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Infection and Immunity, June 2009, p. 2544-2556, Vol. 77, No. 6
0019-9567/09/$08.00+0     doi:10.1128/IAI.01425-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Campylobacter jejuni Glycosylation Island Important in Cell Charge, Legionaminic Acid Biosynthesis, and Colonization of Chickens{triangledown}

Sarah L. Howard,1 Aparna Jagannathan,2 Evelyn C. Soo,3 Joseph P. M. Hui,3 Annie J. Aubry,4 Imran Ahmed,1 Andrey Karlyshev,5 John F. Kelly,4 Michael A. Jones,6 Mark P. Stevens,2 Susan M. Logan,4 and Brendan W. Wren1*

Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, London WC1E 7HT, United Kingdom,1 Institute for Animal Health, Compton, Berkshire RG20 7NN, United Kingdom,2 Institute for Marine Biosciences, National Research Council of Canada, 1411 Oxford Street, Halifax, Nova Scotia B3H 3Z1, Canada,3 Institute for Biological Sciences, National Research Council of Canada, 100 Sussex Drive, Ottawa, Ontario K1A 0R6, Canada,4 School of Life Sciences, Kingston University, Penrhyn Road, Kingston upon Thames KT1 2EE, United Kingdom,5 School of Veterinary Medicine and Science, University of Nottingham, Sutton Bonington LE12 5RD, United Kingdom6

Received 20 November 2008/ Returned for modification 6 January 2009/ Accepted 13 March 2009

Previously, we identified five genes (Cj1321 to Cj1326, of which Cj1325 and Cj1326 are a single gene) in the O-linked flagellin glycosylation island that are highly prevalent in Campylobacter jejuni isolates from chickens. We report mutagenesis, functional, and structural data to confirm that this locus, and Cj1324 in particular, has a significant contributory role in the colonization of chickens by C. jejuni. A motile {Delta}Cj1324 mutant with intact flagella was considerably less hydrophobic and less able to autoagglutinate and form biofilms than the parent strain, 11168H, suggesting that the surface charge of flagella of Cj1324-deficient strains was altered. The physical and functional attributes of the parent were restored upon complementation. Structural analysis of flagellin protein purified from the {Delta}Cj1324 mutant revealed the absence of two legionaminic acid glycan modifications that were present in the parent strain, 11168H. These glycoform modifications were shown to be prevalent in chicken isolates and confirm that differences in the highly variable flagellin glycosylation locus can relate to the strain source. The discovery of molecular mechanisms influencing the persistence of C. jejuni in poultry aids the rational design of approaches to control this problematic pathogen in the food chain.

* Corresponding author. Mailing address: Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, London WC1E 7HT, United Kingdom. Phone: 44 207 927 2288. Fax: 44 207 637 4314. E-mail: brendan.wren{at}lshtm.ac.uk

{triangledown} Published ahead of print on 23 March 2009.

Editor: S. R. Blanke

Infection and Immunity, June 2009, p. 2544-2556, Vol. 77, No. 6
0019-9567/09/$08.00+0     doi:10.1128/IAI.01425-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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