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Infection and Immunity, October 2000, p. 5679-5689, Vol. 68, No. 10
Food Animal Health Research
Program,1 and Department of Veterinary
Preventive Medicine,2 The Ohio State
University, Wooster, Ohio 44691
Received 10 April 2000/Returned for modification 10 May
2000/Accepted 10 July 2000
The major outer membrane protein (MOMP), a putative porin and a
multifunction surface protein of Campylobacter jejuni, may play an important role in the adaptation of the organism to various host environments. To begin to dissect the biological functions and
antigenic features of this protein, the gene (designated
cmp) encoding MOMP was identified and characterized from 22 strains of C. jejuni and one strain of C. coli.
It was shown that the single-copy cmp locus encoded a
protein with characteristics of bacterial outer membrane proteins.
Prediction from deduced amino acid sequences suggested that each MOMP
subunit consisted of 18
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Copyright © 2000, American Society for Microbiology. All rights reserved.
Sequence Polymorphism, Predicted Secondary Structures, and
Surface-Exposed Conformational Epitopes of Campylobacter
Major Outer Membrane Protein
-strands connected by short periplasmic
turns and long irregular external loops. Alignment of the amino acid
sequences of MOMP from different strains indicated that there were
seven localized variable regions dispersed among highly conserved
sequences. The variable regions were located in the putative external
loop structures, while the predicted
-strands were formed by
conserved sequences. The sequence homology of cmp appeared
to reflect the phylogenetic proximity of C. jejuni strains,
since strains with identical cmp sequences had
indistinguishable or closely related macrorestriction fragment
patterns. Using recombinant MOMP and antibodies recognizing linear or
conformational epitopes of the protein, it was demonstrated that
the surface-exposed epitopes of MOMP were predominantly
conformational in nature. These findings are instrumental in the design
of MOMP-based diagnostic tools and vaccines.
*
Corresponding author. Mailing address: Food Animal
Health Research Program, Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, The Ohio State University, 1680 Madison Ave., Wooster, OH 44691. Phone: (330) 263-3747. Fax: (330) 263-3677. E-mail: zhang.234{at}osu.edu.
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