期刊
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
卷 57, 期 8, 页码 3917-3922出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.00862-13
关键词
-
资金
- Deutsche Forschungsgemeinschaft [ER47-13]
- BMBF-ERA-NET PathoGeNoMics project Glycoshield
- BMBF-ERA-NET PathoGeNoMics project OXYstress
- Peter & Traudl Engelhorn fellowship
The human fungal pathogen Candida albicans releases a large glycofragment of the Msb2 surface protein (Msb2*) into the growth environment, which protects against the action of human antimicrobial peptides (AMPs) LL-37 and histatin-5. Quantitation of Msb2*/LL-37 interactions by microscale thermophoresis revealed high-affinity binding (dissociation constant [K-D] = 73 nM), which was lost or greatly diminished by lack of O-glycosylation or by Msb2* denaturation. Msb2* also interacted with human alpha- and beta-defensins and protected C. albicans against these AMPs. In addition, the lipopeptide antibiotic daptomycin was bound and inactivated by Msb2*, which prevented the killing of bacterial pathogens Staphylococcus aureus, Enterococcus faecalis, and Corynebacterium pseudodiphtheriticum. In coculturings or mixed biofilms of S. aureus with C. albicans wild-type but not msb2 mutant strains, the protective effects of Msb2* on the bactericidal action of daptomycin were demonstrated. These results suggest that tight binding of shed Msb2* to AMPs that occurs during bacterial coinfections with C. albicans compromises antibacterial therapy by inactivating a relevant reserve antibiotic.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据