Cold shock exoribonuclease R (VacB) is involved in Aeromonas hydrophila pathogenesis

Tatiana E. Erova, Valeri G. Kosykh, Amin A. Fadl, Jian Sha, Amy J. Horneman, Ashok Chopra

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Abstract

In this study, we cloned and sequenced a virulence-associated gene (vacB) from a clinical isolate SSU of Aeromonas hydrophila. We identified this gene based on our recently annotated genome sequence of the environmental isolate ATCC 7966T of A hydrophila and the vacB gene of Shigella flexneri. The A. hydrophila VacB protein contained 798 amino acid residues, had a molecular mass of 90.5 kDa, and exhibited an exoribonuclease (RNase R) activity. The RNase R of A. hydrophila was a cold-shock protein and was required for bacterial growth at low temperature. The vacB isogenic mutant, which we developed by homologous recombination using marker exchange mutagenesis, was unable to grow at 4°C. In contrast, the wild-type (WT) A. hydrophila exhibited significant growth at this low temperature. Importantly, the vacB mutant was not defective in growth at 37°. The vacB mutant also exhibited reduced motility, and these growth and motility phenotype defects were restored after complementation of the vacB mutant. The A. hydrophila RNase R-lacking strain was found to be less virulent in a mouse lethality model (70% survival) when given by the intraperitoneal route at as two 50% lethal doses (LD 50). On the other hand, the WT and complemented strains of A. hydrophila caused 80 to 90% of the mice to succumb to infection at the same LD50 dose. Overall, this is the first report demonstrating the role of RNase R in modulating the expression of A. hydrophila virulence.

Original languageEnglish (US)
Pages (from-to)3467-3474
Number of pages8
JournalJournal of Bacteriology
Volume190
Issue number10
DOIs
StatePublished - May 2008

Fingerprint

Exoribonucleases
Aeromonas hydrophila
Shock
Lethal Dose 50
Growth
Virulence
Cold Shock Proteins and Peptides
Genes
Shigella flexneri
Temperature
Homologous Recombination
Mutagenesis
Genome
Phenotype
Amino Acids
ribonuclease R

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Cold shock exoribonuclease R (VacB) is involved in Aeromonas hydrophila pathogenesis. / Erova, Tatiana E.; Kosykh, Valeri G.; Fadl, Amin A.; Sha, Jian; Horneman, Amy J.; Chopra, Ashok.

In: Journal of Bacteriology, Vol. 190, No. 10, 05.2008, p. 3467-3474.

Research output: Contribution to journalArticle

Erova, Tatiana E. ; Kosykh, Valeri G. ; Fadl, Amin A. ; Sha, Jian ; Horneman, Amy J. ; Chopra, Ashok. / Cold shock exoribonuclease R (VacB) is involved in Aeromonas hydrophila pathogenesis. In: Journal of Bacteriology. 2008 ; Vol. 190, No. 10. pp. 3467-3474.
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abstract = "In this study, we cloned and sequenced a virulence-associated gene (vacB) from a clinical isolate SSU of Aeromonas hydrophila. We identified this gene based on our recently annotated genome sequence of the environmental isolate ATCC 7966T of A hydrophila and the vacB gene of Shigella flexneri. The A. hydrophila VacB protein contained 798 amino acid residues, had a molecular mass of 90.5 kDa, and exhibited an exoribonuclease (RNase R) activity. The RNase R of A. hydrophila was a cold-shock protein and was required for bacterial growth at low temperature. The vacB isogenic mutant, which we developed by homologous recombination using marker exchange mutagenesis, was unable to grow at 4°C. In contrast, the wild-type (WT) A. hydrophila exhibited significant growth at this low temperature. Importantly, the vacB mutant was not defective in growth at 37°. The vacB mutant also exhibited reduced motility, and these growth and motility phenotype defects were restored after complementation of the vacB mutant. The A. hydrophila RNase R-lacking strain was found to be less virulent in a mouse lethality model (70{\%} survival) when given by the intraperitoneal route at as two 50{\%} lethal doses (LD 50). On the other hand, the WT and complemented strains of A. hydrophila caused 80 to 90{\%} of the mice to succumb to infection at the same LD50 dose. Overall, this is the first report demonstrating the role of RNase R in modulating the expression of A. hydrophila virulence.",
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