{"entity": "researcher", "timestamp": "2026-07-14T04:34:40.523Z", "family": "Knight", "given": "Stefan David", "initials": "SD", "orcid": "0000-0002-7180-8758", "affiliations": ["Department of Cell and Molecular Biology, Biomedical Centre, Uppsala University, Uppsala, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/9e9971d1ebb542a8b54601675c3869f5.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/9e9971d1ebb542a8b54601675c3869f5"}}, "publications": [{"entity": "publication", "iuid": "f8ebe7efa7b642fe889dab9c051a3e5e", "links": {"self": {"href": "https://publications.scilifelab.se/publication/f8ebe7efa7b642fe889dab9c051a3e5e.json"}, "display": {"href": "https://publications.scilifelab.se/publication/f8ebe7efa7b642fe889dab9c051a3e5e"}}, "title": "Antiparallel stacking of Csu pili drives Acinetobacter baumannii 3D biofilm assembly", "authors": [{"family": "Malmi", "given": "Henri", "initials": "H", "orcid": "0000-0001-9872-8523", "researcher": {"href": "https://publications.scilifelab.se/researcher/0a082b1f8b334faca225e6000daabcf9.json"}}, {"family": "Pakharukova", "given": "Natalia", "initials": "N", "orcid": "0000-0002-8363-6105", "researcher": {"href": "https://publications.scilifelab.se/researcher/555b7be2f9ba46a9b78549d89e69b41b.json"}}, {"family": "Paul", "given": "Bindusmita", "initials": "B", "orcid": "0000-0001-9844-9751", "researcher": {"href": "https://publications.scilifelab.se/researcher/1667be16b3c947a2a35eb58ee357868a.json"}}, {"family": "Tuittila", "given": "Minna", "initials": "M"}, {"family": "Ahmad", "given": "Irfan", "initials": "I"}, {"family": "Knight", "given": "Stefan David", "initials": "SD", "orcid": "0000-0002-7180-8758", "researcher": {"href": "https://publications.scilifelab.se/researcher/9e9971d1ebb542a8b54601675c3869f5.json"}}, {"family": "Uhlin", "given": "Bernt Eric", "initials": "BE", "orcid": "0000-0002-2991-8072", "researcher": {"href": "https://publications.scilifelab.se/researcher/9faa19d33fd84728bb6df987ba16475f.json"}}, {"family": "Ghosal", "given": "Debnath", "initials": "D", "orcid": "0000-0002-2227-0330", "researcher": {"href": "https://publications.scilifelab.se/researcher/d50f9497285b4b709f1011366d074f2a.json"}}, {"family": "Zavialov", "given": "Anton V", "initials": "AV", "orcid": "0000-0001-6191-5931", "researcher": {"href": "https://publications.scilifelab.se/researcher/79863c4e5ca94dffa0103c111a5da35c.json"}}], "type": "journal-article", "published": "2026-02-07", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "17", "issue": "1", "issn-l": "2041-1723"}, "abstract": null, "doi": "10.1038/s41467-026-68860-z", "pmid": null, "labels": {"Integrated Microscopy Technologies Ume\u00e5": "Service", "Cryo-EM": "Service"}, "xrefs": [], "notes": [], "created": "2026-06-24T09:43:26.636Z", "modified": "2026-06-24T09:43:26.992Z"}, {"entity": "publication", "iuid": "84be06817c144739a3b32c8d33eb25f2", "links": {"self": {"href": "https://publications.scilifelab.se/publication/84be06817c144739a3b32c8d33eb25f2.json"}, "display": {"href": "https://publications.scilifelab.se/publication/84be06817c144739a3b32c8d33eb25f2"}}, "title": "Archaic chaperone-usher pili self-secrete into superelastic zigzag springs.", "authors": [{"family": "Pakharukova", "given": "Natalia", "initials": "N", "orcid": "0000-0002-8363-6105", "researcher": {"href": "https://publications.scilifelab.se/researcher/555b7be2f9ba46a9b78549d89e69b41b.json"}}, {"family": "Malmi", "given": "Henri", "initials": "H", "orcid": "0000-0001-9872-8523", "researcher": {"href": "https://publications.scilifelab.se/researcher/0a082b1f8b334faca225e6000daabcf9.json"}}, {"family": "Tuittila", "given": "Minna", "initials": "M"}, {"family": "Dahlberg", "given": "Tobias", "initials": "T"}, {"family": "Ghosal", "given": "Debnath", "initials": "D"}, {"family": "Chang", "given": "Yi-Wei", "initials": "YW", "orcid": "0000-0003-2391-473X", "researcher": {"href": "https://publications.scilifelab.se/researcher/53c3646339b4487aa76fa4fb6503e14c.json"}}, {"family": "Myint", "given": "Si Lhyam", "initials": "SL"}, {"family": "Paavilainen", "given": "Sari", "initials": "S"}, {"family": "Knight", "given": "Stefan David", "initials": "SD", "orcid": "0000-0002-7180-8758", "researcher": {"href": "https://publications.scilifelab.se/researcher/9e9971d1ebb542a8b54601675c3869f5.json"}}, {"family": "Lamminm\u00e4ki", "given": "Urpo", "initials": "U"}, {"family": "Uhlin", "given": "Bernt