{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T17:23:44Z","timestamp":1793381024701,"version":"4.5.0"},"reference-count":49,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2006,6,27]],"date-time":"2006-06-27T00:00:00Z","timestamp":1151366400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2006,8]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>NhhA, <jats:styled-content><jats:italic>N<\/jats:italic><\/jats:styled-content><jats:italic>eisseria<\/jats:italic><jats:styled-content>h<\/jats:styled-content>ia\/hsf <jats:styled-content>h<\/jats:styled-content>omologue, or GNA0992, is an oligomeric outer membrane protein of <jats:italic>Neisseria meningitidis,<\/jats:italic> recently included in the family of trimeric autotransporter adhesins. In this study we present the structural and functional characterization of this protein. By expressing in <jats:italic>Escherichia coli<\/jats:italic> the full\u2010length gene, deletion mutants and chimeric proteins of NhhA, we demonstrated that the last 72 C\u2010terminal residues are able to allow trimerization and localization of the N\u2010terminal protein domain to the bacterial surface. In addition, we investigated on the possible role of NhhA in bacterial\u2013host interaction events. We assessed <jats:italic>in vitro<\/jats:italic> the ability of recombinant purified NhhA to bind human epithelial cells as well as laminin and heparan sulphate. Furthermore, we shown that <jats:italic>E.\u2003coli<\/jats:italic> strain expressing NhhA was able to adhere to epithelial cells, and observed a reduced adherence in a meningococcal isogenic MC58\u0394NhhA mutant. We concluded that this protein is a multifunctional adhesin, able to promote the bacterial adhesion to host cells and extracellular matrix components. Collectively, our results underline a putative role of NhhA in meningococcal pathogenesis and ascertain its structural and functional belonging to the emerging group of bacterial autotransporter adhesins with trimeric architecture.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2006.05261.x","type":"journal-article","created":{"date-parts":[[2006,6,27]],"date-time":"2006-06-27T14:28:48Z","timestamp":1151418528000},"page":"631-644","source":"Crossref","is-referenced-by-count":98,"title":["<i>Neisseria meningitidis<\/i> NhhA is a multifunctional trimeric autotransporter 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