Abstract
Hemagglutination (HA) by the mammalian reoviruses is mediated by interactions between the viral σ 1 protein and sialoglycoproteins on the erythrocyte surface. Three serotype 3 (T3) reovirus strains were identified that do not agglutinate either bovine or type O human erythrocytes (HA negative): T3 clone 43 (T3C43), T3 clone 44 (T3C44), and T3 clone 84 (T3C84). These three strains also showed a diminished capacity to bind the major erythrocyte sialoglycoprotein, glycophorin, in an enzyme-linked immunosorbent assay. To determine the molecular basis for these findings, we examined the deduced σ 1 amino acid sequences of the three HA-negative T3 strains and four HA-positive T3 strains. The limited number of sequence differences in the σ 1 proteins of these seven strains allowed us to identify single unique amino acid residues in each of the HA-negative strains (aspartate 198 in T3C43, leucine 204 in T3C44, and tryptophan 202 in T3C84) that cluster within a discrete region of the σ 1 tail. The identification of σ 1 residues important for HA and glycophorin binding suggests that tail-forming sequences are exposed on the virion surface, where they interact with carbohydrate residues on the surface of cells.
Original language | English (US) |
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Pages (from-to) | 5173-5176 |
Number of pages | 4 |
Journal | Journal of virology |
Volume | 64 |
Issue number | 10 |
State | Published - 1990 |
ASJC Scopus subject areas
- Microbiology
- Immunology
- Insect Science
- Virology