Cited by 319Bacterial Genetics and BiotechnologyAntimicrobial Resistance in StaphylococcusAntimicrobial Peptides and Activities

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Daptomycin-Mediated Reorganization of Membrane Architecture Causes Mislocalization of Essential Cell Division Proteins

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Pogliano, J., Pogliano, N., Silverman, J. A.·2012·Journal of Bacteriology

DOI 10.1128/jb.00011-12PMC PMC3415520

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Abstract

Daptomycin is a lipopeptide antibiotic used clinically for the treatment of certain types of Gram-positive infections, including those caused by methicillin-resistant Staphylococcus aureus (MRSA). Details of the mechanism of action of daptomycin continue to be elucidated, particularly the question of whether daptomycin acts on the cell membrane, the cell wall, or both. Here, we use fluorescence microscopy to directly visualize the interaction of daptomycin with the model Gram-positive bacterium Bacillus subtilis. We show that the first observable cellular effects are the formation of membrane distortions (patches of membrane) that precede cell death by more than 30 min. Membrane patches are able to recruit the essential cell division protein DivIVA. Recruitment of DivIVA correlates with membrane defects and changes in cell morphology, suggesting a localized alteration in the activity of enzymes involved in cell wall synthesis that could account for previously described effects of daptomycin on cell wall morphology and septation. Membrane defects colocalize with fluorescently labeled daptomycin, DivIVA, and fluorescent reporters of peptidoglycan biogenesis (Bocillin FL and BODIPY FL-vancomycin), suggesting that daptomycin plays a direct role in these events. Our results support a mechanism for daptomycin with a primary effect on cell membranes that in turn redirects the localization of proteins involved in cell division and cell wall synthesis, causing dramatic cell wall and membrane defects, which may ultimately lead to a breach in the cell membrane and cell death. These results help resolve the longstanding questions regarding the mechanism of action of this important class of antibiotics.

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Authors: Pogliano, J., Pogliano, N., & Silverman, J. A.
Affiliations: University of California San Diego (US)
Cubist Pharmaceuticals (United States) (US)
ORCID: Pogliano, J.
Venue: Journal of Bacteriology
Publisher: American Society for Microbiology
Published: 2012-06-01
Volume: 194
Issue: 17
Pages: 4494-4504
ISSN: 0021-9193 (ISSN-L)
DOI: 10.1128/jb.00011-12
PMC: PMC3415520
OpenAlex: W2113063737
Cited by: 319
References: 59
Citations by year: 2026: 8 · 2025: 10 · 2024: 23 · 2023: 19 · 2022: 23 · 2021: 22 · 2020: 27 · 2019: 27 · 2018: 23 · 2017: 30 · 2016: 30 · 2015: 29 · 2014: 25 · 2013: 18 · 2012: 5
FWCI: 14.84
Type: journal article
Language: en
Open access: green
europepmc.org
Locations: Journal of Bacteriology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (R01GM073898, GM073898)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
Keywords: daptomycin, antibiotic mechanism of action, membrane deformation, DivIVA, cell division proteins, cell wall biosynthesis, Bacillus subtilis, methicillin-resistant Staphylococcus aureus, cell morphology, septation
MeSH terms: Anti-Bacterial Agents, Bacillus subtilis, Bacterial Proteins, Cell Division, Cell Membrane, Cell Wall, Microbial Sensitivity Tests, Microscopy, Fluorescence, Peptidoglycan, Daptomycin, Cell Cycle Proteins

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Daptomycin-Mediated Reorganization of Membrane Architecture Causes Mislocalization of Essential Cell Division Proteins

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