Disease relevance of traT

• The remainder of the predicted protein showed an amino acid composition almost identical with that determined for the traT protein from the E. coli F factor [1].
• The structural gene for the F sex factor outer membrane surface exclusion protein ( traT ) was cloned onto a high-copy-number plasmid where it is expressed from the phage lambda promoter pL [2].
• Contribution of the traT gene to serum resistance among clinical isolates of enterobacteriaceae [3].
• The traT protein is able to normalize the phenotype of a plasmid-carried permeability mutation of Salmonella typhimurium [4].
• TraT lipoprotein, a plasmid-specified mediator of interactions between gram-negative bacteria and their environment [5].

High impact information on traT

• The product of the F sex factor traT surface exclusion gene is a lipoprotein [6].
• The product of the Escherichia coli sex factor F traT gene (TraTp), an outer membrane protein of Mr = 25,000, is covalently modified in vivo by the addition of glycerol and fatty acids [6].
• Being a secreted protein, TraTp is made from a signal sequence containing precursor, and glycerol and fatty acids can be detected in both the precursor and mature (processed) species of TraTp [6].
• Consistent with this result, and as would be expected for a bacterial lipoprotein, the novel amino acid glycerylcysteine can be detected in purified TraTp [6].
• Diglyceride modification of the Cys residue at the site of signal sequence cleavage probably precedes and is a prerequisite for processing of the TraTp signal sequence [6].

Chemical compound and disease context of traT

• To show a new potential use of the TraT display system, we employed a biotin labeling technique coupled with SDS-PAGE and flow cytometry analyses to further demonstrate and confirm the expression of TraT-RHO on the E. coli surface [7].

Biological context of traT

• Nucleotide sequence of the surface exclusion genes traS and traT from the IncF0 lac plasmid pED208 [8].
• The nucleotide sequences of several traT genes have been determined, and comparison of the corresponding amino acid sequences suggests that a central region of five amino acid residues flanked by hydrophobic domains determines the specificity of the protein in surface exclusion [5].
• Altogether 49% of Finnish and 42% of Israeli isolates had at least one virulence gene, but genes other than traT were present in only 24% of Finnish and 5% of Israeli isolates [9].
• None of the antimicrobial resistance patterns of the isolates were the same as those demonstrated by R plasmids known to carry the traT gene [10].
• Only clones with functioning traT (irrespective of copy number) restored the normal antibiotic-resistant phenotype in the SS-A mutant [4].

Anatomical context of traT

• The incidence of traT in strains isolated from cases of urinary tract infections was variable. traT was found to be frequently associated with production of the K1 capsule and with the carriage of ColV plasmids, but not with the carriage of R plasmids, nor with serum resistance or the production of haemolysin [11].
• Augmentation of HIV-specific lymphoproliferation in HIV-infected individuals by TraT: a novel T-cell immunopotentiating agent [12].
• The presence of the outer membrane protein TraT, encoded by plasmid R6-5, reduces the sensitivity of Escherichia coli cells to phagocytosis by macrophages [13].

Associations of traT with chemical compounds

• Compared with probe hybridization, the PCR assay's specificity was 100% and sensitivity 97.1%. fyuA (yersiniabactin: overall prevalence, 93%), traT (serum resistance, 68%), and a pathogenicity-associated island marker (71%) occurred in most strains from both compromised and noncompromised hosts [14].
• Under conditions in which traT and iss conferred at least a 50- and 10-fold increase in survival, respectively, the consumption of C6, C7, C8, and C9 was the same for bacteria with and without the plasmid genes [15].
• Both had a smooth lipopolysaccharide layer, contained traT, and lacked a capsule, but the mutant possessed a 16.2-kilodalton outer-membrane protein (OMP) not present in the wild-type [16].
• This plasmid DNA was examined for the presence of certain known virulence-related genes including cvaC, traT, and some aerobactin-related sequences [17].
• The structure and function of the TraT protein determined by plasmid R6-5 was probed by genetic insertion of a foreign antigenic determinant, the C3 epitope of polio virus, at residues 61, 125, 180, 200 or 216 of the protein [18].

Other interactions of traT

• Ten VFs were less prevalent (p <0.05) in the ESBL isolates than the susceptible E. coli, while iutA and traT were more prevalent in ESBL isolates (p <0.05) [19].
• No significant differences were found between the two groups of isolates in the occurrence of cvaC-, traT-, or ompA-homologous sequences or in rLPSr [20].
• Further characterization of complement resistance conferred on Escherichia coli by the plasmid genes traT of R100 and iss of ColV,I-K94 [15].

Analytical, diagnostic and therapeutic context of traT

• Furthermore, we showed, using immunoprecipitation of TraTp, that normal amounts of this protein could be present in the cell without producing normal levels of surface exclusion [21].
• TraTp wqs also examined by two-dimensional gel electrophoresis, where it ran as a discrete spot with a very basic isoelectric point [22].

References