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N-glycosylated proteins and distinct lipooligosaccharide glycoforms of Campylobacter jejuni target the human C-type lectin receptor MGL

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العنوان:	N-glycosylated proteins and distinct lipooligosaccharide glycoforms of Campylobacter jejuni target the human C-type lectin receptor MGL
المؤلفون:	Eirikur Saeland, Nina M. van Sorge, Sandra J. van Vliet, Jos P. M. van Putten, Nancy M. C. Bleumink, Yvette van Kooyk, W. Ludo van der Pol
المساهمون:	CCA - Immuno-pathogenesis, Molecular cell biology and Immunology
المصدر:	Cellular Microbiology, 11(12), 1768-1781. Wiley-Blackwell van Sorge, N M, Bleumink, N M C, van Vliet, S J, Saeland, E, van der Pol, W L, van Kooyk, Y & van Putten, J W 2009, ' N-glycosylated proteins and distinct lipooligosaccharide glycoforms of Campylobacter jejuni target the human C-type lectin receptor MGL ', Cellular Microbiology, vol. 11, no. 12, pp. 1768-1781 . https://doi.org/10.1111/j.1462-5822.2009.01370.xTest
سنة النشر:	2009
مصطلحات موضوعية:	Lipopolysaccharides, Glycan, Glycosylation, Acetylgalactosamine, Immunology, CHO Cells, medicine.disease_cause, Microbiology, Campylobacter jejuni, law.invention, Substrate Specificity, chemistry.chemical_compound, Cricetulus, Bacterial Proteins, law, C-type lectin, Virology, Cricetinae, Campylobacter Infections, medicine, Escherichia coli, Animals, Humans, Lectins, C-Type, Edetic Acid, Chelating Agents, Glycoproteins, chemistry.chemical_classification, biology, Interleukin-6, Lectin, Dendritic Cells, biology.organism_classification, Recombinant Proteins, carbohydrates (lipids), Biochemistry, chemistry, Host-Pathogen Interactions, biology.protein, Recombinant DNA, Glycoprotein
الوصف:	An increasing number of bacterial pathogens produce an array of glycoproteins of unknown function. Here we report that Campylobacter jejuni proteins that are modified by the N-linked glycosylation machinery encoded by the pgl locus bind the human Macrophage Galactose-type lectin (MGL). MGL receptor binding was abrogated by EDTA and N-acetylgalactosamine (GalNAc) and was successfully transferred to Escherichia coli by introducing the C. jejuni pgl locus together with a glycan acceptor protein. In addition to glycoproteins, C. jejuni lipooligosaccharide with a terminal GalNAc residue was recognized by MGL. Recombinant E. coli expressing the C. jejuni pgl locus in the absence of a suitable glycan acceptor protein produced altered lipopolysaccharide glycoforms that gained MGL reactivity. Infection assays demonstrated high levels of GalNAc-dependent interaction of the recombinant E. coli with MGL-transfected mammalian cells. In addition, interleukin-6 production by human dendritic cells was enhanced by C. jejuni lacking N-linked glycans compared with wild-type bacteria. Collectively, our results provide evidence that both N-linked glycoproteins and distinct lipooligosaccharide glycoforms of C. jejuni are ligands for the human C-type lectin MGL and that the C. jejuni N-glycosylation machinery can be exploited to target recombinant bacteria to MGL-expressing eukaryotic cells.
تدمد:	1462-5814
الوصول الحر:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b511c01b8c1568aef3f687c74341ee5Test https://hdl.handle.net/1871/28498Test
حقوق:	OPEN
رقم الانضمام:	edsair.doi.dedup.....8b511c01b8c1568aef3f687c74341ee5
قاعدة البيانات:	OpenAIRE

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Here we report that Campylobacter jejuni proteins that are modified by the N-linked glycosylation machinery encoded by the pgl locus bind the human Macrophage Galactose-type lectin (MGL). MGL receptor binding was abrogated by EDTA and N-acetylgalactosamine (GalNAc) and was successfully transferred to Escherichia coli by introducing the C. jejuni pgl locus together with a glycan acceptor protein. In addition to glycoproteins, C. jejuni lipooligosaccharide with a terminal GalNAc residue was recognized by MGL. Recombinant E. coli expressing the C. jejuni pgl locus in the absence of a suitable glycan acceptor protein produced altered lipopolysaccharide glycoforms that gained MGL reactivity. Infection assays demonstrated high levels of GalNAc-dependent interaction of the recombinant E. coli with MGL-transfected mammalian cells. In addition, interleukin-6 production by human dendritic cells was enhanced by C. jejuni lacking N-linked glycans compared with wild-type bacteria. 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