Premium
Neisseria meningitidis NhhA is a multifunctional trimeric autotransporter adhesin
Author(s) -
Scarselli Maria,
Serruto Davide,
Montanari Paolo,
Capecchi Barbara,
AduBobie Jeannette,
Veggi Daniele,
Rappuoli Rino,
Pizza Mariagrazia,
Aricò Beatrice
Publication year - 2006
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2006.05261.x
Subject(s) - bacterial adhesin , biology , bacterial outer membrane , microbiology and biotechnology , neisseria meningitidis , escherichia coli , neisseria , mutant , pilus , biofilm , recombinant dna , bacteria , gene , biochemistry , genetics
Summary NhhA, N eisseria h ia/hsf h omologue, or GNA0992, is an oligomeric outer membrane protein of Neisseria meningitidis, 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 Escherichia coli the full‐length gene, deletion mutants and chimeric proteins of NhhA, we demonstrated that the last 72 C‐terminal residues are able to allow trimerization and localization of the N‐terminal protein domain to the bacterial surface. In addition, we investigated on the possible role of NhhA in bacterial–host interaction events. We assessed in vitro the ability of recombinant purified NhhA to bind human epithelial cells as well as laminin and heparan sulphate. Furthermore, we shown that E. coli strain expressing NhhA was able to adhere to epithelial cells, and observed a reduced adherence in a meningococcal isogenic MC58ΔNhhA 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.