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-Structure paper
タイトル | The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation. |
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ジャーナル・号・ページ | Sci Rep, Vol. 6, Page 32371, Year 2016 |
掲載日 | 2016年9月1日 |
著者 | Tim 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 要旨 | 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 ...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. |
リンク | Sci Rep / PubMed:27582320 / PubMed Central |
手法 | SAS (X-ray synchrotron) / X線回折 |
解像度 | 2.1 Å |
構造データ | SASDAC6: SASDAE6: PDB-5jui: |
化合物 | ChemComp-NA: ChemComp-GOL: ChemComp-HOH: |
由来 |
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キーワード | STRUCTURAL PROTEIN / Streptococcus pneumoniae / Pneumococcal Serine Rich Repeat Protein / Oligomerisation / Bacterial aggregation / Biofilm formation / DNA |