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Transcriptional regulation of adhesive properties of Bacillus subtilis to extracellular matrix proteins through the fibronectin‐binding protein YloA
Author(s) -
Rodriguez Ayala Facundo,
Bauman Carlos,
Bartolini Marco,
Saball Ester,
Salvarrey Marcela,
Leñini Cecilia,
Cogliati Sebastián,
Strauch Mark,
Grau Roberto
Publication year - 2017
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13666
Subject(s) - biology , bacillus subtilis , fibronectin , extracellular matrix , microbiology and biotechnology , extracellular , dna binding protein , matrix (chemical analysis) , biochemistry , bacteria , genetics , transcription factor , gene , materials science , composite material
Summary Bacterial adherence to extracellular matrix proteins (ECMp) plays important roles during host–pathogen interaction, however its genetic regulation remains poorly understood. yloA of the model bacterium Bacillus subtilis shows high homology to genes encoding fibronectin‐binding proteins of Gram‐positive pathogens. Here, we characterized the regulatory network of YloA‐dependent adhesive properties of the probiotic B. subtilis natto ( Bs n). YloA‐proficient, but not YloA‐deficient, Bs n specifically bound to ECMp in a concentration‐dependent manner and were proficient in biofilm formation. yloA expression showed a continuous increase in activity during the growth phase and decreased during the stationary phase. The transcription factors AbrB and DegU downregulated yloA expression during the logarithmic and stationary growth phases respectively. Analysis of the yloA promoter region revealed the presence of AT‐rich direct and inverted repeats previously reported to function as DegU‐recognized binding sites. In spo0A cells, yloA expression was completely turned off because of upregulation of AbrB throughout growth. Accordingly, DNase I footprinting analysis confirmed that AbrB bound to the promoter region of yloA . Interestingly, Bs n bound fibronectin with higher affinity, lower Kd , than several bacterial pathogens and competitively excluded them from binding to immobilized‐fibronectin, a finding that might be important for the anti‐infective properties of B. subtilis and its relatives.