Journal of Experimental Medicine, Vol 161, 1539-1553, Copyright © 1985 by Rockefeller University Press

ARTICLES

Pili of Neisseria meningitidis. Analysis of structure and investigation of structural and antigenic relationships to gonococcal pili

DS Stephens, AM Whitney, J Rothbard and GK Schoolnik

To provide information useful for the design of a pilus vaccine effective for the prevention of both meningococcal and gonococcal disease, the electron microscopic morphology of meningococcal pili and the structural and antigenic relationships of meningococcal pili to gonococcal pili were investigated. Meningococcal pili were 4-6 nm in width, extended 500-6,000 nm from the organism surface, and occurred singly or in bundles composed of 8-10 pili per bundle. Meningococcal pilin varied between 17,250 and 20,600 daltons. Pilin was present in outer membrane preparations of some meningococcal isolates that were nonpiliated by electron microscopic examination. Antibodies to gonococcal pili, cyanogen bromide cleavage fragments of gonococcal pilin, or synthetic peptide analogues corresponding to regions of the gonococcal pilin sequence, were used to detect common meningococcal and gonococcal antigenic determinants that might indicate the existence of a conserved sequence beyond residue 29. Antibody to intact gonococcal pili or to the variable CNBR-3 region of gonococcal pilin detected little shared antigenicity with meningococcal pilin. However, pilin from all tested meningococcal isolates reacted with antibody to the CNBR-2 fragment of gonococcal pilin, a region highly conserved among gonococcal strains. Meningococcal pilins were also broadly crossreactive with antibody to a synthetic peptide corresponding to residues 69-84 of the gonococcal sequence, a part of the CNBR-2 region that appears to be critical for gonococcal receptor-binding function. If a sequence similar to 69-84 is also important for receptor-binding function in meningococcal pili, a peptide corresponding to this region may elicit antibodies that block the adherence function of pili elaborated by both Neisseria gonorrhoeae and N. meningitidis.
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This article has been cited by other articles:

• Kahler, C. M., Martin, L. E., Tzeng, Y.-L., Miller, Y. K., Sharkey, K., Stephens, D. S., Davies, J. K. (2001). Polymorphisms in Pilin Glycosylation Locus of Neisseria meningitidis Expressing Class II Pili. Infect. Immun. 69: 3597-3604 [Abstract] [Full Text]  
• van Deuren, M., Brandtzaeg, P., van der Meer, J. W. M. (2000). Update on Meningococcal Disease with Emphasis on Pathogenesis and Clinical Management. Clin. Microbiol. Rev. 13: 144-166 [Abstract] [Full Text]  

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