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Susceptibility difference between methicillin‐susceptible and methicillin‐resistant S taphylococcus aureus to a bovine myeloid antimicrobial peptide ( BMAP ‐28)
Author(s) -
Takagi Shiaki,
Nishimura Junko,
Bai Lanlan,
Miyagi Hikaru,
Kuroda Kengo,
Hayashi Shunji,
Yoneyama Hiroshi,
Ando Tasuke,
Isogai Hiroshi,
Isogai Emiko
Publication year - 2014
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1111/asj.12098
Subject(s) - antimicrobial , staphylococcus aureus , cathelicidin , peptide , microbiology and biotechnology , palmitic acid , antimicrobial peptides , chemistry , fatty acid , biology , biochemistry , bacteria , genetics
A bovine myeloid antimicrobial peptide antimicrobial peptide ( BMAP ‐28) is a member of the cathelicidin family and acts as a component of innate immunity. There are few reports of susceptibility difference of methicillin‐resistant S taphylococcus aureus ( MRSA ) and susceptible strains ( MSSA ) against BMAP ‐28. This study aims to clarify how a few amino acid substitutions of BMAP ‐28 are related to its antimicrobial activity using four analog peptides of BMAP ‐28. We also compared cellular fatty acid components of MSSA and MRSA using gas chromatography. We found that a few amino acid substitutions of BMAP ‐28 do not change antimicrobial activity. It was also revealed that the percentage of cis‐11‐eicosenoic acid in total detected fatty acids of MRSA was significantly higher than that of MSSA . In addition, the percentage of palmitic acid in total detected fatty acids of MRSA tended to be lower than that of MSSA . Our results will provide new information to deal with the question of differences in bacterial susceptibility against BMAP ‐28.