Recent studies have led to new insights regarding the molecular mechanisms of viral pathogenesis. Although the infectious process is quite complex, it is clear that one critical event, the interaction of viral attachment proteins with cell surface receptors, plays 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 hemagglutinin ((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 hemagglutinin, we have cloned a cDNA copy of the reovirus type 3 Sl double-stranded RNA gene that encodes the viral hemagglutinin and sequenced the DNA complementary to the Sl gene. Analysis of the predicted amino acid sequence of the viral hemagglutinin 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. With this information we have designed a model that shows how the reovirus hemagglutinin is attached to the viral particle.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.71980 |
| Date | January 1985 |
| Creators | Bassel-Duby, Rhonda Susan |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Doctor of Philosophy (Department of Biochemistry.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 000213708, proquestno: AAINL20841, Theses scanned by UMI/ProQuest. |
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