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Rotaviruses code for two types of glycoprotein precursors
Journal of Cellular Biochemistry
|January 1, 1983
Summary
This study details how rotaviruses synthesize glycoproteins. The research clarifies the processing of viral glycoproteins, offering insights into rotavirus SA11 morphogenesis.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Rotaviruses are nonenveloped viruses encoding two key glycoproteins: VP7 and NS29.
- Understanding glycoprotein synthesis is crucial for viral replication and morphogenesis.
Purpose of the Study:
- To investigate the synthesis and processing of rotavirus glycoproteins, VP7 and NS29.
- To elucidate the role of signal sequences in membrane insertion and glycosylation.
Main Methods:
- Cell-free synthesis of rotavirus glycoprotein precursors (37K for VP7, 20K for NS29).
- Utilized dog pancreatic microsomes for studying signal sequence cleavage and glycosylation.
- Analyzed cotranslational membrane insertion and posttranslational oligosaccharide processing.
Main Results:
- The VP7 precursor (37K) possesses a cleavable signal sequence, enabling authentic processing via signal sequence cleavage and core glycosylation.
- The NS29 precursor (20K) contains a non-cleavable, integral signal sequence.
- Both precursors were cotranslationally inserted into membranes, and their glycosylated products underwent posttranslational oligosaccharide modification.
Conclusions:
- The findings provide a detailed morphogenetic scheme for simian rotavirus SA11.
- Differential signal sequence processing dictates distinct pathways for rotavirus glycoprotein maturation.