RESUMO
The COVID-19 pandemic has spread rapidly around the world; some countries have introduced controls on imported products, including testing for viral nucleic acids. In this work, the influence of disinfectants for treating various SARS-CoV-2-contaminated surfaces on the detection of viral RNA fragments in swabs from these surfaces was analyzed using quantitative RT-PCR. Quaternary ammonium salt, hydrogen peroxide, 1-propanol, and sodium salt of dichloroisocyanuric acid, as well as ultraviolet irradiation, were tested as such disinfecting agents. Our results show that without exposure to disinfectants, viral RNA can be detected on the surface of all examined materials for at least 3 days. UV irradiation or irrigation with a disinfectant containing 0.2% active chlorine had the greatest effect on the decontamination of nonporous surfaces as measured by RT-PCR of swabs from these surfaces. Irrigation with disinfectants of porous surfaces (cardboard) had practically no effect on the detection of SARS-CoV-2 RNA by RT-PCR.
RESUMO
Plant virus-encoded movement proteins (MPs) interact with endoplasmic reticulum (ER) membranes, the cytoskeleton, and plasmodesmata (PD) to mediate intracellular delivery of the virus genome to PD and its further transport through PD from infected to healthy cells. The Hibiscus green spot virus MP termed BMB2 has been shown to induce constrictions of ER tubules and to occur at highly curved membranes, thus showing properties similar to those of reticulons, a class of cellular proteins inducing membrane curvature and shaping the ER tubules. Consistent with this BMB2 function, mRFP-BMB2 localizes to discrete, constricted regions scattered along the ER tubules. Here, using BMB2-mRFP fusion protein as a BMB2 derivative with partially disabled functionality, we demonstrate that the focal localization of BMB2 to discrete sites along the ER tubules is insufficient to induce local tubule constrictions at these sites, suggesting that the formation of ER tubule constrictions represents a specific BMB2 function and is not simply a mechanistic consequence of its localization to the ER. The presented data suggest that the formation of ER-residing BMB2-containing distinct small aggregates, or protein platforms, can be uncoupled from BMB2-induced ER tubule constrictions, whereas the anchoring of platforms at particular ER sites appears to be linked to the constriction of ER tubules at these sites.
Assuntos
Retículo Endoplasmático/metabolismo , Proteínas do Movimento Viral em Plantas/metabolismo , Vírus de Plantas/metabolismo , Plantas Geneticamente Modificadas , Proteínas Recombinantes de Fusão/metabolismo , Nicotiana/genética , Nicotiana/virologiaRESUMO
Members of the genus Tobamovirus represent one of the best-characterized groups of plant positive, single stranded RNA viruses. Previous studies have shown that genomes of some tobamoviruses contain not only genes coding for coat protein, movement protein, and the cistron coding for different domains of RNA-polymerase, but also a gene, named ORF6, coding for a poorly conserved small protein. The amino acid sequences of ORF6 proteins encoded by different tobamoviruses are highly divergent. The potential role of ORF6 proteins in replication of tobamoviruses still needs to be elucidated. In this study, using biochemical and immunological methods, we have shown that ORF6 peptide is accumulated after infection in case of two isolates of Tobacco mosaic virus strain U1 (TMV-U1 common and TMV-U1 isolate A15). Unlike virus particles accumulating in the cytoplasm, the product of the ORF6 gene is found mainly in nuclei, which correlates with previously published data about transient expression of ORF6 isolated from TMV-U1. Moreover, we present new data showing the presence of ORF6 genes in genomes of several tobamoviruses. For example, in the genomes of other members of the tobamovirus subgroup 1, including Rehmannia mosaic virus, Paprika mild mottle virus, Tobacco mild green mosaic virus, Tomato mosaic virus, Tomato mottle mosaic virus, and Nigerian tobacco latent virus, sequence comparisons revealed the existence of a similar open reading frame like ORF6 of TMV.