To localize the epitopes recognized by monoclonal antibodies (MAbs) specific for the Si subunit of the murine coronavirus JHMV spike protein, we have expressed S1 proteins with different deletions from the C terminus of SI. Slutt is composed of the entire 769-amino-acid (aa) Si protein; S1NM, SIN, SlN(330), and SlN(220) are deletion mutants with 594, 453, 330, and 220 aa from the N terminus of the Si protein. The expressed Si deletion mutant proteins were examined for reactivities to a panel of MAbs. All MAbs classified in groups A and B, those reactive to most mouse hepatitis virus (MHV) strains and those specific for isolate JHMV, respectively, recognized SIN(330) and the larger Si deletion mutants but failed to react with SlN(220). MAbs in group C, specific for the larger S protein of JHMV, reacted only with the Slutt protein without any deletion. These results indicated that the domain composed of the N-terminal 330 aa comprised the cluster of conformational epitopes recognized by MAbs in groups A and B. It was also shown that the epitopes of MAbs in group C were not restricted to the region missing in the smaller S protein. These results together with the fact that all MAbs in group B retained high neutralizing activity suggested the possibility that the N-terminal 330 aa are responsible for binding to the MHV-specific receptors. In investigate this possibility, we expressed
Enterovirus 68 strains were detected in 14 specimens from children with respiratory tract infections and 1 specimen from a child with febrile convulsions during 2010 in Osaka, Japan. These strains had deletions in the 5′ untranslated region and were genetically different from reported strains. This virus is associated with respiratory tract infections in Japan.
Rotavirus A (RVA) genotype G1P[8], a hallmark of the Wa-like strain, typically contains only genotype 1 genes. However, an unusual RVA G1P[8] with genotype 2 genes was recently detected in Japan. We determined the complete genomic constellation of this RVA. Our findings suggest that mixed RVAs may be more competitive than once thought.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.