Zobrazeno 1 - 10
of 57
pro vyhledávání: '"Isabelle Saint Girons"'
Autor:
Paula Ristow, Pascale Bourhy, Flávia Weykamp da Cruz McBride, Claudio Pereira Figueira, Michel Huerre, Patrick Ave, Isabelle Saint Girons, Albert I Ko, Mathieu Picardeau
Publikováno v:
PLoS Pathogens, Vol 3, Iss 7, p e97 (2007)
Pathogenic mechanisms of Leptospira interrogans, the causal agent of leptospirosis, remain largely unknown. This is mainly due to the lack of tools for genetic manipulations of pathogenic species. In this study, we characterized a mutant obtained by
Externí odkaz:
https://doaj.org/article/734f8db732ae4f868a3cff735ce760ce
Differential TLR Recognition of Leptospiral Lipid A and Lipopolysaccharide in Murine and Human Cells
Autor:
Catherine Werts, Viviane Balloy, Christian R. H. Raetz, Isabelle Saint Girons, Edith Fournié-Amazouz, Marie-Anne Nahori, Michel Chignard, Nanette L.S. Que-Gewirth
Publikováno v:
The Journal of Immunology. 175:6022-6031
Leptospira interrogans is a spirochete that is responsible for leptospirosis, a zoonotic disease. This bacterium possesses an unusual LPS that has been shown to use TLR2 instead of TLR4 for signaling in human cells. The structure of its lipid A was r
Autor:
Suzanne R. Kalb, Christian R. H. Raetz, Anthony A. Ribeiro, Robert J. Cotter, Nanette L S Que-Gewirth, Dieter M. Bulach, Isabelle Saint Girons, Ben Adler, Catherine Werts
Publikováno v:
Journal of Biological Chemistry. 279:25420-25429
Leptospira interrogans differs from other spirochetes in that it contains homologs of all the Escherichia coli lpx genes required for the biosynthesis of the lipid A anchor of lipopolysaccharide (LPS). LPS from L. interrogans cells is unusual in that
Publikováno v:
Molecular Microbiology. 49:745-754
Unlike the spirochetes Borrelia burgdorferi and Treponema pallidum, Leptospira spp. contain genes encoding the enzymes for most biosynthetic pathways. In this study, we describe the first haem biosynthetic pathway genes in the order Spirochaetales. S
Publikováno v:
FEMS Microbiology Letters. 229:277-281
Toxin-antitoxin systems encoded by bacterial plasmids and chromosomes typically consist of a toxin that inhibits growth of the host cell and a specific antitoxin. In this report, the chpK gene from the chromosomal toxin-antitoxin locus of the spiroch
Publikováno v:
Microbiology. 149:689-693
In bacteria, the first reaction of the tryptophan biosynthetic pathway involves the conversion of chorismate and glutamine to anthranilate by the action of anthranilate synthase, which is composed of the alpha (trpE gene product) and beta (trpG gene
Autor:
Stewart T. Cole, Isabelle Saint-Girons
This chapter summarizes the recent findings of bacterial genomics and comments on the themes and trends which are emerging. A variety of techniques and methods are available to construct physical maps, and those most commonly employed involve pulsed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ed21f81f7fc06280d73f12a98daae388
https://doi.org/10.1128/9781555818180.ch3
https://doi.org/10.1128/9781555818180.ch3
Publikováno v:
Molecular Microbiology. 40:189-199
Leptospira spp. offer many advantages as model bacteria for the study of spirochaetes. However, homologous recombination between introduced DNA and the corresponding chromosomal loci has never been demonstrated. A unique feature of spirochaetes is th
Autor:
Isabelle Saint Girons, Pascale Bourhy
Publikováno v:
FEMS Microbiology Letters. 191:259-263
An open reading frame of 885 nucleotides was identified as the Leptospira interrogans metF gene. The deduced amino acid sequence (294 amino acids) showed similarities with Escherichia coli methylene tetrahydrofolate reductase (MetF or MTHFR) (33% ide
Autor:
S. Strathdee, K. Phillips, O. Navratil, John B. Rafferty, Iain W. Manfield, Peter G. Stockley, Simon E. V. Phillips, Isabelle Saint-Girons, William S. Somers, Iain G. Old, Teresa McNally, Yi-Yuan He
Publikováno v:
Annals of the New York Academy of Sciences. 726:105-117
The crystal structure of the E. coli met repressor in complex with a synthetic 19-base pair oligonucleotide reveals two dimeric repressor molecules bound to adjacent sites on the DNA. The oligonucleotide contains two adjacent repeats of an 8-mer know