A peptide based on homologous sequences of the -barrel assembly machinery component BamD potentiates antibiotic susceptibility of Pseudomonas aeruginosa | Zendy

N. Môri | Zendy; Y. Ishii | Zendy; Tateda Kazuhiro | Zendy; Soichiro Kimura | Zendy; Yuichi Kouyama | Zendy; Hidetoshi Inoko | Zendy; Shigeki Mitsunaga | Zendy; K. Yamaguchi | Zendy; Eisaku Yoshihara | Zendy

Open Access

A peptide based on homologous sequences of the -barrel assembly machinery component BamD potentiates antibiotic susceptibility of Pseudomonas aeruginosa

Author(s) -

N. Môri,

Y. Ishii,

Tateda Kazuhiro,

Soichiro Kimura,

Yuichi Kouyama,

Hidetoshi Inoko,

Shigeki Mitsunaga,

K. Yamaguchi,

Eisaku Yoshihara

Publication year - 2012

Publication title -

journal of antimicrobial chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.124

H-Index - 194

eISSN - 1460-2091

pISSN - 0305-7453

DOI - 10.1093/jac/dks174

Subject(s) - pseudomonas aeruginosa , colistin , peptide , microbiology and biotechnology , bacterial outer membrane , biology , levofloxacin , antibiotics , peptide sequence , antimicrobial peptides , chemistry , antimicrobial , biochemistry , bacteria , escherichia coli , gene , genetics

The β-barrel assembly machinery (BAM) complex plays a critical role in outer membrane protein (OMP) biogenesis. The outer membrane (OM) of Pseudomonas aeruginosa is centrally involved in mechanisms of antibiotic resistance. This study aimed to identify effects of a synthetic peptide based on conserved sequences in the putative BamA-binding region of BamD, focusing on antibiotic susceptibility and OMP characteristics in P. aeruginosa.

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