Identification and cloning of a hemin storage locus involved in the pigmentation phenotype of Yersinia pestis

Perry, Robert D.; Pendrak, Michael L.; Schuetze, Paul

doi:10.1128/jb.172.10.5929-5937.1990

Cited by 169 publications

(165 citation statements)

References 45 publications

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“…Primers Iuc-3 and Iuc-4 were used to amplify a 539 bp digoxigenin (DIG)-labelled fragment from the aerobactin locus of KIM6+ genomic DNA. Colony blot hybridization of the DIG-labelled fragment to a KIM6+ genomic DNA library (Perry et al, 1990) resulted in the identification of clone 1985 (renamed pAero1985; Table 1). Based upon restriction enzyme analysis and DNA sequencing, pAero1985 contains a 9035 bp insert that encompasses the putative aerobactin biosynthetic genes (iucA1-A2-B-C-D) and the outer-membrane receptor (iutA) (data not shown).…”

Section: Methodsmentioning

confidence: 99%

“…Primers Fhu-1 and Fhu-2 were used to generate a 302 bp DIG-labelled probe that hybridized to clone 1310 (renamed pFhuYp1310) in the KIM6+ genomic library (Perry et al, 1990). This clone contains an approximately 8.3 kb insert that includes the Y. pestis fhuCDB operon.…”

Section: Methodsmentioning

confidence: 99%

“…A recombinant plasmid, pAero1985, containing the aerobactin region was identified from a Y. pestis genomic library (Perry et al, 1990). The insert of pAero1985 includes 373 bp of DNA upstream of the putative start codon for iucA1, containing the putative promoter elements and the iucA2, iucB, iucC, iucD and iutA genes.…”

Section: Y Pestis Does Not Synthesize Aerobactinmentioning

confidence: 99%

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Analysis of the aerobactin and ferric hydroxamate uptake systems of Yersinia pestis

et al. 2007

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Yersinia pestis genomes contain genes homologous to the aerobactin receptor (iutA) and biosynthetic genes (iucABCD) as well as the ferric hydroxamate uptake system (fhuCDB) of Escherichia coli. However, iucA is disrupted by a frameshift mutation. An E. coli strain carrying the cloned Y. pestis aerobactin region was unable to produce aerobactin, but could use the siderophore as an iron source. Repair of the frameshift mutation in iucA did not allow aerobactin production in E. coli or Y. pestis. In contrast, a Y. pestis strain with a plasmid encoding the iucABCD-iutA genes from Shigella flexneri or pColV-K30 did produce and secrete the siderophore. In addition, Yersinia pseudotuberculosis PB1, which encodes the iucABCD-iutA locus without the Y. pestis-specific frameshift mutation, also failed to produce aerobactin. The Y. pestis fhuCDB operon, encoding an ABC transporter for a range of hydroxamate siderophores, was able to complement a strain of E. coli with a transposon insertion in fhuC, allowing utilization of aerobactin and ferrichrome. Y. pestis KIM6, a strain deficient in the production of the siderophore yersiniabactin, was able to use both the ferrichrome and the aerobactin siderophores as a source of iron. Mutations in iutA or the fhu operon abolished the ability of KIM6 to use aerobactin. Mutations in the fhu operon, but not in iutA, affected the ability of KIM6 to use ferrichrome. This demonstrates that Y. pestis uses both ferrichrome and aerobactin, but has lost the ability to synthesize aerobactin.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Y Pestis Does Not Synthesize Aerobactinmentioning

confidence: 99%

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Analysis of the aerobactin and ferric hydroxamate uptake systems of Yersinia pestis

et al. 2007

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“…However, studies with Pgm-Y. pestis M23 derivatives containing p H M S l exhibit a n H m s " phenotype (Lillard et al, 1997;Pendrak & Perry, 1991Perry et al, 1990). T h i s suggests t h a t additional fnctor(s) encoded outside the pgm locus m a y be required for regulating o r establishing a n Hms' phenotype (Lillrird rt al., 1997).…”

Section: Introductionmentioning

confidence: 99%

HmsT, a protein essential for expression of the haemin storage (Hms+) phenotype of Yersinia pestis

Jones¹,

Lillard²,

Perry³

1999

Microbiology

120

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The haemin storage (Hrns) phenotype of Yersinia pestis has been shown to be involved in the blockage of fleas that is required for the transmission of plague from fleas to mammals. Previously, an operon encoding four genes, hmsHFRS, that are essential for the temperature-regulated Hms+ phenotype has been characterized. Here the isolation and characterization of a fifth gene, hmsT, that is essential for this phenotype is described. Conceptual translation of hmsT suggests it encodes a 44.8 kDa protein with a pl of 7.75. The gene for

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“…This is required for colonization and eventual blockage of the flea proventriculus -allowing efficient transmission of plague from some fleas, like the oriental rat flea, to mammals (Bacot & Martin, 1914;Bacot, 1915;Hinnebusch et al, 1996;Lillard et al, 1997Lillard et al, , 1999Pendrak & Perry, 1991Perry et al, 1990Perry et al, , 1993Perry et al, , 2004Perry & Fetherston, 1997;Pollitzer, 1954). Biofilm formation is not involved in mammalian virulence -an in-frame deletion in hmsR did not affect the LD 50 in a bubonic plague model .…”

Section: Introductionmentioning

confidence: 99%

Identification of critical amino acid residues in the plague biofilm Hms proteins

et al. 2006

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Yersinia pestis biofilm formation causes massive adsorption of haemin or Congo red in vitro as well as colonization and eventual blockage of the flea proventriculus in vivo. This blockage allows effective transmission of plague from some fleas, like the oriental rat flea, to mammals. Four Hms proteins, HmsH, HmsF, HmsR and HmsS, are essential for biofilm formation, with HmsT and HmsP acting as positive and negative regulators, respectively. HmsH has a β-barrel structure with a large periplasmic domain while HmsF possesses polysaccharide deacetylase and COG1649 domains. HmsR is a putative glycosyltransferase while HmsS has no recognized domains. In this study, specific amino acids within conserved domains or within regions of high similarity in HmsH, HmsF, HmsR and HmsS proteins were selected for site-directed mutagenesis. Some but not all of the substitutions in HmsS and within the periplasmic domain of HmsH were critical for protein function. Substitutions within the glycosyltransferase domain of HmsR and the deacetylase domain of HmsF abolished biofilm formation in Y. pestis. Surprisingly, substitution of highly conserved residues within COG1649 did not affect HmsF function.

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Identification and cloning of a hemin storage locus involved in the pigmentation phenotype of Yersinia pestis

Abstract: The temperature-dependent absorption of sufficient exogenous hemin or Congo red to form pigmented colonies of Yersinia pestis has been termed the pigmentation phenotype (Pgm+). Spontaneous

Cited by 169 publications

References 45 publications

Analysis of the aerobactin and ferric hydroxamate uptake systems of Yersinia pestis

Analysis of the aerobactin and ferric hydroxamate uptake systems of Yersinia pestis

HmsT, a protein essential for expression of the haemin storage (Hms+) phenotype of Yersinia pestis

Identification of critical amino acid residues in the plague biofilm Hms proteins

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