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Title

In vitro biofilm development of Streptococcus pneumoniae and formation of choline-binding protein–DNA complexes

AuthorsDomenech, Mirian ; Ruiz, Susana; Moscoso, Miriam ; García, Ernesto
KeywordsPseudomonas-aeruginosa biofilms
Extracellular dna
Nasopharyngeal colonization
Phosphorylcholine esterase
Transition-metals
Crystal-structure
Epithelial-cells
Normal growth
Factor-h
Matrix
Issue DateOct-2015
PublisherJohn Wiley & Sons
CitationEnviron Microbiol Rep 7(5) 715-27 (2015)
AbstractExtracellular deoxyribonucleic acid (eDNA) is an essential component of bacterial biofilm matrices, and is required in their formation and maintenance. Extracellular DNA binds to exopolysaccharides or extracellular proteins, affording biofilms greater structural integrity. Recently, we reported evidence of intercellular eDNA-LytC complexes in pneumococcal biofilms. The LytC lysozyme is a member of the choline-binding family of proteins (CBPs) located on the pneumococcal surface. The present work shows that other CBPs, i.e. LytA, LytB, Pce, PspC and CbpF, which have a pI between 5 and 6, can bind DNA in vitro. This process requires the presence of divalent cations other than Mg(2+). This DNA binding capacity of CBPs appears to be independent of their enzymatic activity and, at least in the case of LytA, does not require the choline-binding domain characteristic of CBPs. Positively charged, surface-exposed, 25 amino acid-long peptides derived from the catalytic domain of LytB, were also found capable of DNA binding through electrostatic interactions. Confocal laser scanning microcopy revealed the existence of cell-associated LytB-eDNA complexes in Streptococcus pneumoniae biofilms. These and other findings suggest that these surface-located proteins of S. pneumoniae could play roles of varying importance in the colonization and/or invasion of human host where different environmental conditions exist.
Description13 p.-6 fig.
Publisher version (URL)https://doi.org/10.1111/1758-2229.12295
URIhttp://hdl.handle.net/10261/214725
DOI10.1111/1758-2229.12295
E-ISSN1758-2229
Appears in Collections:(CIB) Artículos
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