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Absence of pneumococcal PcsB is associated with overexpression of LysM domain containing proteins.
MedLine Citation:
PMID:  21474534     Owner:  NLM     Status:  Publisher    
The streptococcal Protein required for Cell Separation B (PcsB) is predicted to play an important role in peptidoglycan metabolism based on sequence motifs and altered phenotypes of gene deletion mutant cells exhibiting defects in cell separation. However, no enzymatic activity has been demonstrated for PcsB so far. By generating gene deletion mutant strains in four different genetic backgrounds we could demonstrate that pcsB is not essential for cell survival in Streptococcus pneumoniae, but for proper cell division. Deletion mutant cells displayed cluster formation due to aberrant cell division, reduced growth and antibiotic sensitivity that were fully reverted by transformation with a plasmid carrying pcsB. Immunofluorescence staining revealed that PcsB was localized to the cell poles similarly to PBP3 and LytB, enzymes with demonstrated peptidoglycan degrading activity required for daughter cell separation. Similarly to other studies with PcsB homologues, we could not detect peptidoglycan lytic activity with recombinant or native pneumococcal PcsB in vitro. In addition to defects in septum placement and separation, absence of PcsB induced increased release of several proteins, such as enolase, MalX and SP0107 LysM domain protein. Interestingly, genes encoding both LysM domain containing proteins that are present in the pneumococcal genome (SP0107 and SP2063) and predicted to be involved in cell wall metabolism, were found to be highly overexpressed (14-33 fold increase) in ΔpcsB cells in two different genetic backgrounds. Otherwise, we detected very little changes in the global gene expression profile of cells lacking PcsB. Thus our data suggest that LysM domain proteins might partially compensate for the lack of PcsB function and allow survival and slow growth of pneumococcus.
Carmen Giefing-Kröll; Kira E Jelencsics; Siegfried Reipert; Eszter Nagy
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-4-7
Journal Detail:
Title:  Microbiology (Reading, England)     Volume:  -     ISSN:  1465-2080     ISO Abbreviation:  -     Publication Date:  2011 Apr 
Date Detail:
Created Date:  2011-4-8     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9430468     Medline TA:  Microbiology     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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