Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6139095 | Virology | 2015 | 6 Pages |
Abstract
Enteroviruses (EV) uridylylate a peptide, VPg, as the first step in their replication. VPgpUpU, found free in infected cells, serves as the primer for RNA elongation. The abilities of four polymerases (3Dpol), from EV-species A-C, to uridylylate VPgs that varied by up to 60% of their residues were compared. Each 3Dpol was able to uridylylate all five VPgs using polyA RNA as template, while showing specificity for its own genome encoded peptide. All 3Dpol uridylylated a consensus VPg representing the physical chemical properties of 31 different VPgs. Thus the residues required for uridylylation and the enzymatic mechanism must be similar in diverse EV. As VPg-binding sites differ in co-crystal structures, the reaction is probably done by a second 3Dpol molecule. The conservation of polymerase residues whose mutation reduces uridylylation but not RNA elongation is compared.
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Immunology and Microbiology
Virology
Authors
Catherine H. Schein, Mengyi Ye, Aniko V. Paul, M. Steven Oberste, Nora Chapman, Gerbrand J. van der Heden van Noort, Dmitri V. Filippov, Kyung H. Choi,