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VanZ Reduces the Binding of Lipoglycopeptide Antibiotics to Staphylococcus aureus and Streptococcus pneumoniae Cells
- 1.0524558 - MBÚ 2021 RIV CH eng J - Journal Article
Vimberg, Vladimír - Zieglerová, Leona - Buriánková, Karolína - Branny, Pavel - Balíková Novotná, Gabriela
VanZ Reduces the Binding of Lipoglycopeptide Antibiotics to Staphylococcus aureus and Streptococcus pneumoniae Cells.
Frontiers in Microbiology. Roč. 11, APR 3 (2020), č. článku 566. ISSN 1664-302X. E-ISSN 1664-302X
R&D Projects: GA MZd(CZ) NV15-28807A; GA ČR(CZ) GA19-03269S; GA MŠMT(CZ) ED1.1.00/02.0109
Institutional support: RVO:61388971
Keywords : Staphylococcus aureus * Streptococcus pneumoniae * antibiotic resistance
OECD category: Microbiology
Impact factor: 5.640, year: 2020
Method of publishing: Open access
https://www.frontiersin.org/articles/10.3389/fmicb.2020.00566/full
vanZ, a member of the VanA glycopeptide resistance gene cluster, confers resistance to lipoglycopeptide antibiotics independent of cell wall precursor modification by the vanHAX genes. Orthologs of vanZ are present in the genomes of many clinically relevant bacteria, including Enterococcus faecium and Streptococcus pneumoniae, however, vanZ genes are absent in Staphylococcus aureus. Here, we show that the expression of enterococcal vanZ paralogs in S. aureus increases the minimal inhibitory concentrations of lipoglycopeptide antibiotics teicoplanin, dalbavancin, oritavancin and new teicoplanin pseudoaglycone derivatives. The reduction in the binding of fluorescently labeled teicoplanin to the cells suggests the mechanism of VanZ-mediated resistance. In addition, using a genomic vanZ gene knockout mutant of S. pneumoniae, we have shown that the ability of VanZ proteins to compromise the activity of lipoglycopeptide antibiotics by reducing their binding is a more general feature of VanZ-superfamily proteins.
Permanent Link: http://hdl.handle.net/11104/0308900
Number of the records: 1