Analysis of Yersinia pestis chromosomal determinants Pgm+ and Psts associated with virulence

Кутырев, Владимир; Filippov, Andrew A.; Oparina, O. S.; Protsenko, Oľga A.

doi:10.1016/0882-4010(92)90051-o

Cited by 56 publications

(41 citation statements)

References 28 publications

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“…Earlier studies showed that Hms ϩ but not Hms Ϫ strains of Y. pestis were able to block the flea proventriculus, the valve which separates the esophagus from the midgut of the flea. Efficient transmission of plague from fleas to mammals is dependent upon blockage of the flea by biofilm formation (17,21,25,34). Temperature-dependent expression of the Hms phenotype is probably controlled by the degradation of select Hms proteins.…”

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confidence: 99%

Phenotypic Convergence Mediated by GGDEF-Domain-Containing Proteins

et al. 2005

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GGDEF domain-containing proteins have been implicated in bacterial signal transduction and synthesis of the second messenger molecule cyclic-di-GMP. A number of GGDEF proteins are involved in controlling the formation of extracellular matrices. AdrA (Salmonella enterica serovar Typhimurium) and HmsT (Yersinia pestis) contain GGDEF domains and are required for extracellular cellulose production and biofilm formation, respectively. Here we show that hmsT is able to restore cellulose synthesis to a Salmonella serovar Typhimurium adrA mutant and that adrA can replace hmsT in Y. pestis Hms-dependent biofilm formation. Like Y. pestis HmsT overproducers, Y. pestis cells carrying adrA under the control of an arabinose-inducible promoter produced substantial biofilms in the presence of arabinose. Finally, we demonstrate that HmsT is involved in the synthesis of cyclic di-GMP.

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Phenotypic Convergence Mediated by GGDEF-Domain-Containing Proteins

et al. 2005

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“…Transmission of Y. pestis from some fleas to mammals involves colonization and blockage of the proventricular valve, which separates the midgut from the esophagus (24,27). This blockage depends upon a set of genes in Y. pestis, designated the hemin storage (hms) locus, that are involved in the production of an extracellular matrix or biofilm and causes the flea to regurgitate a bacterium-laced blood meal (9,24,34). The hmsHFRS and hmsT genes were first identified as essential for temperature-dependent hemin and Congo red (CR) binding by Y. pestis.…”

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Polyamines Are Essential for the Formation of Plague Biofilm

Patel¹,

Wortham²,

et al. 2006

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We provide the first evidence for a link between polyamines and biofilm levels in Yersinia pestis, the causative agent of plague. Polyamine-deficient mutants of Y. pestis were generated with a single deletion in speA or speC and a double deletion mutant. The genes speA and speC code for the biosynthetic enzymes arginine decarboxylase and ornithine decarboxylase, respectively. The level of the polyamine putrescine compared to the parental speA ؉ speC ؉ strain (KIM6؉) was depleted progressively, with the highest levels found in the Y. pestis ⌬speC mutant (55% reduction), followed by the ⌬speA mutant (95% reduction) and the ⌬speA ⌬speC mutant (>99% reduction). Spermidine, on the other hand, remained constant in the single mutants but was undetected in the double mutant. The growth rates of mutants with single deletions were not altered, while the ⌬speA ⌬speC mutant grew at 65% of the exponential growth rate of the speA ؉ speC ؉ strain. Biofilm levels were assayed by three independent measures: Congo red binding, crystal violet staining, and confocal laser scanning microscopy. The level of biofilm correlated to the level of putrescine as measured by high-performance liquid chromatography-mass spectrometry and as observed in a chemical complementation curve. Complementation of the ⌬speA ⌬speC mutant with speA showed nearly full recovery of biofilm to levels observed in the speA ؉ speC ؉ strain. Chemical complementation of the double mutant and recovery of the biofilm defect were only observed with the polyamine putrescine.

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“…Regions of the pgm locus not involved in hemin storage have been linked to the iron-regulated expression of several proteins (IrpB to IrpE and HMWP1 HMWP2) and sensitivity to the bacteriocin pesticin (7,22,53,65). Only Pgm' Y pestis cells lacking the 9.5-kb pesticin plasmid (encoding pesticin and immunity to pesticin) are sensitive (Psts) to the bacteriocin (7 [38]), which is part of a Pgm-linked inorganiciron transport system (64,65). We have previously reported the cloning and sequencing of the Y pestis fur homolog of the E. coli fur gene and demonstrated its ability to complementfur mutations in E. coli and Y enterocolitica.…”

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Pleiotropic effects of a Yersinia pestis fur mutation

1994

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A Yersinia pestis fur mutation was constructed by insertionally disrupting the fur open reading frame.Analysis of a Fur-regulated 0-galactosidase reporter gene revealed a loss of iron regulation as a result of the fur mutation. trans complementation with the cloned Y. pestisfur gene restored iron regulation. The expression of most iron-regulated proteins was also deregulated by this mutation; however, a number of iron-repressible and two iron-inducible polypeptides retained normal regulation. Mutations infur or hmsH, a gene encoding an 86-kDa surface protein required for hemin storage, increased the sensitivity of Y. pestis cells to the bacteriocin pesticin. Interestingly, the Y. pestis fur mutant lost temperature control of hemin storage; however, expression of the HmsH polypeptide was not deregulated. When grown with excess iron, a Y. pestisfur mutant possessing the 102-kb pigmentation locus exhibited severe growth inhibition and a dramatic increase in the number of spontaneous nonpigmented chromosomal deletion mutants present at late log phase. These results suggest that the Fur protein of Y. pestis is an important global regulator and that a separate Fur-independent iron regulatory system may exist.Iron is an essential element that must often be acquired from iron-deficient environments. The regulation of diverse genes belonging to global iron limitation stimulons has been described previously for a number of bacteria, including Escherichia coli (6,10,37,47,51), Vibrio species (20, 25, 69), yersiniae (12,13,65,68), Neisseria gonorrhoeae (4), Neisseria meningitidis (73), Pseudomonas aeruginosa (60), shigellae (52), Salmonella typhimurium (18), Corynebacterium diphtheriae (5, 62), and Serratia marcescens (58). Many of these iron-regulated factors are involved in virulence, especially acquisition of iron from the host (9, 27, 51), while the roles of other genes in virulence or iron acquisition are less clearly defined. The coordinate regulation of these iron-regulated genes in a number of bacterial species is controlled by the Fur (ferric uptake regulation) system (4,10,11,18,20,25,33,58,60,67,68).The Fur protein is a negative transcriptional regulator that binds DNA when complexed with ferrous iron or other divalent metal ions. Fur-regulated genes possess operator regions with Fur binding sequences (Fur boxes). These -21-bp regions contain inverted repeats which are bound by the Fur-Fe2" complex, thereby preventing transcription. Insufficient cytoplasmic ferrous iron results in apo-Fur and relieves this repression (6, 47).In Yersinia pestis, iron starvation at 370C induces over 30 iron-repressible proteins (44) and an energy-dependent, highaffinity inorganic-iron uptake system which is inhibited by relatively weak iron chelators (56

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Analysis of Yersinia pestis chromosomal determinants Pgm+ and Psts associated with virulence

Cited by 56 publications

References 28 publications

Phenotypic Convergence Mediated by GGDEF-Domain-Containing Proteins

Phenotypic Convergence Mediated by GGDEF-Domain-Containing Proteins

Polyamines Are Essential for the Formation of Plague Biofilm

Pleiotropic effects of a Yersinia pestis fur mutation

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