A functional Two-Partner Secretion System contributes to adhesion of Neisseria meningitidis to epithelial cells

University of Wuerzburg, Institute of Hygiene and Microbiology, Josef-Schneider-Str. 2/E1, 97080 Wuerzburg, Germany; Institute of Infections, Immunity and Inflammation, School of Molecular Medical Sciences Centre for Biomolecular Sciences, University Park, University of Nottingham, Nottingham NG7 2RD, UK

^* To whom correspondence should be addressed. Email: okurzai{at}hygiene.uni-wuerzburg.de.

	Abstract

Neisseria meningitidis is a frequent commensal of the human nasopharynx causing severe invasive infections in rare cases. A functional two-partner secretion (TPS) system in N. meningitidis, composed of the secreted effector protein HrpA and its cognate transporter HrpB, is identified and characterized in this study. Although all meningococcal strains harbour at least one TPS system, the hrpA genes display significant C-terminal sequence variation. Meningococcal genes encoding the TPS effector proteins and their transporters are closely associated and transcribed into a single mRNA. HrpA proteins are translocated across the meningococcal outer membrane by their cognate transporters HrpB and mainly released into the environment. During this process, HrpA is proteolytically processed to a mature 180 kDa form. In contrast to other known TPS systems, immature HrpA proteins are stable in the absence of HrpB and accumulate within the bacterial cell. A small percentage of mature HrpA remains associated with the bacteria and contributes to the interaction of meningococci with epithelial cells.