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Identification of the chain-dispersing peptidoglycan hydrolase LytB of Streptococcus gordonii
Bacterial cell division ends with the separation of the daughter cells, a process that requires peptidoglycan hydrolases (PGHs). Bacteria lacking cell separating PGHs are impaired in cell separation with the formation of long chains or clusters. We identified a gene in Streptococcus gordonii encodin...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5393624/ https://www.ncbi.nlm.nih.gov/pubmed/28414782 http://dx.doi.org/10.1371/journal.pone.0176117 |
Sumario: | Bacterial cell division ends with the separation of the daughter cells, a process that requires peptidoglycan hydrolases (PGHs). Bacteria lacking cell separating PGHs are impaired in cell separation with the formation of long chains or clusters. We identified a gene in Streptococcus gordonii encoding for a putative glucosaminidase (lytB). The lytB isogenic mutant grew in long bacterial chains and resulted in impaired biofilm formation. Purified recombinant LytB showed a murolytic activity on Micrococcus lysodeikticus cell suspension and was able to disperse the long chains of the mutant, restoring the wild type diplococci/short chain phenotype. LytB protein was localized only in culture supernatant cell fraction of S. gordonii, and co-cultures of wild type and lytB mutant showed a significant reduction of bacterial chain length, indicating that LytB is a secreted enzyme. Our results demonstrate that LytB is a secreted peptidoglycan hydrolase required for S. gordonii cell separation. |
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