作者: Maria Scarselli , Davide Serruto , Paolo Montanari , Barbara Capecchi , Jeannette Adu‐Bobie
DOI: 10.1111/J.1365-2958.2006.05261.X
关键词:
摘要: Summary NhhA, Neisseriahia/hsf homologue, or GNA0992, is an oligomeric outer membrane protein of Neisseria meningitidis, recently included in the family trimeric autotransporter adhesins. In this study we present structural and functional characterization protein. By expressing Escherichia coli full-length gene, deletion mutants chimeric proteins NhhA, demonstrated that last 72 C-terminal residues are able to allow trimerization localization N-terminal domain bacterial surface. addition, investigated on possible role NhhA bacterial–host interaction events. We assessed vitro ability recombinant purified bind human epithelial cells as well laminin heparan sulphate. Furthermore, shown E. coli strain was adhere cells, observed a reduced adherence meningococcal isogenic MC58ΔNhhA mutant. concluded multifunctional adhesin, promote adhesion host extracellular matrix components. Collectively, our results underline putative pathogenesis ascertain its belonging emerging group adhesins with architecture.