A Vibrio cholerae BolA-Like Protein Is Required for Proper Cell Shape and Cell Envelope Integrity

التفاصيل البيبلوغرافية
العنوان: A Vibrio cholerae BolA-Like Protein Is Required for Proper Cell Shape and Cell Envelope Integrity
المؤلفون: Libin Xu, Abdelrahim Zoued, Matthew K. Waldor, Felipe Cava, Laura Alvarez, Kelly M. Hines, Aurore Fleurie, Brigid M. Davis
المصدر: mBio
mBio, Vol 10, Iss 4 (2019)
mBio, Vol 10, Iss 4, p e00790-19 (2019)
بيانات النشر: American Society for Microbiology, 2019.
سنة النشر: 2019
مصطلحات موضوعية: Iron-Sulfur Proteins, Molecular Biology and Physiology, cell envelope, Protein family, Iron–sulfur cluster, Peptidoglycan, Biology, medicine.disease_cause, Microbiology, cell shape, 03 medical and health sciences, chemistry.chemical_compound, iron-sulfur cluster, Mice, Bacterial Proteins, Cell Wall, Virology, medicine, Animals, Homeostasis, Cell shape, Vibrio cholerae, 030304 developmental biology, 0303 health sciences, 030306 microbiology, Cell Membrane, biology.organism_classification, Phenotype, QR1-502, 3. Good health, Cell biology, Animals, Suckling, Intestines, chemistry, Mutation, BolA, Cell envelope, IbaG, Bacteria, Research Article
الوصف: BolA-like proteins are conserved across prokaryotes and eukaryotes. These proteins have been linked to a variety of phenotypes, but the pathways and mechanisms through which they act have not been extensively characterized. Here, we unraveled the role of the BolA-like protein IbaG in the cholera pathogen Vibrio cholerae. The absence of IbaG was associated with dramatic changes in cell morphology, sensitivity to envelope stressors, and intestinal colonization defects. IbaG was found to be required for biogenesis of several components of the V. cholerae cell envelope and to interact with numerous iron-sulfur cluster-containing proteins and factors involved in their assembly. Thus, our findings suggest that IbaG governs V. cholerae cell shape and cell envelope homeostasis through its effects on iron-sulfur proteins and associated pathways. The diversity of processes involving iron-sulfur-containing proteins is likely a factor underlying the range of phenotypes associated with BolA family proteins.
BolA family proteins are conserved in Gram-negative bacteria and many eukaryotes. While diverse cellular phenotypes have been linked to this protein family, the molecular pathways through which these proteins mediate their effects are not well described. Here, we investigated the roles of BolA family proteins in Vibrio cholerae, the cholera pathogen. Like Escherichia coli, V. cholerae encodes two BolA proteins, BolA and IbaG. However, in marked contrast to E. coli, where bolA is linked to cell shape and ibaG is not, in V. cholerae, bolA mutants lack morphological defects, whereas ibaG proved critical for the generation and/or maintenance of the pathogen’s morphology. Notably, the bizarre-shaped, multipolar, elongated, and wide cells that predominated in exponential-phase ΔibaG V. cholerae cultures were not observed in stationary-phase cultures. The V. cholerae ΔibaG mutant exhibited increased sensitivity to cell envelope stressors, including cell wall-acting antibiotics and bile, and was defective in intestinal colonization. ΔibaG V. cholerae had reduced peptidoglycan and lipid II and altered outer membrane lipids, likely contributing to the mutant’s morphological defects and sensitivity to envelope stressors. Transposon insertion sequencing analysis of ibaG’s genetic interactions suggested that ibaG is involved in several processes involved in the generation and homeostasis of the cell envelope. Furthermore, copurification studies revealed that IbaG interacts with proteins containing iron-sulfur clusters or involved in their assembly. Collectively, our findings suggest that V. cholerae IbaG controls cell morphology and cell envelope integrity through its role in biogenesis or trafficking of iron-sulfur cluster proteins.
اللغة: English
تدمد: 2150-7511
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8802a9008e38e90cbc3128e2984e74e0
http://europepmc.org/articles/PMC6747721
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....8802a9008e38e90cbc3128e2984e74e0
قاعدة البيانات: OpenAIRE