Identification of critical amino acids within the foot-and-mouth disease virus Leader protein, a cysteine protease

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Standard

Identification of critical amino acids within the foot-and-mouth disease virus Leader protein, a cysteine protease. / Roberts, Peter J.; Belsham, Graham J.

I: Virology, Bind 213, Nr. 1, 71554, 20.10.1995, s. 140-146.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Roberts, PJ & Belsham, GJ 1995, 'Identification of critical amino acids within the foot-and-mouth disease virus Leader protein, a cysteine protease', Virology, bind 213, nr. 1, 71554, s. 140-146. https://doi.org/10.1006/viro.1995.1554

APA

Roberts, P. J., & Belsham, G. J. (1995). Identification of critical amino acids within the foot-and-mouth disease virus Leader protein, a cysteine protease. Virology, 213(1), 140-146. [71554]. https://doi.org/10.1006/viro.1995.1554

Vancouver

Roberts PJ, Belsham GJ. Identification of critical amino acids within the foot-and-mouth disease virus Leader protein, a cysteine protease. Virology. 1995 okt. 20;213(1):140-146. 71554. https://doi.org/10.1006/viro.1995.1554

Author

Roberts, Peter J. ; Belsham, Graham J. / Identification of critical amino acids within the foot-and-mouth disease virus Leader protein, a cysteine protease. I: Virology. 1995 ; Bind 213, Nr. 1. s. 140-146.

Bibtex

@article{52d90813584f48869b4628ec629591cf,
title = "Identification of critical amino acids within the foot-and-mouth disease virus Leader protein, a cysteine protease",
abstract = "The Leader protein of foot-and-mouth disease virus (FMDV) is the first component of the virus polyprotein. It is synthesized in two forms, Lab and Lb, both of which display the ability to cleave the L/P1 junction in trans and to induce the cleavage of the cap-binding complex component eIF-4G (p220). The L protease has weak homology to the family of cysteine proteases, which have a catalytic dyad composed of a cysteine and a histidine. Mutations have been introduced into FMDV cDNA to modify each of the four cysteine residues and the three conserved histidine residues within the Lb species. The activities of the mutant L proteins have been determined. Modification of a single cysteine residue (residue 51) or of a single histidine residue (residue 148) abolished the abilities of L to cleave the L/P1 junction and to inhibit cap-dependent protein synthesis. In contrast, modification of each of the other cysteine residues and other conserved histidine residues had no apparent effect on these activities.",
author = "Roberts, {Peter J.} and Belsham, {Graham J.}",
year = "1995",
month = oct,
day = "20",
doi = "10.1006/viro.1995.1554",
language = "English",
volume = "213",
pages = "140--146",
journal = "Virology",
issn = "0042-6822",
publisher = "Academic Press",
number = "1",

}

RIS

TY - JOUR

T1 - Identification of critical amino acids within the foot-and-mouth disease virus Leader protein, a cysteine protease

AU - Roberts, Peter J.

AU - Belsham, Graham J.

PY - 1995/10/20

Y1 - 1995/10/20

N2 - The Leader protein of foot-and-mouth disease virus (FMDV) is the first component of the virus polyprotein. It is synthesized in two forms, Lab and Lb, both of which display the ability to cleave the L/P1 junction in trans and to induce the cleavage of the cap-binding complex component eIF-4G (p220). The L protease has weak homology to the family of cysteine proteases, which have a catalytic dyad composed of a cysteine and a histidine. Mutations have been introduced into FMDV cDNA to modify each of the four cysteine residues and the three conserved histidine residues within the Lb species. The activities of the mutant L proteins have been determined. Modification of a single cysteine residue (residue 51) or of a single histidine residue (residue 148) abolished the abilities of L to cleave the L/P1 junction and to inhibit cap-dependent protein synthesis. In contrast, modification of each of the other cysteine residues and other conserved histidine residues had no apparent effect on these activities.

AB - The Leader protein of foot-and-mouth disease virus (FMDV) is the first component of the virus polyprotein. It is synthesized in two forms, Lab and Lb, both of which display the ability to cleave the L/P1 junction in trans and to induce the cleavage of the cap-binding complex component eIF-4G (p220). The L protease has weak homology to the family of cysteine proteases, which have a catalytic dyad composed of a cysteine and a histidine. Mutations have been introduced into FMDV cDNA to modify each of the four cysteine residues and the three conserved histidine residues within the Lb species. The activities of the mutant L proteins have been determined. Modification of a single cysteine residue (residue 51) or of a single histidine residue (residue 148) abolished the abilities of L to cleave the L/P1 junction and to inhibit cap-dependent protein synthesis. In contrast, modification of each of the other cysteine residues and other conserved histidine residues had no apparent effect on these activities.

UR - http://www.scopus.com/inward/record.url?scp=0028884251&partnerID=8YFLogxK

U2 - 10.1006/viro.1995.1554

DO - 10.1006/viro.1995.1554

M3 - Journal article

AN - SCOPUS:0028884251

VL - 213

SP - 140

EP - 146

JO - Virology

JF - Virology

SN - 0042-6822

IS - 1

M1 - 71554

ER -

ID: 379029435