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Infect Immun, August 1998, p. 3666-3672, Vol. 66, No. 8
Department of Microbiology, Washington State
University, Pullman, Washington 99164-42331;
Department of Plant and Microbial Science, University of
Canterbury, Christchurch, New Zealand2; and
Food and Feed Safety Research Unit, Food Animal Protection
Research Laboratory, Agricultural Research Service, United States
Department of Agriculture, College Station, Texas
7787453
Received 13 March 1998/Returned for modification 5 May
1998/Accepted 1 June 1998
Campylobacter jejuni, a microaerophilic, gram-negative
bacterium, is a common cause of gastrointestinal disease in humans. Heat shock proteins are a group of highly conserved, coregulated proteins that play important roles in enabling organisms to cope with
physiological stresses. The primary aim of this study was to
characterize the heat shock response of C. jejuni.
Twenty-four proteins were preferentially synthesized by C. jejuni immediately following heat shock. Upon immunoscreening of
Escherichia coli transformants harboring a
Campylobacter genomic DNA library, one recombinant plasmid
that encoded a heat shock protein was isolated. The recombinant
plasmid, designated pMEK20, contained an open reading frame of 1,119 bp
that was capable of encoding a protein of 372 amino acids with a
calculated molecular mass of 41,436 Da. The deduced amino acid sequence
of the open reading frame shared similarity with that of DnaJ, which
belongs to the Hsp-40 family of molecular chaperones, from a number of
bacteria. An E. coli dnaJ mutant was successfully
complemented with the pMEK20 recombinant plasmid, as judged by the
ability of bacteriophage
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Characterization of the Thermal Stress Response of
Campylobacter jejuni
to form plaques, indicating that the
C. jejuni gene encoding the 41-kDa protein is a functional
homolog of the dnaJ gene from E. coli. The
ability of each of two C. jejuni dnaJ mutants to form
colonies at 46°C was severely retarded, indicating that DnaJ plays an
important role in C. jejuni thermotolerance. Experiments revealed that a C. jejuni DnaJ mutant was unable to
colonize newly hatched Leghorn chickens, suggesting that heat shock
proteins play a role in vivo.
*
Corresponding author. Mailing address: Department of
Microbiology, Washington State University, Pullman, WA 99164-4233. Phone: (509) 335-5039. Fax: (509) 335-1907. E-mail:
konkel{at}mail.wsu.edu.
Infect Immun, August 1998, p. 3666-3672, Vol. 66, No. 8
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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