The amino terminus of the salmonid alphavirus capsid protein determines subcellular localization and inhibits cellular proliferation

Salmonid alphavirus (SAV) is the most divergent member of the family Togaviridae and constitutes a threat to farming of salmonid fish in Europe. Here, we report cloning, expression and preliminary functional analysis of the capsid protein of SAV, confirming it to be expressed as an approximately 31-kDa protein in infected cells. The protein localizes strictly to the cytoplasm in Chinook salmon embryo cells, and either to the nucleus or cytoplasm in bluegill fry cells. An expression study of full-length and different truncated versions of the SAV capsid fused to the enhanced green fluorescent protein demonstrated that the localization is independent of other viral components in both cell lines, and controlled by the N-terminal 82 aa, which include a conserved, predicted helix and a downstream positively charged region. Thus, the results suggest that the SAV capsid possesses a cell-type-dependent potential for nuclear import and export. Moreover, the SAV capsid and its N-terminal 82 aa were shown to be associated with inhibition of cellular proliferation, a hallmark of the cytopathic effect caused by SAV. These results highlight that the SAV capsid is a multifunctional protein with possible importance for pathogenesis.     

Effect of sensory training of the posterior thigh on trunk control and upper extremity functions in stroke patients

Neurological Sciences - Some studies show that sensorial rehabilitation is effective on functionality. The aim of this study is to investigate the effect of sensory training of the posterior thigh...     

In Vitro Susceptibility of Mycobacterium tuberculosis to Trimethoprim and Sulfonamides in France

Five type strains and 55 Mycobacterium tuberculosis complex clinical isolates were found resistant to trimethoprim with a MIC of >200 mg/liter and susceptible to both sulfadiazine and cotrimoxazole with a MIC₉₀ of 10 mg/liter. Two M. canettii isolates uniquely yielded silent mutations C₁₅₆ → T and G₂₃₈ → C in the folP1 gene. Combined with scarce published data, these data indicate that sulfamides could be considered alternative antituberculous antibiotics.