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J Med Microbiol 53 (2004), 821-832; DOI: 10.1099/jmm.0.45529-0
© 2004 Society for General Microbiology
ISSN 0022-2615

Neisseria meningitidis: an overview of the carriage state

Siamak P. Yazdankhah1 and Dominique A. Caugant1,2

1Department of Airborne Infections, Division of Infectious Disease Control, Norwegian Institute of Public Health, PO Box 4404 Nydalen, NO-0403 Oslo, Norway 2Department of Oral Biology, University of Oslo, Oslo, Norway

Correspondence Siamak P. Yazdankhah siamak.yazdankhah{at}fhi.no


During periods of endemic disease, about 10 % of the general population harbour Neisseria meningitidis in the nasopharynx. Since N. meningitidis is a strict human pathogen and most patients have not been in contact with other cases, asymptomatic carriers are presumably the major source of the pathogenic strains. Most carrier isolates are shown to lack capsule production. The capsule deficient state of meningococcal strains in the nasopharynx may aid evasion of the human immune defence and hence be selected to survive nasopharyngeal colonization. Carriage itself can be an immunizing process resulting in systemic protective antibody responses. Frequent nasopharyngeal colonization with related bacteria like Neisseria lactamica improves natural immunity to meningococci by the formation of cross-reacting antibodies. While most meningococcal strains recovered from patients belong to a limited number of clonal groups worldwide, strains isolated from carriers comprise numerous genotypes, with only a small proportion of the strains representing invasive clones. During the carriage state, co-colonization with other pathogenic and non-pathogenic bacteria may lead to genetic exchange, which may result in the emergence of new meningococcal clones. The high diversity of meningococcal carrier strains, compared with hypervirulent strains, supports the idea that transmissibility, not invasion, is essential in the life cycle of N. meningitidis.


Abbreviations: LOS, lipooligosaccharides; LPS, lipopolysaccharides; OMP, outer-membrane protein.




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