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TitleThe BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation.
Journal, issue, pagesSci Rep, Vol. 6, Page 32371, Year 2016
Publish dateSep 1, 2016
AuthorsTim Schulte / Cecilia Mikaelsson / Audrey Beaussart / Alexey Kikhney / Maya Deshmukh / Sebastian Wolniak / Anuj Pathak / Christine Ebel / Jonas Löfling / Federico Fogolari / Birgitta Henriques-Normark / Yves F Dufrêne / Dmitri Svergun / Per-Åke Nygren / Adnane Achour /
PubMed AbstractThe major human pathogen Streptococcus pneumoniae is a leading cause of disease and death worldwide. Pneumococcal biofilm formation within the nasopharynx leads to long-term colonization and ...The major human pathogen Streptococcus pneumoniae is a leading cause of disease and death worldwide. Pneumococcal biofilm formation within the nasopharynx leads to long-term colonization and persistence within the host. We have previously demonstrated that the capsular surface-associated pneumococcal serine rich repeat protein (PsrP), key factor for biofilm formation, binds to keratin-10 (KRT10) through its microbial surface component recognizing adhesive matrix molecule (MSCRAMM)-related globular binding region domain (BR187-385). Here, we show that BR187-385 also binds to DNA, as demonstrated by electrophoretic mobility shift assays and size exclusion chromatography. Further, heterologous expression of BR187-378 or the longer BR120-378 construct on the surface of a Gram-positive model host bacterium resulted in the formation of cellular aggregates that was significantly enhanced in the presence of DNA. Crystal structure analyses revealed the formation of BR187-385 homo-dimers via an intermolecular β-sheet, resulting in a positively charged concave surface, shaped to accommodate the acidic helical DNA structure. Furthermore, small angle X-ray scattering and circular dichroism studies indicate that the aggregate-enhancing N-terminal region of BR120-166 adopts an extended, non-globular structure. Altogether, our results suggest that PsrP adheres to extracellular DNA in the biofilm matrix and thus promotes pneumococcal biofilm formation.
External linksSci Rep / PubMed:27582320 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution2.1 Å
Structure data

SASDAC6:
PsrP functional binding region (Functional binding region (187-385) of the pneumococcal serine-rich repeat protein, PsrP BR(187-385))
Method: SAXS/SANS

SASDAE6:
PsrP functional binding region (Functional binding region (120-395) of the pneumococcal serine-rich repeat protein, PsrP BR*(120-395))
Method: SAXS/SANS

PDB-5jui:
domain-swapped dimer of the the KRT10-binding region (BR) of PsrP
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • Streptococcus pneumoniae (bacteria)
  • streptococcus pneumoniae serotype 4 (strain atcc baa-334 / tigr4) (bacteria)
KeywordsSTRUCTURAL PROTEIN / Streptococcus pneumoniae / Pneumococcal Serine Rich Repeat Protein / Oligomerisation / Bacterial aggregation / Biofilm formation / DNA

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