Eric", "initials": "BE", "orcid": "0000-0002-2991-8072", "researcher": {"href": "https://publications.scilifelab.se/researcher/9faa19d33fd84728bb6df987ba16475f.json"}}, {"family": "Andersson", "given": "Magnus", "initials": "M", "orcid": "0000-0002-9835-3263", "researcher": {"href": "https://publications.scilifelab.se/researcher/fe860af5d944447086cbf2d00e3beb3e.json"}}, {"family": "Jensen", "given": "Grant", "initials": "G", "orcid": "0000-0003-1556-4864", "researcher": {"href": "https://publications.scilifelab.se/researcher/4fdad82f6f3e41e8ad427f8d2b5b0d0b.json"}}, {"family": "Zavialov", "given": "Anton V", "initials": "AV", "orcid": "0000-0001-6191-5931", "researcher": {"href": "https://publications.scilifelab.se/researcher/79863c4e5ca94dffa0103c111a5da35c.json"}}], "type": "journal article", "published": "2022-09-00", "journal": {"title": "Nature", "issn": "1476-4687", "volume": "609", "issue": "7926", "pages": "335-340", "issn-l": "0028-0836"}, "abstract": "Adhesive pili assembled through the chaperone-usher pathway are hair-like appendages that mediate host tissue colonization and biofilm formation of Gram-negative bacteria1-3. Archaic chaperone-usher pathway pili, the most diverse and widespread chaperone-usher pathway adhesins, are promising vaccine and drug targets owing to their prevalence in the most troublesome multidrug-resistant pathogens1,4,5. However, their architecture and assembly-secretion process remain unknown. Here, we present the cryo-electron microscopy structure of the prototypical archaic Csu pilus that mediates biofilm formation of Acinetobacter baumannii-a notorious multidrug-resistant nosocomial pathogen. In contrast to the thick helical tubes of the classical type 1 and P pili, archaic pili assemble into an ultrathin zigzag architecture secured by an elegant clinch mechanism. The molecular clinch provides the pilus with high mechanical stability as well as superelasticity, a property observed for the first time, to our knowledge, in biomolecules, while enabling a more economical and faster pilus production. Furthermore, we demonstrate that clinch formation at the cell surface drives pilus secretion through the outer membrane. These findings suggest that clinch-formation inhibitors might represent a new strategy to fight multidrug-resistant bacterial infections.", "doi": "10.1038/s41586-022-05095-0", "pmid": "35853476", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC9452303"}, {"db": "pii", "key": "10.1038/s41586-022-05095-0"}], "notes": [], "created": "2023-11-26T14:07:20.315Z", "modified": "2023-11-26T14:07:20.536Z"}, {"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"}, {"entity": "publication", "iuid": "1ce032b1771744128a78cdd029bd2371", "links": {"self": {"href": "https://publications.scilifelab.se/publication/1ce032b1771744128a78cdd029bd2371.json"}, "display": {"href": "https://publications.scilifelab.se/publication/1ce032b1771744128a78cdd029bd2371"}}, "title": "Structures of two fimbrial adhesins, AtfE and UcaD, from the uropathogen Proteus mirabilis.", "authors": [{"family": "Jiang", "given": "Wangshu", "initials": "W"}, {"family": "Ubhayasekera", "given": "Wimal", "initials": "W"}, {"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": "2018-11-01", "journal": {"title": "Acta Crystallogr D Struct Biol", "issn": "2059-7983", "volume": "74", "issue": "Pt 11", "pages": "1053-1062", "issn-l": "2059-7983"}, "abstract": "The important uropathogen Proteus mirabilis encodes a record number of chaperone/usher-pathway adhesive fimbriae. Such fimbriae, which are used for adhesion to cell surfaces/tissues and for biofilm formation, are typically important virulence factors in bacterial pathogenesis. Here, the structures of the receptor-binding domains of the tip-located two-domain adhesins UcaD (1.5 \u00c5 resolution) and AtfE (1.58 \u00c5 resolution) from two P. mirabilis fimbriae (UCA/NAF and ATF) are presented. The structures of UcaD and AtfE are both similar to the F17G type of tip-located fimbrial receptor-binding domains, and the structures are very similar despite having only limited sequence similarity. These structures represent an important step towards a molecular-level understanding of P. mirabilis fimbrial adhesins and their roles in the complex pathogenesis of urinary-tract infections.", "doi": "10.1107/S2059798318012391", "pmid": "30387764", "labels": {"Protein Science Facility (PSF)": "Service"}, "xrefs": [{"db": "pii", "key": "S2059798318012391"}], "notes": [], "created": "2024-04-03T14:36:45.656Z", "modified": "2024-04-03T14:36:45.672Z"}]}