{"entity": "publication", "iuid": "e7aa8bb8c70b4b3ba992a62c9da38faa", "timestamp": "2026-07-18T17:40:22.267Z", "links": {"self": {"href": "https://publications.scilifelab.se/publication/e7aa8bb8c70b4b3ba992a62c9da38faa.json"}, "display": {"href": "https://publications.scilifelab.se/publication/e7aa8bb8c70b4b3ba992a62c9da38faa"}}, "title": "The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation.", "authors": [{"family": "Schulte", "given": "Tim", "initials": "T"}, {"family": "Mikaelsson", "given": "Cecilia", "initials": "C"}, {"family": "Beaussart", "given": "Audrey", "initials": "A"}, {"family": "Kikhney", "given": "Alexey", "initials": "A"}, {"family": "Deshmukh", "given": "Maya", "initials": "M"}, {"family": "Wolniak", "given": "Sebastian", "initials": "S"}, {"family": "Pathak", "given": "Anuj", "initials": "A"}, {"family": "Ebel", "given": "Christine", "initials": "C"}, {"family": "L\u00f6fling", "given": "Jonas", "initials": "J"}, {"family": "Fogolari", "given": "Federico", "initials": "F"}, {"family": "Henriques-Normark", "given": "Birgitta", "initials": "B"}, {"family": "Dufr\u00eane", "given": "Yves F", "initials": "YF"}, {"family": "Svergun", "given": "Dmitri", "initials": "D"}, {"family": "Nygren", "given": "Per-\u00c5ke", "initials": "P\u00c5"}, {"family": "Achour", "given": "Adnane", "initials": "A"}], "type": "journal article", "published": "2016-09-01", "journal": {"volume": "6", "issn": "2045-2322", "issue": null, "pages": "32371", "title": "Sci Rep", "issn-l": "2045-2322"}, "abstract": "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 \u03b2-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.", "doi": "10.1038/srep32371", "pmid": "27582320", "labels": {"Protein Science Facility (PSF)": "Service"}, "xrefs": [{"db": "pii", "key": "srep32371"}, {"db": "pmc", "key": "PMC5007671"}], "notes": [], "created": "2017-05-03T13:02:42.402Z", "modified": "2017-09-06T11:42:09.440Z"}