Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
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A series of lipoproteins was detected in the membrane fraction of Yersinia enterocolitica W227, a typical strain from serotype O:9. At least two of them, YlpA and YlpB, are encoded by the pYV plasmid. The sequence of ylpA reveals the presence of a typical lipoprotein signal peptide. The mature YlpA protein would be 223 residues long with a calculated molecular weight of 23798 for the proteic moiety of the molecule. YlpA shares 88% identical residues with the TraT protein encoded by plasmid pED208, 80% identity with TraT proteins encoded by plasmids R100 and F, and 77% identity with the TraT protein encoded by the virulence plasmid of Salmonella typhimurium. The ylpA gene hybridized with the pYV plasmid of Yersinia pseudotuberculosis, suggesting that this gene is conserved among Yersinia spp. The production of YlpA is controlled by virF and only occurs at 37 degrees C in the absence of Ca2+ ions. This co-regulation with the yop genes suggests that ylpA is a virulence determinant. However, mutations in ylpA clearly affect neither the resistance to human serum nor the virulence for intravenously inoculated mice.
Mol Microbiol 1990 Sep
PMID:The pYV plasmid of Yersinia encodes a lipoprotein, YlpA, related to TraT. 228 80

The yopE gene of Yersinia pseudotuberculosis was recently sequenced, and YopE was identified as an indispensable virulence determinant when tested in a mouse model (A. Forsberg and H. Wolf-Watz, Mol. Microbiol. 2:121-133, 1988). In the study described here, the DNA sequences of the yopE genes of Yersinia pestis EV76 and Yersinia enterocolitica 8081 were determined and compared with that of the Y. pseudotuberculosis gene. Only two codons were found to differ, both leading to amino acid replacements, when the gene from Y. pestis was compared. These two replacements were also present in the gene from Y. enterocolitica; in addition, 18 other codons were found to differ. Thirteen of these substitutions led to amino acid replacements. Downstream of the yopE gene, the plasmid partition locus par was found to be conserved in all three species. In Y. enterocolitica 8081, the sequence homology was interrupted by a putative insertion sequence element inserted between the yopE gene and the par region at a position only 5 base pairs downstream of the yopE stop codon. Upstream of the yopE gene, 620 base pairs were conserved in the three species. This region contained a 130-amino-acid-long open reading frame reading in the opposite direction to the yopE gene and expressed a 14-kilodalton protein in minicells. An insertion mutation in this region constructed in Y. pseudotuberculosis expressed significantly lower amounts of YopE protein in vitro than did the corresponding wild type. The expression level could be restored by transcomplementation. This new locus was designated yerA, for yopE-regulating gene A. The yerA mutant was avirulent when mice were challenged by oral infection.
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PMID:Genetic analysis of the yopE region of Yersinia spp.: identification of a novel conserved locus, yerA, regulating yopE expression. 230 58

Plasmids with the sizes of 5.7; 51; 70-77; and 120-130 kb were found in six strains among the ten strains collection of Yersinia pseudotuberculosis. The restriction endonucleases analysis. Southern-blot hybridization and physical maps construction were performed for the plasmids. The 70-77 kb plasmids were found to be analogous to the Ca2(+)-dependence plasmid pYVO19 from Yersinia pestis EV76. The difference between the plasmids of this type is in the insertions or deletions located on the similar fragments of the restriction maps. The 51 kb plasmid has no common fragments with the Ca2(+)-dependence plasmids and does not code for virulence properties of the strain harbouring it. No homology is shared by the 5.7 kb plasmid and the 10 kb plasmid from Yersinia pestis EV76. Replicon of the 5.7 kb plasmid has been used to construct the pVS11 vector plasmid.
Mol Gen Mikrobiol Virusol 1990 Feb
PMID:[Plasmids of Yersinia pseudotuberculosis]. 233 80

92 strains of Yersinia pestis isolated from different natural foci and stored for 3-40 years in the museum of live cultures have been studied. The strains having three typical plasmids, their different combinations, plasmidless strains or the strains carrying nontypical plasmids with the molecular masses 9, 15, 55, 80, 90 and 150 Md were found. The old museum strains are proposed to be used as a source of plasmids for the genetical research. The current control of plasmid contents in the museum strains is suggested by the plasmid changes in course of storage.
Mol Gen Mikrobiol Virusol 1990 Mar
PMID:[Screening of plasmids in museum strains of Yersinia pestis isolated from various natural foci]. 236 98

A pel gene cloned from strain EC153 of Erwinia carotovora encoded a pectate lyase that macerated plant tissue with moderate efficiency. This gene, called pel153, was sequenced and found to possess considerable homology with a pectate lyase gene from Yersinia pseudotuberculosis. The Yersinia protein, however, was truncated at the carboxyl terminal end relative to the Erwinia gene product and had a lower isoelectric point. The Erwinia pel153 gene was overexpressed in cells of Escherichia coli, and a 56-kDa protein was observed on sodium dodecyl sulfate-polyacrylamide gels. This compares with a molecular weight of 61 kDa for the mature, secreted protein as determined from sequencing data. Southern blot analysis disclosed the presence of the pel153 gene in three different strains of E. carotovora, but mutation of the gene in strain EC153 did not affect its ability to soft-rot potato tubers.
Mol Plant Microbe Interact
PMID:Cloning and characterization of a pectate lyase gene from Erwinia carotovora EC153. 252 Jan 59

