Open AccessPermeases of the Sap Transporter Are Required for Cathelicidin Resistance and Virulence of Haemophilus ducreyi in Humans
Author(s) -
Sherri D. Rinker,
Xiaosong Gu,
Kate R. Fortney,
Beth Zwickl,
B. P. Katz,
D. M. Janowicz,
Stanley M. Spinola,
Margaret E. Bauer
Publication year - 2012
Publication title -
the journal of infectious diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.69
H-Index - 252
eISSN - 1537-6613
pISSN - 0022-1899
DOI - 10.1093/infdis/jis525
Subject(s) - mutant , permease , virulence , haemophilus ducreyi , membrane transport protein , microbiology and biotechnology , biology , transporter , periplasmic space , cathelicidin , atp binding cassette transporter , biochemistry , antimicrobial , haemophilus influenzae , escherichia coli , gene , antimicrobial peptides , pasteurellaceae , antibiotics
Haemophilus ducreyi encounters several classes of antimicrobial peptides (APs) in vivo and utilizes the sensitive-to-antimicrobial-peptides (Sap) transporter as one mechanism of AP resistance. A mutant lacking the periplasmic solute-binding component, SapA, was somewhat more sensitive to the cathelicidin LL-37 than the parent strain and was partially attenuated for virulence. The partial attenuation led us to question whether the transporter is fully abrogated in the sapA mutant.
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