{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,2]],"date-time":"2026-08-02T21:52:41Z","timestamp":1785707561365,"version":"3.56.0"},"reference-count":34,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2020,7,7]],"date-time":"2020-07-07T00:00:00Z","timestamp":1594080000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2020,8,25]],"date-time":"2020-08-25T00:00:00Z","timestamp":1598313600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["mBio"],"published-print":{"date-parts":[[2020,8,25]]},"abstract":"<jats:p>\n            Binding of\n            <jats:named-content content-type=\"genus-species\">Staphylococcus pseudintermedius<\/jats:named-content>\n            surface proteins SpsD and SpsL to fibronectin (Fn) plays a critical role in the invasion of canine epithelial cells. Here, we discover that both adhesins have different mechanisms for binding to Fn. The force required to separate SpsD from Fn is extremely strong, consistent with the unusual \u03b2-sheet organization of a high-affinity tandem \u03b2-zipper. By contrast, unbinding of the SpsL-Fn complex involves the sequential rupture of single weak bonds. Our findings may be of biological relevance as SpsD and SpsL are likely to play complementary roles during invasion. While the SpsD \u03b2-zipper supports strong bacterial adhesion and triggers invasion, the weak SpsL interaction would favor fast detachment, enabling the pathogen to colonize new sites.\n          <\/jats:p>","DOI":"10.1128\/mbio.00371-20","type":"journal-article","created":{"date-parts":[[2020,7,6]],"date-time":"2020-07-06T13:43:28Z","timestamp":1594043008000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":5,"title":["The Molecular Complex between Staphylococcal Adhesin SpsD and Fibronectin Sustains Mechanical Forces in the Nanonewton Range"],"prefix":"10.1128","volume":"11","author":[{"given":"Felipe","family":"Viela","sequence":"first","affiliation":[{"name":"Louvain Institute of Biomolecular Science and Technology, UCLouvain, Louvain-la-Neuve, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marion","family":"Matheli\u00e9-Guinlet","sequence":"additional","affiliation":[{"name":"Louvain Institute of Biomolecular Science and Technology, UCLouvain, Louvain-la-Neuve, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giampiero","family":"Pietrocola","sequence":"additional","affiliation":[{"name":"Department of Molecular Medicine, Unit of Biochemistry, University of Pavia, Pavia, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pietro","family":"Speziale","sequence":"additional","affiliation":[{"name":"Department of Molecular Medicine, Unit of Biochemistry, University of Pavia, Pavia, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yves F.","family":"Dufr\u00eane","sequence":"additional","affiliation":[{"name":"Louvain Institute of Biomolecular Science and Technology, UCLouvain, Louvain-la-Neuve, Belgium"},{"name":"Walloon Excellence in Life Sciences and Biotechnology (WELBIO), Wavre, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","volume-title":"Muller and Kirk\u2019s small animal dermatology","author":"Miller WH","year":"2012","unstructured":"Miller WH, Jr, Griffin CE, Campbell KL. 2012. 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