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Status: Bibliographieeintrag

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Verfasst von:Swidergall, Marc [VerfasserIn]   i
 Ernst, Andreas M. [VerfasserIn]   i
 Ernst, Joachim F. [VerfasserIn]   i
Titel:Candida albicans mucin Msb2 is a broad-range protectant against antimicrobial peptides
Verf.angabe:Marc Swidergall, Andreas M. Ernst, and Joachim F. Ernst
E-Jahr:2013
Jahr:3 June 2013
Umfang:6 S.
Fussnoten:Gesehen am 27.01.2022
Titel Quelle:Enthalten in: Antimicrobial agents and chemotherapy
Ort Quelle:Washington, DC : Soc., 1972
Jahr Quelle:2013
Band/Heft Quelle:57(2013), 8, Seite 3917-3922
ISSN Quelle:1098-6596
Abstract: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 [KD] = 73 nM), which was lost or greatly diminished by lack of O-glycosylation or by Msb2* denaturation. Msb2* also interacted with human α- and β-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.
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Volltext: https://journals.asm.org/doi/abs/10.1128/AAC.00862-13
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1787313581
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