scholarly journals Identification of a nth-Like Gene Encoding an Endonuclease III in Campylobacter jejuni

2019 ◽  
Vol 10 ◽  
Author(s):  
Lei Dai ◽  
Jing Xia ◽  
Orhan Sahin ◽  
Qijing Zhang
Keyword(s):  
Campylobacter Jejuni ◽  
Gene Encoding ◽  
Endonuclease Iii

scholarly journals Phase Variation of Campylobacter jejuni 81-176 Lipooligosaccharide Affects Ganglioside Mimicry and Invasiveness In Vitro

2002 ◽  
Vol 70 (2) ◽  
pp. 787-793 ◽  
Author(s):  
Patricia Guerry ◽  
Christine M. Szymanski ◽  
Martina M. Prendergast ◽  
Thomas E. Hickey ◽  
Cheryl P. Ewing ◽  
...  
Keyword(s):  
Campylobacter Jejuni ◽  
Phase Variation ◽  
Outer Core ◽  
Gene Encoding ◽  
Site Specific ◽  
Reading Frame ◽  
Specific Mutation ◽  
Normal Human ◽  
A Site

ABSTRACT The outer cores of the lipooligosaccharides (LOS) of many strains of Campylobacter jejuni mimic human gangliosides in structure. A population of cells of C. jejuni strain 81-176 produced a mixture of LOS cores which consisted primarily of structures mimicking GM2 and GM3 gangliosides, with minor amounts of structures mimicking GD1b and GD2. Genetic analyses of genes involved in the biosynthesis of the outer core of C. jejuni 81-176 revealed the presence of a homopolymeric tract of G residues within a gene encoding CgtA, an N-acetylgalactosaminyltransferase. Variation in the number of G residues within cgtA affected the length of the open reading frame, and these changes in cgtA corresponded to a change in LOS structure from GM2 to GM3 ganglioside mimicry. Site-specific mutation of cgtA in 81-176 resulted in a major LOS core structure that lacked GalNAc and resembled GM3 ganglioside. Compared to wild-type 81-176, the cgtA mutant showed a significant increase in invasion of INT407 cells. In comparison, a site-specific mutation of the neuC1 gene resulted in the loss of sialic acid in the LOS core and reduced resistance to normal human serum but had no affect on invasion of INT407 cells.

scholarly journals A DNase Encoded by Integrated Element CJIE1 Inhibits Natural Transformation of Campylobacter jejuni

2009 ◽  
Vol 191 (7) ◽  
pp. 2296-2306 ◽  
Author(s):  
Esther J. Gaasbeek ◽  
Jaap A. Wagenaar ◽  
Magalie R. Guilhabert ◽  
Marc M. S. M. Wösten ◽  
Jos P. M. van Putten ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Molecular Mechanism ◽  
Campylobacter Jejuni ◽  
Natural Transformation ◽  
Dnase Activity ◽  
Comparative Genome Hybridization ◽  
Dna Uptake ◽  
Knockout Mutant ◽  
Gene Encoding ◽  
Plasmid Analysis

ABSTRACT The species Campylobacter jejuni is considered naturally competent for DNA uptake and displays strong genetic diversity. Nevertheless, nonnaturally transformable strains and several relatively stable clonal lineages exist. In the present study, the molecular mechanism responsible for the nonnatural transformability of a subset of C. jejuni strains was investigated. Comparative genome hybridization indicated that C. jejuni Mu-like prophage integrated element 1 (CJIE1) was more abundant in nonnaturally transformable C. jejuni strains than in naturally transformable strains. Analysis of CJIE1 indicated the presence of dns (CJE0256), which is annotated as a gene encoding an extracellular DNase. DNase assays using a defined dns mutant and a dns-negative strain expressing Dns from a plasmid indicated that Dns is an endogenous DNase. The DNA-hydrolyzing activity directly correlated with the natural transformability of the knockout mutant and the dns-negative strain expressing Dns from a plasmid. Analysis of a broader set of strains indicated that the majority of nonnaturally transformable strains expressed DNase activity, while all naturally competent strains lacked this activity. The inhibition of natural transformation in C. jejuni via endogenous DNase activity may contribute to the formation of stable lineages in the C. jejuni population.

scholarly journals Identification and molecular cloning of a gene encoding a fibronectin‐binding protein (CadF) from Campylobacter jejuni

1997 ◽  
Vol 24 (5) ◽  
pp. 953-963 ◽  
Author(s):  
Michael E. Konkel ◽  
Steven G. Garvis ◽  
Stephanie L. Tipton ◽  
Donald E. Anderson, Jr ◽  
Witold Cieplak, Jr
Keyword(s):  
Molecular Cloning ◽  
Campylobacter Jejuni ◽  
Binding Protein ◽  
Gene Encoding ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

Cloning and expression of the hup gene encoding a histone-like protein of Campylobacter jejuni

Gene ◽  
1994 ◽  
Vol 146 (1) ◽  
pp. 83-86 ◽  
Author(s):  
Michael E. Konkel ◽  
Richard T. Marconi ◽  
David J. Mead ◽  
Witold Cieplak
Keyword(s):  
Campylobacter Jejuni ◽  
Cloning And Expression ◽  
Gene Encoding

scholarly journals Sialylation of Lipooligosaccharide Cores Affects Immunogenicity and Serum Resistance of Campylobacter jejuni

2000 ◽  
Vol 68 (12) ◽  
pp. 6656-6662 ◽  
Author(s):  
Patricia Guerry ◽  
Cheryl P. Ewing ◽  
Thomas E. Hickey ◽  
Martina M. Prendergast ◽  
Anthony P. Moran
Keyword(s):  
Electrophoretic Mobility ◽  
Campylobacter Jejuni ◽  
Polyclonal Antiserum ◽  
Wild Type ◽  
Gene Encoding ◽  
Whole Cells ◽  
Acetylneuraminic Acid ◽  
Genes Encoding ◽  
Hyperimmune Antiserum ◽  
Human Sera

ABSTRACT Three genes involved in biosynthesis of the lipooligosaccharide (LOS) core of Campylobacter jejuni MSC57360, the type strain of the HS:1 serotype, whose structure mimics GM2ganglioside, have been cloned and characterized. Mutation of genes encoding proteins with homology to a sialyl transferase (cstII) and a putative N-acetylmannosamine synthetase (neuC1), part of the biosynthetic pathway ofN-acetylneuraminic acid (NeuNAc), have identical phenotypes. The LOS cores of these mutants display identical changes in electrophoretic mobility, loss of reactivity with cholera toxin (CT), and enhanced immunoreactivity with a hyperimmune polyclonal antiserum generated against whole cells of C. jejuni MSC57360. Loss of sialic acid in the core of the neuC1 mutant was confirmed by fast atom bombardment mass spectrometry. Mutation of a gene encoding a putative β-1,4-N-acetylgalactosaminyltransferase (Cgt) resulted in LOS cores intermediate in electrophoretic mobility between that of wild type and the mutants lacking NeuNAc, loss of reactivity with CT, and a reduced immunoreactivity with hyperimmune antiserum. Chemical analyses confirmed the loss of N-acetylgalactosamine (GalNAc) and the presence of NeuNAc in the cgt mutant. These data suggest that the Cgt enzyme is capable of transferring GalNAc to an acceptor with or without NeuNAc and that the Cst enzyme is capable of transferring NeuNAc to an acceptor with or without GalNAc. A mutant with a nonsialylated LOS core is more sensitive to the bactericidal effects of human sera than the wild type or the mutant lacking GalNAc.

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