*; D017931:DNA Primers; D004357:Drug Synergism; D016983:Enterococcus / Q000235:genetics; D008087:Listeria / Q000187:drug effects; D008564:Membrane Potentials / Q000187:drug effects; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000494:pharmacology*; D020133:Reverse Transcriptase Polymerase Chain Reaction
D001430:Bacteriocins; D017931:DNA Primers; D010455:Peptides; C121783:enterocin CRL35