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Infection and Immunity, May 2002, p. 2264-2270, Vol. 70, No. 5
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.5.2264-2270.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Functional Substitution of the TibC Protein of Enterotoxigenic Escherichia coli Strains for the Autotransporter Adhesin Heptosyltransferase of the AIDA System

Corinna Moormann, Inga Benz, and M. Alexander Schmidt*

Institut für Infektiologie, Zentrum für Molekularbiologie der Entzündung, Westfälische Wilhelms-Universität Münster, D-48149 Münster, Germany

Received 28 August 2001/ Returned for modification 4 December 2001/ Accepted 23 January 2002

The plasmid-encoded AIDA (adhesin involved in diffuse adherence) autotransporter protein derived from diffuse-adhering clinical Escherichia coli isolate 2787 and the TibA (enterotoxigenic invasion locus B) protein encoded by the chromosomal tib locus of enterotoxigenic E. coli (ETEC) strain H10407 are posttranslationally modified by carbohydrate substituents. Analysis of the AIDA-I adhesin showed that the modification involved heptose residues. AIDA-I is modified by the heptosyltransferase activity of the product of the aah gene, which is located directly upstream of adhesin-encoding gene aidA. The carbohydrate modification of the TibA adhesin/invasin is mediated by the TibC protein but has not been elucidated. Based on the sequence similarities between TibC and AAH (autotransporter adhesin heptosyltransferase) and between the TibA and the AIDA proteins we hypothesized that the AIDA system and the Tib system encoded by the tib locus are structurally and functionally related. Here we show that (i) TibC proteins derived from different ETEC strains appear to be highly conserved, (ii) recombinant TibC proteins can substitute for the AAH heptosyltransferase in introducing the heptosyl modification to AIDA-I, (iii) this modification is functional in restoring the adhesive function of AIDA-I, (iv) a single amino acid substitution at position 358 completely abolishes this activity, and (v) antibodies directed at the functionally active AIDA-I recognize a protein resembling modified TibA in ETEC strains. In summary, we conclude that, like AAH, TibC represents an example of a novel class of heptosyltransferases specifically transferring heptose residues onto multiple sites of a protein backbone. A potential consensus sequence for the modification site is suggested.

* Corresponding author. Mailing address: Institute of Infectiology-ZMBE, Von-Esmarch-Str. 56, D-48149 Münster, Germany. Phone: 49 251 835 64 66. Fax: 49 251 835 64 67. E-mail: infekt{at}uni-muenster.de.

Editor: V. J. DiRita

Infection and Immunity, May 2002, p. 2264-2270, Vol. 70, No. 5
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.5.2264-2270.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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