{"entity": "researcher", "timestamp": "2026-07-11T05:11:28.725Z", "family": "Ubhayasekera", "given": "Wimal", "initials": "W", "orcid": "0000-0001-5223-2434", "affiliations": ["Department of Cell and Molecular Biology, Uppsala University, Biomedical Center, Uppsala, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/a01d8f6c38d3494a972b80f588f51f51.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/a01d8f6c38d3494a972b80f588f51f51"}}, "publications": [{"entity": "publication", "iuid": "bfb15759c8644cef8d58bca5a0c0e8c7", "links": {"self": {"href": "https://publications.scilifelab.se/publication/bfb15759c8644cef8d58bca5a0c0e8c7.json"}, "display": {"href": "https://publications.scilifelab.se/publication/bfb15759c8644cef8d58bca5a0c0e8c7"}}, "title": "MrpH, a new class of metal-binding adhesin, requires zinc to mediate biofilm formation.", "authors": [{"family": "Jiang", "given": "Wangshu", "initials": "W", "orcid": "0000-0003-1570-1208", "researcher": {"href": "https://publications.scilifelab.se/researcher/9908e45f950149e2963961d88783dabb.json"}}, {"family": "Ubhayasekera", "given": "Wimal", "initials": "W", "orcid": "0000-0001-5223-2434", "researcher": {"href": "https://publications.scilifelab.se/researcher/a01d8f6c38d3494a972b80f588f51f51.json"}}, {"family": "Breed", "given": "Michael C", "initials": "MC"}, {"family": "Norsworthy", "given": "Allison N", "initials": "AN"}, {"family": "Serr", "given": "Nina", "initials": "N", "orcid": "0000-0003-1335-0790", "researcher": {"href": "https://publications.scilifelab.se/researcher/5468ea52baea4e33a0c64ce395093c2d.json"}}, {"family": "Mobley", "given": "Harry L T", "initials": "HLT", "orcid": "0000-0001-9195-7665", "researcher": {"href": "https://publications.scilifelab.se/researcher/4db7193117fd4f5aaa3e2685372f01e2.json"}}, {"family": "Pearson", "given": "Melanie M", "initials": "MM", "orcid": "0000-0003-4553-3276", "researcher": {"href": "https://publications.scilifelab.se/researcher/2c675562ba474fdb81810f9fec308fe6.json"}}, {"family": "Knight", "given": "Stefan D", "initials": "SD", "orcid": "0000-0002-7180-8758", "researcher": {"href": "https://publications.scilifelab.se/researcher/9e9971d1ebb542a8b54601675c3869f5.json"}}], "type": "journal article", "published": "2020-08-00", "journal": {"title": "PLoS Pathog.", "issn": "1553-7374", "volume": "16", "issue": "8", "pages": "e1008707", "issn-l": "1553-7366"}, "abstract": "Proteus mirabilis, a Gram-negative uropathogen, is a major causative agent in catheter-associated urinary tract infections (CAUTI). Mannose-resistant Proteus-like fimbriae (MR/P) are crucially important for P. mirabilis infectivity and are required for biofilm formation and auto-aggregation, as well as for bladder and kidney colonization. Here, the X-ray crystal structure of the MR/P tip adhesin, MrpH, is reported. The structure has a fold not previously described and contains a transition metal center with Zn2+ coordinated by three conserved histidine residues and a ligand. Using biofilm assays, chelation, metal complementation, and site-directed mutagenesis of the three histidines, we show that an intact metal binding site occupied by zinc is essential for MR/P fimbria-mediated biofilm formation, and furthermore, that P. mirabilis biofilm formation is reversible in a zinc-dependent manner. Zinc is also required for MR/P-dependent agglutination of erythrocytes, and mutation of the metal binding site renders P. mirabilis unfit in a mouse model of UTI. The studies presented here provide important clues as to the mechanism of MR/P-mediated biofilm formation and serve as a starting point for identifying the physiological MR/P fimbrial receptor.", "doi": "10.1371/journal.ppat.1008707", "pmid": "32780778", "labels": {"Protein Science Facility (PSF)": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC7444556"}, {"db": "pii", "key": "PPATHOGENS-D-20-00342"}], "notes": [], "created": "2024-04-03T13:40:54.913Z", "modified": "2024-04-03T13:40:56.097Z"}]}