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Identification of the chain-dispersing peptidoglycan hydrolase LytB of Streptococcus gordonii.


ABSTRACT: 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.

SUBMITTER: Arrigucci R 

PROVIDER: S-EPMC5393624 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

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Identification of the chain-dispersing peptidoglycan hydrolase LytB of Streptococcus gordonii.

Arrigucci Riccardo R   Pozzi Gianni G  

PloS one 20170417 4


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 Mic  ...[more]

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