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Sapovirus Translation Requires an Interaction between VPg and the Cap Binding Protein eIF4E
Hosmillo, Myra,Chaudhry, Yasmin,Kim, Deok-Song,Goodfellow, Ian,Cho, Kyoung-Oh American Society for Microbiology 2014 Journal of virology Vol.88 No.21
<P>Sapoviruses of the <I>Caliciviridae</I> family of small RNA viruses are emerging pathogens that cause gastroenteritis in humans and animals. Molecular studies on human sapovirus have been hampered due to the lack of a cell culture system. In contrast, porcine sapovirus (PSaV) can be grown in cell culture, making it a suitable model for understanding the infectious cycle of sapoviruses and the related enteric caliciviruses. Caliciviruses are known to use a novel mechanism of protein synthesis that relies on the interaction of cellular translation initiation factors with the virus genome-encoded viral protein genome (VPg) protein, which is covalently linked to the 5′ end of the viral genome. Using PSaV as a representative member of the <I>Sapovirus</I> genus, we characterized the role of the viral VPg protein in sapovirus translation. As observed for other caliciviruses, the PSaV genome was found to be covalently linked to VPg, and this linkage was required for the translation and the infectivity of viral RNA. The PSaV VPg protein was associated with the 4F subunit of the eukaryotic translation initiation factor (eIF4F) complex in infected cells and bound directly to the eIF4E protein. As has been previously demonstrated for feline calicivirus, a member of the <I>Vesivirus</I> genus, PSaV translation required eIF4E and the interaction between eIF4E and eIF4G. Overall, our study provides new insights into the novel mechanism of sapovirus translation, suggesting that sapovirus VPg can hijack the cellular translation initiation mechanism by recruiting the eIF4F complex through a direct eIF4E interaction.</P><P><B>IMPORTANCE</B> Sapoviruses, which are members of the <I>Caliciviridae</I> family, are one of the causative agents of viral gastroenteritis in humans. However, human sapovirus remains noncultivable in cell culture, hampering the ability to characterize the virus infectious cycle. Here, we show that the VPg protein from porcine sapovirus, the only cultivatable sapovirus, is essential for viral translation and functions via a direct interaction with the cellular translation initiation factor eIF4E. This work provides new insights into the novel protein-primed mechanism of calicivirus VPg-dependent translation initiation.</P>
Shin, Bora,Kim, Byung-Yong,Cho, Eunji,Oh, Ki-Bong,Shin, Jongheon,Goodfellow, Michael,Oh, Dong-Chan American Chemical Society and American Society of 2016 Journal of natural products Vol.79 No.7
<P>A new secondary metabolite, actinomadurol (1), was isolated along with the known compound JBIR-65 (2) from a rare actinomycete, Actinomadura strain KC 191. The structure of 1 was established as a rare member of the bacterial C-19 norditerpenoid class by NMR data and ECD calculations. The absolute configuration of 2, which was previously reported without stereochemical analysis, was determined by using the modified Mosher's method and ECD calculations. Actinomadurol (1) exhibited potent antibacterial activity against pathogenic strains, such as Staphylococcus aureus, Kocuria rhizophila, and Proteus hauseri (MIC = 0.39-0.78 mu g/mL), whereas JBIR-65 (2) showed no antibacterial activity.</P>
Cellulomonas composti sp. nov., a cellulolytic bacterium isolated from cattle farm compost
Kang, Myung-Suk,Im, Wan-Taek,Jung, Hae-Min,Kim, Myung Kyum,Goodfellow, Michael,Kim, Kwang Kyu,Yang, Hee-Chan,An, Dong-Shan,Lee, Sung-Taik Microbiology Society 2007 International journal of systematic and evolutiona Vol.57 No.6
Porcine sapovirus replication is restricted by the type I interferon response in cell culture
Hosmillo, Myra,Sorgeloos, Fré,dé,ric,Hiraide, Rintaro,Lu, Jia,Goodfellow, Ian,Cho, Kyoung-Oh Society for General Microbiology 2015 The Journal of general virology Vol.96 No.1
<P><I>Porcine sapovirus</I> (PSaV) of the family <I>Caliciviridae</I>, is the only member of the genus <I>Sapovirus</I> with cell culture and reverse genetics systems. When combined with the piglet model, these approaches provide a system to understand the molecular basis of sapovirus pathogenesis. The replication of PSaV in cell culture is, however, restricted, displaying an absolute requirement for bile acids and producing lower levels of infectious virus than other caliciviruses. The effect of bile acids has previously been linked to a reduction in the signal transducer and activator of transcription (STAT1)-mediated signalling pathway. In the current study, we observed that even in the presence of bile acids, PSaV replication in cell culture was restricted by soluble factors produced from infected cells. This effect was at least partially due to secreted IFN because treatment of cells with recombinant porcine IFN-β resulted in significantly reduced viral replication. Moreover, IFN-mediated signalling pathways (IFN, STAT1 and the 2′,5′-oligoadenylate synthetase) were activated during PSaV infection. Characterization of PSaV growth in cell lines deficient in their ability to induce or respond to IFN showed a 100–150-fold increase in infectious virus production, indicating that the primary role of bile acids was not the inactivation of the innate immune response. Furthermore, the use of IFN-deficient cell lines enabled more efficient recovery of PSaV from cDNA constructs. Overall, the highly efficient cell culture and reverse genetics system established here for PSaV highlighted the key role of the innate immune response in the restriction of PSaV infection and should greatly facilitate further molecular studies on sapovirus host–cell interactions.</P>
Numerical Identification of a Streptomyces Strain Producing Thiol Protease Inhibitor
KIM, IN SEOP,KIM, HYOUNG TAE,WARD, ALAN C.,GOODFELLOW, MICHAEL,HAH, YUNG CHIL,LEE, KYE JOON 한국미생물 · 생명공학회 1992 Journal of microbiology and biotechnology Vol.2 No.3
Chemotaxonomic and numerical identification were carried out for an isolate of Streptomyces strain SMF13 producing thiol protease inhibitor. Fifty taxonomic unit characters were tested and the data were analyzed numerically using the TAXON program. The isolate SMF13 was identified to be a member of the cluster 5 of Streptomyces and best matched to Streptomyces omiyaensis which is a synonym of Streptomyces exfoliatus. Therefore, it was concluded that the isolate was identified to be a strain of Streptomyces exfoliatus.