The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities. / Medina, Miguel; Domingo, Esteban; Brangwyn, Julia K.; Belsham, Graham J.

In: Virology, Vol. 194, No. 1, 05.1993, p. 355-359.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Medina, M, Domingo, E, Brangwyn, JK & Belsham, GJ 1993, 'The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities', Virology, vol. 194, no. 1, pp. 355-359. https://doi.org/10.1006/viro.1993.1267

APA

Medina, M., Domingo, E., Brangwyn, J. K., & Belsham, G. J. (1993). The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities. Virology, 194(1), 355-359. https://doi.org/10.1006/viro.1993.1267

Vancouver

Medina M, Domingo E, Brangwyn JK, Belsham GJ. The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities. Virology. 1993 May;194(1):355-359. https://doi.org/10.1006/viro.1993.1267

Author

Medina, Miguel ; Domingo, Esteban ; Brangwyn, Julia K. ; Belsham, Graham J. / The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities. In: Virology. 1993 ; Vol. 194, No. 1. pp. 355-359.

Bibtex

@article{21702f46b77a4898ac9a5e5c9f94fb62,
title = "The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities",
abstract = "Initiation of protein synthesis on the foot-and-mouth disease virus RNA occurs at two sites, thus, two forms of the leader protein, termed Lab and Lb, are produced. Plasmids have been constructed which encode these proteins either together or individually. Plasmids encoding the Lab protein alone express a modified form of this protein in which the second methionine residue, which corresponds to the first amino acid of Lb, is changed to an alternative residue. Four different mutant forms of the Lab sequence were made. Each of the plasmids was introduced into a mammalian cell transient expression system which allowed the determination of the known activities of the L proteins. It was shown that the Lb protein and each of the modified Lab proteins were capable of cleaving the L/P1 junction in trans. Furthermore, each of these proteins induced the cleavage of the p220 component of the cap-binding complex (elF-4F) producing inhibition of cap-dependent translation. These results indicate that the two species of L have the same functions.",
author = "Miguel Medina and Esteban Domingo and Brangwyn, {Julia K.} and Belsham, {Graham J.}",
year = "1993",
month = may,
doi = "10.1006/viro.1993.1267",
language = "English",
volume = "194",
pages = "355--359",
journal = "Virology",
issn = "0042-6822",
publisher = "Academic Press",
number = "1",

}

RIS

TY - JOUR

T1 - The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities

AU - Medina, Miguel

AU - Domingo, Esteban

AU - Brangwyn, Julia K.

AU - Belsham, Graham J.

PY - 1993/5

Y1 - 1993/5

N2 - Initiation of protein synthesis on the foot-and-mouth disease virus RNA occurs at two sites, thus, two forms of the leader protein, termed Lab and Lb, are produced. Plasmids have been constructed which encode these proteins either together or individually. Plasmids encoding the Lab protein alone express a modified form of this protein in which the second methionine residue, which corresponds to the first amino acid of Lb, is changed to an alternative residue. Four different mutant forms of the Lab sequence were made. Each of the plasmids was introduced into a mammalian cell transient expression system which allowed the determination of the known activities of the L proteins. It was shown that the Lb protein and each of the modified Lab proteins were capable of cleaving the L/P1 junction in trans. Furthermore, each of these proteins induced the cleavage of the p220 component of the cap-binding complex (elF-4F) producing inhibition of cap-dependent translation. These results indicate that the two species of L have the same functions.

AB - Initiation of protein synthesis on the foot-and-mouth disease virus RNA occurs at two sites, thus, two forms of the leader protein, termed Lab and Lb, are produced. Plasmids have been constructed which encode these proteins either together or individually. Plasmids encoding the Lab protein alone express a modified form of this protein in which the second methionine residue, which corresponds to the first amino acid of Lb, is changed to an alternative residue. Four different mutant forms of the Lab sequence were made. Each of the plasmids was introduced into a mammalian cell transient expression system which allowed the determination of the known activities of the L proteins. It was shown that the Lb protein and each of the modified Lab proteins were capable of cleaving the L/P1 junction in trans. Furthermore, each of these proteins induced the cleavage of the p220 component of the cap-binding complex (elF-4F) producing inhibition of cap-dependent translation. These results indicate that the two species of L have the same functions.

UR - http://www.scopus.com/inward/record.url?scp=0027275622&partnerID=8YFLogxK

U2 - 10.1006/viro.1993.1267

DO - 10.1006/viro.1993.1267

M3 - Journal article

C2 - 8386879

AN - SCOPUS:0027275622

VL - 194

SP - 355

EP - 359

JO - Virology

JF - Virology

SN - 0042-6822

IS - 1

ER -

ID: 381222604