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Infection and Immunity, June 2001, p. 3597-3604, Vol. 69, No. 6
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.6.3597-3604.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Polymorphisms in Pilin Glycosylation Locus of Neisseria meningitidis Expressing Class II Pili

Charlene M. Kahler,1,* Larry E. Martin,2,3 Yih-Ling Tzeng,2,3 Yoon K. Miller,2,3 Kerith Sharkey,1 David S. Stephens,2,3 and John K. Davies1

Department of Microbiology, Monash University, Clayton, Australia,1 and Departments of Medicine and Microbiology and Immunology, Emory University School of Medicine,2 and Research Service, Veterans Administration Medical Center,3 Atlanta, Georgia

Received 28 November 2000/Returned for modification 28 December 2000/Accepted 27 February 2001

We have located a locus, pgl, in Neisseria meningitidis strain NMB required for the glycosylation of class II pili. Between five and eight open reading frames (ORFs) (pglF, pglB, pglC, pglB2, orf2, orf3, orf8, and avtA) were present in the pgl clusters of different meningococcal isolates. The Class I pilus-expressing strains Neisseria gonorrhoeae MS11 and N. meningitidis MC58 each contain a pgl cluster in which orf2 and orf3 have been deleted. Strain NMB and other meningococcal isolates which express class II type IV pili contained pgl clusters in which pglB had been replaced by pglB2 and an additional novel ORF, orf8, had been inserted between pglB2 and pglC. Insertional inactivation of the eight ORFs of the pgl cluster of strain NMB showed that pglF, pglB2, pglC, and pglD, but not orf2, orf3, orf8, and avtA, were necessary for pilin glycosylation. Pilin glycosylation was not essential for resistance to normal human serum, as pglF and pglD mutants retained wild-type levels of serum resistance. Although pglB2 and pglC mutants were significantly sensitive to normal human serum under the experimental conditions used, subsequent examination of the encapsulation phenotypes revealed that pglB2 and pglC mutants expressed almost 50% less capsule than wild-type NMB. A mutation in orf3, which did not affect pilin glycosylation, also resulted in a 10% reduction in capsule expression and a moderately serum sensitive phenotype. On the basis of these results we suggest that pilin glycosylation may proceed via a lipid-linked oligosaccharide intermediate and that blockages in this pathway may interfere with capsular transport or assembly.

* Corresponding author. Mailing address: Department of Microbiology, Monash University, Wellington Road, Clayton 3800, Australia. Phone: 03 99054842. Fax: 03 99054811. E-mail: charlene.kahler{at}mail1.monash.edu.au.

Infection and Immunity, June 2001, p. 3597-3604, Vol. 69, No. 6
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.6.3597-3604.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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