Sequence of reovirus haemagglutinin predicts a coiled-coil structure View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1985-05

AUTHORS

Rhonda Bassel-Duby, Anula Jayasuriya, Devjani Chatterjee, Nahum Sonenberg, Jacob V. Maizel, Bernard N. Fields

ABSTRACT

The use of modern techniques has led to new insights into the molecular mechanisms of viral pathogenesis1. Although the infectious process is quite complex, it is clear that one critical stage, the interaction of viral attachment proteins with cell-surface receptors, often has a major role in determining the pattern of infection2. The mammalian reoviruses have served as useful models for understanding the molecular basis of viral pathogenesis2. The mammalian reovirus haemagglutinin (σ1 protein), which is an outer capsid protein, has been shown to be a major factor in determining virus–host cell interactions2. To further our understanding of the structure and function of the haemagglutinin, we have cloned a complementary DNA copy of the reovirus type 3 S1 double-stranded RNA gene which encodes the virus haemagglutinin and have sequenced the DNA complementary to the S1 gene. Analysis of the predicted amino-acid sequence of the virus haemagglutinin has allowed us to determine that the amino-terminal portion contains an α-helical coiled-coil structure and that the carboxy-terminal portion contains the receptor-interacting domains. Using this information, we propose here a model of how the reovirus haemagglutinin is attached to the virus particle. More... »

PAGES

421-423

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/315421a0

DOI

http://dx.doi.org/10.1038/315421a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1027001729

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/4000269


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