JlpA, a novel surface-exposed lipoprotein specific to Campylobacter jejuni, mediates adherence to host epithelial cells

Jin, Sun; Joe, Angela; Lynett, Jennifer; Hani, Eric Kurt; Sherman, Philip M.; Chan, Vivien

doi:10.1046/j.1365-2958.2001.02294.x

Cited by 34 publications

(54 citation statements)

References 31 publications

(39 reference statements)

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“…H. hepaticus and H. pylori both lack orthologs of CadF and JlpA (Cj0983). The latter finding is consistent with a report that jlpA (together with the hippurate hydrolase gene hipO) has been acquired by C. jejuni quite recently, and was not present in the common ancestor of C. jejuni and Campylobacter coli (33).…”

Section: Resultssupporting

confidence: 92%

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The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus

Suerbaum

Josenhans

Sterzenbach

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

221

255

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Helicobacter hepaticus causes chronic hepatitis and liver cancer in mice. It is the prototype enterohepatic Helicobacter species and a close relative of Helicobacter pylori, also a recognized carcinogen. Here we report the complete genome sequence of H. hepaticus ATCC51449. H. hepaticus has a circular chromosome of 1,799,146 base pairs, predicted to encode 1,875 proteins. A total of 938, 953, and 821 proteins have orthologs in H. pylori, Campylobacter jejuni, and both pathogens, respectively. H. hepaticus lacks orthologs of most known H. pylori virulence factors, including adhesins, the VacA cytotoxin, and almost all cag pathogenicity island proteins, but has orthologs of the C. jejuni adhesin PEB1 and the cytolethal distending toxin (CDT). The genome contains a 71-kb genomic island (HHGI1) and several genomic islets whose G؉C content differs from the rest of the genome. HHGI1 encodes three basic components of a type IV secretion system and other virulence protein homologs, suggesting a role of HHGI1 in pathogenicity. The genomic variability of H. hepaticus was assessed by comparing the genomes of 12 H. hepaticus strains with the sequenced genome by microarray hybridization. Although five strains, including all those known to have caused liver disease, were indistinguishable from ATCC51449, other strains lacked between 85 and 229 genes, including large parts of HHGI1, demonstrating extensive variation of genome content within the species.genomics ͉ pathogenicity island ͉ evolution

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Section: Resultssupporting

confidence: 92%

“…Three proteins, PEB1 (also called CBF1) (31), CadF (32), and JlpA (33) have been shown to be involved in adhesion of C. jejuni to epithelial cells. H. hepaticus has a protein (HH1481) with strong homology (72% amino acid identity) to PEB1, which is not present in H. pylori.…”

Section: Resultsmentioning

confidence: 99%

The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus

Suerbaum

Josenhans

Sterzenbach

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

221

255

View full text Add to dashboard Cite

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“…Putative adhesion factors have been identified, e.g. the fibronectinbinding proteins CadF and FlpA (Konkel et al, 1997(Konkel et al, , 2010, the autotransporter CapA, and a surface-exposed lipoprotein, JIpA (Jin et al, 2001). In addition, the sialylated lipooligosaccharide outer core of C. jejuni has been demonstrated to be an important factor for the invasion of epithelial cells (Guerry et al, 2000;Louwen et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

et al. 2010

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Campylobacter jejuni, an important food-borne bacterial pathogen in industrialized countries and in the developing world, is one of the major causes of bacterial diarrhoea. To identify genes which are important for the invasion of host cells by the pathogen, we screened altogether 660 clones of a transposon-generated mutant library based on the clinical C. jejuni isolate B2. Thereby, we identified a clone with a transposon insertion in gene cj0952c. As in the well-characterized C. jejuni strain NCTC 11168, the corresponding protein together with the gene product of the adjacent gene cj0951c consists of two transmembrane domains, a HAMP domain and a putative MCP domain, which together are thought to act as a chemoreceptor, designated Tlp7. In this report we show that genes cj0952c and cj0951c (i) are important for the host cell invasion of the pathogen, (ii) are not translated as one protein in C. jejuni isolate B2, contradicting the idea of a postulated read-through mechanism, (iii) affect the motility of C. jejuni, (iv) alter the chemotactic behaviour of the pathogen towards formic acid, and (v) are not related to the utilization of formic acid by formate dehydrogenase.

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“…The recent emergence of antibiotic-resistant strains has triggered renewed interest for the understanding of the pathogenesis of C. jejuni (2,3), which could lead to the identification of novel targets that could be further investigated for the development of therapeutics. A variety of virulence factors has been identified, such as the lipo-oligosaccharide (4 -7), capsule (8), flagellum (9), toxins (10), and adhesins (11)(12)(13)(14). They allow for colonization and invasion of the intestinal epithelium and protection against host immune defense systems.…”

mentioning

confidence: 99%

Cj1121c, a Novel UDP-4-keto-6-deoxy-GlcNAc C-4 Aminotransferase Essential for Protein Glycosylation and Virulence in Campylobacter jejuni

Somalinga

Merkx-Jacques

Ratnayake

et al. 2006

Journal of Biological Chemistry

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Campylobacter jejuni produces glycoproteins that are essential for virulence. These glycoproteins carry diacetamidobacillosamine (DAB), a sugar that is not found in humans. Hence, the enzymes responsible for DAB synthesis represent potential therapeutic targets. We describe the biochemical characterization of Cj1121c, a putative aminotransferase encoded by the general protein glycosylation locus, to assess its role in DAB biosynthesis. By using overexpressed and affinity-purified enzyme, we demonstrate that Cj1121c has pyridoxal phosphate-and glutamate-dependent UDP-4-keto-6-deoxy-GlcNAc C-4 transaminase activity and produces UDP-4-amino-4,6-dideoxy-GlcNAc. This is consistent with a role in DAB biosynthesis and distinguishes Cj1121c from Cj1294, a homologous UDP-2-acetamido-2,6-dideoxy-␤-L-arabino-4-hexulose C-4 aminotransferase that we characterized previously. We show that Cj1121c can also use this 4-keto-arabino sugar indirectly as a substrate, that Cj1121c and Cj1294 are active simultaneously in C. jejuni, and that the activity of Cj1121c is preponderant under standard growth conditions. Kinetic data indicate that Cj1121c has a slightly higher catalytic efficiency than Cj1294 with regard to the 4-keto-arabino substrate. By site-directed mutagenesis, we show that residues Glu-158 and Leu-131 are not essential for catalysis or for substrate specificity contrary to expectations. We further demonstrate that a cj1121c knock-out mutant is impaired for flagella-mediated motility, for invasion of intestinal epithelial cells, and for persistence in the chicken intestine, clearly demonstrating that Cj1121c is essential for host colonization and virulence. Finally, we show that cj1121c is necessary for protein glycosylation by lectin Western blotting. Collectively, these results validate Cj1121c as a promising drug target and provide the means to assay for inhibitors.

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JlpA, a novel surface-exposed lipoprotein specific to Campylobacter jejuni, mediates adherence to host epithelial cells

Cited by 34 publications

References 31 publications

The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus

The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

Cj1121c, a Novel UDP-4-keto-6-deoxy-GlcNAc C-4 Aminotransferase Essential for Protein Glycosylation and Virulence in Campylobacter jejuni

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