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Campylobacter fetus of reptile origin as a human pathogen.

ABSTRACT: A Campylobacter species was isolated from blood from a febrile patient with precursor T-cell acute lymphoblastic leukemia, and after antibiotic treatment, a similar bacterium was isolated from blood 37 days later. Although phenotypic testing did not definitively identify the organisms, molecular analysis indicated that they were the same strain of Campylobacter fetus subsp. fetus and were of reptile origin.

SUBMITTER: Tu ZC

PROVIDER: S-EPMC516294 | biostudies-literature | 2004 Sep

REPOSITORIES: biostudies-literature

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Campylobacter fetus of reptile origin as a human pathogen.

Tu Zheng-Chao ZC Zeitlin Gary G Gagner Jean-Pierre JP Keo Thormika T Hanna Bruce A BA Blaser Martin J MJ

Journal of clinical microbiology 20040901 9

A Campylobacter species was isolated from blood from a febrile patient with precursor T-cell acute lymphoblastic leukemia, and after antibiotic treatment, a similar bacterium was isolated from blood 37 days later. Although phenotypic testing did not definitively identify the organisms, molecular analysis indicated that they were the same strain of Campylobacter fetus subsp. fetus and were of reptile origin. ...[more]

PMID: 15365057

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Project description:Campylobacter fetus is commonly associated with venereal disease and abortions in cattle and sheep, and can also cause intestinal or systemic infections in humans that are immunocompromised, elderly, or exposed to infected livestock. It is also believed that C. fetus infection can result from the consumption or handling of contaminated food products, but C. fetus is rarely detected in food since isolation methods are not suited for its detection and the physiology of the organism makes culturing difficult. In the related species, Campylobacter jejuni, the ability to colonize the host has been linked to N-linked protein glycosylation with quantitative proteomics demonstrating that glycosylation is interconnected with cell physiology. Using label-free quantitative (LFQ) proteomics, we found more than 100 proteins significantly altered in expression in two C. fetus subsp. fetus protein glycosylation (pgl) mutants (pglX and pglJ) compared to the wild-type. Significant increases in the expression of the (NiFe)-hydrogenase HynABC, catalyzing H2-oxidation for energy harvesting, correlated with significantly increased levels of cellular nickel, improved growth in H2 and increased hydrogenase activity, suggesting that N-glycosylation in C. fetus is involved in regulating the HynABC hydrogenase and nickel homeostasis. To further elucidate the function of the C. fetus pgl pathway and its enzymes, heterologous expression in Escherichia coli followed by mutational and functional analyses revealed that PglX and PglY are novel glycosyltransferases involved in extending the C. fetus hexasaccharide beyond the conserved core, while PglJ and PglA have similar activities to their homologs in C. jejuni. In addition, the pgl mutants displayed decreased motility and ethidium bromide efflux and showed an increased sensitivity to antibiotics. This work not only provides insight into the unique protein N-glycosylation pathway of C. fetus, but also expands our knowledge on the influence of protein N-glycosylation on Campylobacter cell physiology.

Dataset Information

Campylobacter fetus of reptile origin as a human pathogen.

Publications

Campylobacter fetus of reptile origin as a human pathogen.

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