Relation of lipopolysaccharide character to P1 sensitivity in Salmonella typhimurium☆
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2022, Journal of Molecular BiologyCitation Excerpt :Furthermore, quantification of P1(S') transduction efficiency on various Gram-negative Enterobactericae, coupled with structural studies of the P1(S') tail fibre as well as the use of synthetic glycans mimicking different regions of LPS oligosaccharides, will help in identifying its receptor and the mechanisms behind P1(S') adsorption. Earlier studies suggested that P1(S) tail fibre recognises the terminal glucose molecule on the outer LPS core without discriminating the orientation of a glycosidic bond.16,49,56 Indeed, glucose molecule is present in the LPS of E. coli and S. flexneri strains tested in our study, which is consistent with the fact that P1(S) infected most of these bacteria.
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2013, Research in MicrobiologyCitation Excerpt :However, when P1cml,clr100 was prepared from a serovar Choleraesuis lysogen (with a low yield of ∼2 × 106 pfu/ml) and used to infect the wild-type strain of Choleraesuis, the frequency of lysogenization was about 4 × 10−3 lysogens/pfu, an observation that suggests additional difficulties for infection over the effect of restriction. P1 resistance in serovars of Salmonella other than Choleraesuis seems to be due to blockage of P1 adsorption by the O antigen (Ornellas and Stocker, 1974). However, serovar Choleraesuis belonging to group C1, possessing antigen O6,7 (LeMinor, 1991) displays less hindrance to infection by P1, a fact that might reflect increased availability particular to the O6,7 antigen.
Genetic Manipulation of Pathogenicity Loci in Non-Typhimurium Salmonella
2012, Journal of Microbiological MethodsCitation Excerpt :Despite its close relatedness to these species, Salmonella strains are resistant to P1. However, mutations in the galE gene confer sensitivity to phage P1 in serovar Typhimurium LT2 (Ornellas and Stocker, 1974); these mutants are unable to epimerize UDP-glucose to UDP-galactose, a required building block for the lipopolysaccharide (LPS) core antigen that forms the foundation for anchoring the O-antigen to the outer membrane (Figure S1). UDP-galactose is also required by many Salmonella serovars to initiate O-antigen biosynthesis (Samuel and Reeves, 2003).
Glutamate at the site of phosphorylation of nitrogen-regulatory protein NTRC mimics aspartyl-phosphate and activates the protein
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This work was supported by Public Health Service Research Grant AI-07168 and Public Health Service Training Grant AI-82 from the National Institute of Allergy and Infectious Diseases.
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Present address: Urology Research, Harvard Medical School, Massachusetts General Hospital, Boston, Massachusetts 02114.