Editor: Mike Koomey
Protein secretion and secreted proteins in pathogenic Neisseriaceae
Article first published online: 9 FEB 2006
FEMS Microbiology Reviews
Volume 30, Issue 2, pages 292–319, March 2006
How to Cite
Van Ulsen, P. and Tommassen, J. (2006), Protein secretion and secreted proteins in pathogenic Neisseriaceae. FEMS Microbiology Reviews, 30: 292–319. doi: 10.1111/j.1574-6976.2006.00013.x
- Issue published online: 9 FEB 2006
- Article first published online: 9 FEB 2006
- Received 7 June 2005; revised 6 September 2005; accepted 20 October 2005.First published online February 2006.
- protein secretion;
- Neisseria meningitidis;
- Neisseria gonorrhoeae;
- repeat-in-toxin (RTX) toxin;
- gene conversion
Secreted proteins of pathogenic bacteria are often essential virulence factors. They are involved, for example, in the adherence of the bacteria to host cells or required to suppress the host's defence mechanisms. Until recently, only IgA1 protease had been studied in detail in the NeisseriaceaeNeisseria meningitidis and Neisseria gonorrhoeae. The availability of their genome sequences, however, has boosted research in this area. Here, we present a survey of the secretome of the pathogenic Neisseriaceae, based on the available genome sequences, and the current knowledge of the functions and structures of the secreted proteins. Of the six protein-secretion pathways that are widely disseminated among Gram-negative bacteria, three pathways appear to be present among the Neisseriaceae, i.e. the autotransporter-, the two-partner- and the type I-secretion mechanisms. Comparison of the predicted secretomes reveals a considerable flexibility. As compared with N. meningitidis and the nonpathogen N. lactamica, N. gonorrhoeae appears to have a considerably degenerated secretome, which may reflect its altered niche occupancy. The flexibility of the secretome may be enhanced by the presence of ORFs in the genomes potentially encoding fragments of secreted proteins. We hypothesize that these ORFs may substitute for the corresponding fragments in the full-length genes through genetic recombination, thereby changing the host-cell receptor specificity of the secreted protein.