An aroA mutant of Yersinia pestis is attenuated in guinea-pigs, but virulent in mice

Article Abstract:

The Yersinia pestis GB-delta-aroA mutant strain is avirulent in guinea pigs but virulent in BALB/c mice. The mutant strain contains a deletion mutation in the aroA gene and is cleared from the reticulo-endothelial system of the guinea pigs. The immune reponse of the guniea pigs against the mutants protects them against virulent strains of Y. pestis. The mice take longer to die than those infected with the wild-type bacteria. This is due to a slower growth of the mutant in the mice. There is a degree of amino acid sequence similarity between aroA gene of Y. pestis and other species.

Analysis, Physiological aspects, Gene mutations, Gene mutation, Laboratory animals, Virulence (Microbiology), Mice as laboratory animals, House mouse, Guinea pigs as laboratory animals, Guinea pigs, Yersinia pestis

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Phosphorylation and association with the transcription factor Atf1 regulate localization of Spc1/Sty1 stress-activated kinase in fission yeast

Article Abstract:

Subcellular localization studies suggest that nuclear localization of Spc1, a stress-activated protein kinase in fission yeast, requires phosphorylation by Wis1 as well as association with the transcription factor Atf1. Transient nuclear localization of Spc1 occurs under stress, as Spc1 becomes disassociated from Wis1, its activator kinase, which is located in the cytoplasm. However, forms of Spc1 that cannot be phosphorylated become dispersed throughout the cytoplasm and nucleus rather than localized.

Cellular signal transduction, Yeast, Yeast (Food product), Protein kinases, Phosphorylation

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Yersinia pseudotuberculosis and yersinia pestis are more resistant to bactericidal cationic peptides than Yersinia enterocolitica

Article Abstract:

A study was conducted to test whether the live cells of Yersinia pseudotuberculosis and Y. pestis are more resistant to polycations than those of Y. enterocolitica. Dansylcadaverine was utilized to evaluate lipopolysaccharide-polycation affinity while permeability changes were determined by lysozyme and novobiocin. Results indicated that species and temperature differences associated with polycation resistance correlate with the invasiveness and intracellular multiplication of Y. spp.

Peptides, Yersinia infections, Cations

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