INVITRO GUANYLYLATION OF INFECTIOUS PANCREATIC NECROSIS VIRUS POLYPEPTIDE VP1

被引:42
作者
DOBOS, P
机构
[1] Department of Microbiology, College of Biological Sciences, University of Guelph, Guelph
基金
加拿大自然科学与工程研究理事会;
关键词
D O I
10.1006/viro.1993.1137
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Incubation of purified infectious pancreatic necrosis virus (IPNV) in the presence of [α32P]GTP resulted in the formation of VP1-GMP. The GMP is linked to VP1 by a phosphodiester bond and its formation does not require the presence of divalent cations. In contrast to reovirus guanylyl transferase, the formation of IPNV VP1-GMP is not reversible and the guanylylation reaction is not inhibited by inorganic pyrophosphate. Furthermore, the IPNV VP1-GMP cannot transfer the GMP to an acceptor molecule (such as GTP) indicating that VP1 is not a capping enzyme. Time-course experiments revealed that after the initial guanylylation of VP1 to form VP1-pG, a second GMP is added to form VP1-pGpG, the formation of which is template-dependent. Since VP1 is present in the virion both as a free polypeptide and in a genome-linked form as VPg, and it is also the virion-associated RNA polymerase, the results suggest that VP1 may function as a primer during in vitro RNA synthesis. © 1993 Academic Press Inc.
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页码:403 / 413
页数:11
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