Enterocin X, a Novel Two-Peptide Bacteriocin from Enterococcus faecium KU-B5, Has an Antibacterial Spectrum Entirely Different from Those of Its Component Peptides

Autor:	Wanna Malaphan, Jiro Nakayama, Kenji Sonomoto, Chih Bo Hu, Takeshi Zendo
Rok vydání:	2010
Předmět:	Bridged-Ring Compounds Enterococcus faecium Molecular Sequence Data Genetics and Molecular Biology Peptide Microbial Sensitivity Tests Applied Microbiology and Biotechnology Bacteriocins Bacteriocin Amino Acid Sequence Peptide sequence Antibacterial agent chemistry.chemical_classification Bacteria Base Sequence Ecology biology food and beverages Drug Synergism Sequence Analysis DNA biochemical phenomena metabolism and nutrition Streptococcaceae biology.organism_classification Anti-Bacterial Agents Biochemistry chemistry bacteria Peptides Antibacterial activity Drug Antagonism Food Science Biotechnology
Zdroj:	Applied and Environmental Microbiology. 76:4542-4545
ISSN:	1098-5336 0099-2240
DOI:	10.1128/aem.02264-09
Popis:	Enterocin X, composed of two antibacterial peptides (Xα and Xβ), is a novel class IIb bacteriocin from Enterococcus faecium KU-B5. When combined, Xα and Xβ display variably enhanced or reduced antibacterial activity toward a panel of indicators compared to each peptide individually. In E. faecium strains that produce enterocins A and B, such as KU-B5, only one additional bacteriocin had previously been known.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b44f378c489b7373c6174c5bd784ea78 https://doi.org/10.1128/aem.02264-09 Zobrazit plný text záznamu