The effect of temperature on coagulase and fibrinolysin expression (Pla) by Yersinia pestis has been implicated in the transmission of plague by fleas. In an attempt to improve our understanding of this process, we have cloned, sequenced and characterized the gene encoding the Pla phenotypes in Y. pestis, and examined its temperature-dependent regulation. The coding region for this gene overlaps a 900bp Y. pestis-specific DNA fragment that we have previously shown to be capable of detecting plague bacilli in fleas. The pla gene contains a single open reading frame encoding 312 amino acids with a predicted molecular weight of 34.7 kD and a putative signal sequence of 20 amino acids. This coding region appears to be sufficient for both coagulase and fibrinolytic activities. In Y. pestis, modulation between coagulase and fibrinolytic activities is temperature-dependent: coagulase activity is most evident at temperatures below 30 degrees C but fibrinolytic activity increases with higher temperatures (greater than 30 degrees C), regardless of the temperature at which the bacteria are grown. Our results lead us to believe that this regulation occurs post-translationally. It is possible that the alternative forms of the Pla protein are essential to 'flea blockage' and subsequent transmission of the plague bacillus to animals.
Mol Microbiol 1989 Jun
PMID:A Yersinia pestis-specific DNA fragment encodes temperature-dependent coagulase and fibrinolysin-associated phenotypes. 252 82

The strains of Yersinia pestis that restrict their growth on the media deficient for Mg2+ ions at 37 degrees C have been found. The bacterial cell lysis is registered under these conditions. The effect of Yersinia pestis own plasmids on the level of growth restriction in the absence of Mg2+ ions has been studied. The phenomenon is not connected with the presence of the plasmid determining Ca2(+)-dependence. The presence of 6Md plasmid coding for pesticinogenicity increased the frequency of colony formation, while the heavy plasmid determining the production of "mouse" toxin favoured the increase in growth restriction on Mg2(+)-less media. The clones growing under the latter conditions acquire the rearrangements in the DNA of the plasmid coding for the "mouse" toxin.
Mol Gen Mikrobiol Virusol 1989 Dec
PMID:[The effect of Mg 2+ ions on the properties of various strains of Yersinia pestis]. 263 16

A 2 kb fragment of Yersinia pestis genome cloned in Escherichia coli cells of the strain HB101 contains a gene able to complement the recA-dependent deficiency of E. coli cells in UV-resistance, resistance to alkylating agents, UV- and MNNG-induced mutability. Cellular capability for homologous recombination in crosses with HfrH donor, derepressed synthesis of bacteriocins (colicin E1 and pesticin 1) is also complemented by the fragment in E. coli recA-strains. The obtained data suggest the functional homology of the cloned recA-like gene product with the product of E. coli recA-gene.
Mol Gen Mikrobiol Virusol 1989 May
PMID:[Cloning and study of the function of recA-like gene of Yersinia pestis in Escherichia coli cells]. 266 89

Electrophoresis in agarose gel has been used to study the plasmid spectra of 854 Yersinia pseudotuberculosis strains isolated from different sources. The plasmids found in the microbial strains are represented by the elements with molecular masses 82; 57; 45; 5.5; 4.4; 3.5; 2.7; 2.4; 2.3 Md. The variable spectra of plasmids is peculiar only for serovar I of Yersinia pseudotuberculosis. Plasmids p45 and p82 are classified as the main, while other plasmids as auxiliary ones. In accord with the classification all plasmid containing strains are divided into 8 plasmid strains. Using the proposed method for intraspecific typing of Yersinia pseudotuberculosis permits one to perfect the epidemiological analysis of pseudotuberculosis infection and make concrete the direction of prophylactic and antiepidemic measures.
Mol Gen Mikrobiol Virusol 1989 Jun
PMID:[Analysis of the plasmid composition of Yersinia pseudotuberculosis strains and its use for typing pseudotuberculosis pathogens]. 268 19

The entry of enteropathogenic Yersinia into cultured mammalian cells has been studied in order to gain insight into the mechanism of bacterial penetration into host cells during infection. There exist at least three pathways for entry by Yersinia into mammalian cells, the most efficient of which is promoted by invasin, the product of the inv gene. Invasin is an outer membrane protein that attaches to a mammalian cell receptor, initiating the entry process. Several receptors that bind invasin have been identified, and each is a member of the VLA family of integrin cell adhesion molecules. The role of integrins in the entry process is discussed, as is the ability of invasin to stimulate uptake by binding to its integrin receptor.
Mol Microbiol 1989 Oct
PMID:Mammalian cell adhesion functions and cellular penetration of enteropathogenic Yersinia species. 269 98


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