Candida albicans mucin Msb2 is a broad-range protectant against antimicrobial peptides
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 thermophore...
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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
3 June 2013
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| In: |
Antimicrobial agents and chemotherapy
Year: 2013, Volume: 57, Issue: 8, Pages: 3917-3922 |
| ISSN: | 1098-6596 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://journals.asm.org/doi/abs/10.1128/AAC.00862-13
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| Author Notes: | Marc Swidergall, Andreas M. Ernst, and Joachim F. Ernst |
| Summary: | 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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| Item Description: | Gesehen am 27.01.2022 |
| Physical Description: | Online Resource |
| ISSN: | 1098-6596 |