PBP4 Is Likely Involved in Cell Division of the Longitudinally Dividing Bacterium <i>Candidatus</i> Thiosymbion Oneisti
Peptidoglycan (PG) is essential for bacterial survival and maintaining cell shape. The rod-shaped model bacterium <i>Escherichia coli</i> has a set of seven endopeptidases that remodel the PG during cell growth. The gamma proteobacterium <i>Candidatus</i> Thiosymbion oneisti...
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MDPI AG
2021-03-01
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| Series: | Antibiotics |
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| Online Access: | https://www.mdpi.com/2079-6382/10/3/274 |
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| author | Jinglan Wang Laura Alvarez Silvia Bulgheresi Felipe Cava Tanneke den Blaauwen |
| author_facet | Jinglan Wang Laura Alvarez Silvia Bulgheresi Felipe Cava Tanneke den Blaauwen |
| author_sort | Jinglan Wang |
| collection | DOAJ |
| description | Peptidoglycan (PG) is essential for bacterial survival and maintaining cell shape. The rod-shaped model bacterium <i>Escherichia coli</i> has a set of seven endopeptidases that remodel the PG during cell growth. The gamma proteobacterium <i>Candidatus</i> Thiosymbion oneisti is also rod-shaped and attaches to the cuticle of its nematode host by one pole. It widens and divides by longitudinal fission using the canonical proteins MreB and FtsZ. The PG layer of <i>Ca</i>. T. oneisti has an unusually high peptide cross-linkage of 67% but relatively short glycan chains with an average length of 12 disaccharides. Curiously, it has only two predicted endopeptidases, MepA and PBP4. Cellular localization of symbiont PBP4 by fluorescently labeled antibodies reveals its polar localization and its accumulation at the constriction sites, suggesting that PBP4 is involved in PG biosynthesis during septum formation. Isolated symbiont PBP4 protein shows a different selectivity for β-lactams compared to its homologue from <i>E. coli</i>. Bocillin-FL binding by PBP4 is activated by some β-lactams, suggesting the presence of an allosteric binding site. Overall, our data point to a role of PBP4 in PG cleavage during the longitudinal cell division and to a PG that might have been adapted to the symbiotic lifestyle. |
| first_indexed | 2024-03-10T13:25:19Z |
| format | Article |
| id | doaj.art-9765110bff9b4a139799fe209f764ae3 |
| institution | Directory Open Access Journal |
| issn | 2079-6382 |
| language | English |
| last_indexed | 2024-03-10T13:25:19Z |
| publishDate | 2021-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antibiotics |
| spelling | doaj.art-9765110bff9b4a139799fe209f764ae32023-11-21T09:42:05ZengMDPI AGAntibiotics2079-63822021-03-0110327410.3390/antibiotics10030274PBP4 Is Likely Involved in Cell Division of the Longitudinally Dividing Bacterium <i>Candidatus</i> Thiosymbion OneistiJinglan Wang0Laura Alvarez1Silvia Bulgheresi2Felipe Cava3Tanneke den Blaauwen4Bacterial Cell Biology & Physiology, Faculty of Science, Swammerdam Institute for Life Sciences, University of Amsterdam, Science Park 904, 1098 XH Amsterdam, The NetherlandsDepartment of Molecular Biology, Umeå University, SE-901 87 Umeå, SwedenEnvironmental Cell Biology, University of Vienna, Althanstrasse 14 (UZA I), 1090 Vienna, AustriaDepartment of Molecular Biology, Umeå University, SE-901 87 Umeå, SwedenBacterial Cell Biology & Physiology, Faculty of Science, Swammerdam Institute for Life Sciences, University of Amsterdam, Science Park 904, 1098 XH Amsterdam, The NetherlandsPeptidoglycan (PG) is essential for bacterial survival and maintaining cell shape. The rod-shaped model bacterium <i>Escherichia coli</i> has a set of seven endopeptidases that remodel the PG during cell growth. The gamma proteobacterium <i>Candidatus</i> Thiosymbion oneisti is also rod-shaped and attaches to the cuticle of its nematode host by one pole. It widens and divides by longitudinal fission using the canonical proteins MreB and FtsZ. The PG layer of <i>Ca</i>. T. oneisti has an unusually high peptide cross-linkage of 67% but relatively short glycan chains with an average length of 12 disaccharides. Curiously, it has only two predicted endopeptidases, MepA and PBP4. Cellular localization of symbiont PBP4 by fluorescently labeled antibodies reveals its polar localization and its accumulation at the constriction sites, suggesting that PBP4 is involved in PG biosynthesis during septum formation. Isolated symbiont PBP4 protein shows a different selectivity for β-lactams compared to its homologue from <i>E. coli</i>. Bocillin-FL binding by PBP4 is activated by some β-lactams, suggesting the presence of an allosteric binding site. Overall, our data point to a role of PBP4 in PG cleavage during the longitudinal cell division and to a PG that might have been adapted to the symbiotic lifestyle.https://www.mdpi.com/2079-6382/10/3/274cell divisionpenicillin binding proteinspeptidoglycanprotein localizationsymbiosis |
| spellingShingle | Jinglan Wang Laura Alvarez Silvia Bulgheresi Felipe Cava Tanneke den Blaauwen PBP4 Is Likely Involved in Cell Division of the Longitudinally Dividing Bacterium <i>Candidatus</i> Thiosymbion Oneisti Antibiotics cell division penicillin binding proteins peptidoglycan protein localization symbiosis |
| title | PBP4 Is Likely Involved in Cell Division of the Longitudinally Dividing Bacterium <i>Candidatus</i> Thiosymbion Oneisti |
| title_full | PBP4 Is Likely Involved in Cell Division of the Longitudinally Dividing Bacterium <i>Candidatus</i> Thiosymbion Oneisti |
| title_fullStr | PBP4 Is Likely Involved in Cell Division of the Longitudinally Dividing Bacterium <i>Candidatus</i> Thiosymbion Oneisti |
| title_full_unstemmed | PBP4 Is Likely Involved in Cell Division of the Longitudinally Dividing Bacterium <i>Candidatus</i> Thiosymbion Oneisti |
| title_short | PBP4 Is Likely Involved in Cell Division of the Longitudinally Dividing Bacterium <i>Candidatus</i> Thiosymbion Oneisti |
| title_sort | pbp4 is likely involved in cell division of the longitudinally dividing bacterium i candidatus i thiosymbion oneisti |
| topic | cell division penicillin binding proteins peptidoglycan protein localization symbiosis |
| url | https://www.mdpi.com/2079-6382/10/3/274 |
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