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Infection and Immunity, February 1999, p. 834-843, Vol. 67, No. 2
Abteilung Infektionsbiologie,
Received 17 August 1998/Returned for modification 5 October
1998/Accepted 4 November 1998
Unlike other type 4 pili, the neisserial pili consist of at least
two distinct proteins, the highly variable major subunit PilE forming
the pilus fiber and the tip-associated adhesin PilC. PilC protein
purified either from gonococci or from Escherichia coli
interacted with different human epithelial cell lines, primary epithelial and endothelial cells. The binding of PilC protein efficiently prevented the attachment of piliated Neisseria
gonorrhoeae and Neisseria meningitidis to these cell
types. Fluorescent beads coated with pili prepared from piliated
wild-type N. gonorrhoeae also adhered to these cells, in
contrast to beads coated with pili prepared from a piliated
PilC-deficient mutant. In the latter case, the binding of fluorescent
beads was restored after pretreatment of the pilus-loaded beads with
purified PilC. Piliated wild-type N. gonorrhoeae, the
piliated PilC-deficient mutant, and N. gonorrhoeae pili
assembled in Pseudomonas aeruginosa agglutinated human
erythrocytes, while nonpiliated gonococci did not. Consistently,
purified PilC did not agglutinate or bind to human erythrocytes,
suggesting that N. gonorrhoeae PilE is responsible for
pilus-mediated hemagglutination.
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Roles of PilC and PilE Proteins in Pilus-Mediated
Adherence of Neisseria gonorrhoeae and Neisseria
meningitidis to Human Erythrocytes and Endothelial and
Epithelial Cells

*
Corresponding author. Mailing address:
Max-Planck-Institut für Biologie, Abteilung Infektionsbiologie,
Spemannstr. 34, 72076 Tübingen, Germany. Phone: 49 7071 601 222. Fax: 49 7071 61 03 79. E-mail:
sinfbio{at}mpib-tuebingen.mpg.de.
Present address: Institut für Zellbiologie, Technologiehof,
48149 Münster, Germany.
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