Sequence of reovirus haemagglutinin predicts a coiled-coil structure.
The use of modern techniques has led to new insights into the molecular mechanisms of viral pathogenesis. 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 infection. The mammalian reoviruses have served as useful models for understanding the molecular basis of viral pathogenesis. The mammalian reovirus haemagglutinin (sigma 1 protein), which is an outer capsid protein, has been shown to be a major factor in determining virus-host cell interactions. 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 alpha-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.
D000595:Amino Acid Sequence; D001483:Base Sequence; D005814:Genes, Viral; D006389:Hemagglutinins, Viral / Q000235:genetics; D011487:Protein Conformation; D012087:Reoviridae / Q000648:ultrastructure; D013329:Structure-Activity Relationship
D006389:Hemagglutinins, Viral