{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T19:40:28Z","timestamp":1789501228557,"version":"build-2803163510"},"reference-count":83,"publisher":"Wiley","issue":"21","license":[{"start":{"date-parts":[[2025,7,3]],"date-time":"2025-07-03T00:00:00Z","timestamp":1751500800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001407","name":"Department of Biotechnology, Ministry of Science and Technology, India","doi-asserted-by":"publisher","award":["BT\/PR44816\/MED\/29\/1598\/2022"],"award-info":[{"award-number":["BT\/PR44816\/MED\/29\/1598\/2022"]}],"id":[{"id":"10.13039\/501100001407","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2025,11]]},"abstract":"<jats:p>\n                    <jats:italic>Enterococcus faecalis<\/jats:italic>\n                    is an opportunistic pathogen that causes various clinically significant infections, including infective endocarditis and catheter\u2010associated urinary tract infections.\n                    <jats:italic>E.\u2009faecalis<\/jats:italic>\n                    assembles hair\u2010like appendages termed endocarditis and biofilm\u2010associated pili (Ebp), crucial for adherence, colonization, biofilm formation, and virulence. The Ebp pilus comprises three pilin subunits (EbpA, EbpB, and EbpC) encoded by the\n                    <jats:italic>ebpABC<\/jats:italic>\n                    pilus operon. EbpC forms the Ebp pilus backbone decorated with EbpA and EbpB at the tip and base for adhesion and anchoring, respectively. Experimental structures are not yet available for any of the Ebp pilins. Herein, we report the crystal structures of EbpC, EbpB, and their homologs from\n                    <jats:italic>E.\u2009faecium<\/jats:italic>\n                    . The structures of EbpC and EbpB reveal four and three linearly arranged immunoglobulin\u2010like domains, respectively. The basal pilin EbpB structure fully mimics the features of backbone pilins with a typical pilin motif and CnaB\u2013CnaA\u2013CnaB fold, each with an intact isopeptide bond. The rigid C\u2010terminal fragment of the backbone pilin EbpC, containing three domains, exhibits a CnaB\u2013CnaA\u2013CnaB fold, each with an intradomain isopeptide bond. The flexible N\u2010terminal domain with the CnaB fold in EbpC lacks an isopeptide bond but appears to form in a full\u2010length structure that shows a \u2018beads on a string\u2019 architecture, previously unobserved for four\u2010domain backbone pilins. Structural analysis helped us to identify residues of internal isopeptide bonds and pilin motifs harboring lysine residues responsible for intermolecular covalent links during sortase\u2010mediated pilus assembly and propose a structural model for the Ebp pilus. This knowledge may be useful for developing structure\u2010based approaches targeting pilins and pili in enterococcal infections.\n                  <\/jats:p>","DOI":"10.1111\/febs.70173","type":"journal-article","created":{"date-parts":[[2025,7,3]],"date-time":"2025-07-03T12:53:53Z","timestamp":1751547233000},"page":"5723-5749","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Structural basis of Ebp pilus shaft formation and anchoring in vancomycin\u2010resistant\n                    <i>Enterococci<\/i>"],"prefix":"10.1111","volume":"292","author":[{"given":"Vinay","family":"Sharma","sequence":"first","affiliation":[{"name":"Laboratory of Structural Microbiology, Regional Centre for Biotechnology NCR Biotech Science Cluster  Faridabad 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