Foot-and-mouth disease virus leader proteinase Purification of the Lb form and determination of its cleavage site on eIF-4γ
| Autor: | Kirchweger, R., Ziegler, E., Lamphear, B. J., Waters, D., Liebig -, H. D., Sommergruber, W., Francisco Sobrino, Hohenadl, C., Blaas, D., Rhoads, R. E., Skern, T. |
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| Jazyk: | angličtina |
| Rok vydání: | 1994 |
| Předmět: | |
| Zdroj: | Repositorio de Resultados de Investigación del INIA INIA: Repositorio de Resultados de Investigación del INIA Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria INIA Scopus-Elsevier |
| Popis: | Many picornaviruses cause a dramatic decrease in the translation of cellular mRNAs in the infected cell, without affecting the translation of their own RNA. Specific proteolysis of protein synthesis initiation factor eIF-4γ occurs during infection with rhinoviruses, enteroviruses, and aphthoviruses, apparently leading to an inability of the ribosomes to bind capped mRNAs. Cleavage of eIF-4γ in human rhinoviruses and enteroviruses is carried out by the viral 2A proteinase; in aphthoviruses (i.e.;foot-and- mouth disease viruses), the leader proteinase is responsible for this reaction. We describe here the purification to homogeneity of the Lb form of the leader proteinase expressed in Escherichia coli. The primary cleavage products of eIF-4γ obtained in vitro with purified leader or 2A proteinase are electrophoretically indistinguishable from those found during infection in vivo. However, additional proteolysis products of eIF-4γ are observed with the leader proteinase and the human rhinovirus type 2 2A proteinase in vitro. The cleavage site of the leader proteinase in eIF-4γ from rabbit reticulocyte was determined by sequencing the purified C-terminal cleavage product by automated Edman degradation. The cleavage site is between Gly-479 and Arg-480 and thus differs from that of rhinovirus and enterovirus 2A proteinases, which cleave between Arg-486 and Gly-487. |
| Databáze: | OpenAIRE |
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