Literature DB >> 18305051

Residue L143 of the foot-and-mouth disease virus leader proteinase is a determinant of cleavage specificity.

Christina Mayer1, David Neubauer, Aloysius T Nchinda, Regina Cencic, Katja Trompf, Tim Skern.   

Abstract

The foot-and-mouth disease virus (FMDV) leader proteinase (L(pro)) self-processes inefficiently at the L(pro)/VP4 cleavage site LysLeuLys*GlyAlaGly (* indicates cleaved peptide bond) when the leucine at position P2 is replaced by phenylalanine. Molecular modeling and energy minimization identified the L(pro) residue L143 as being responsible for this discrimination. The variant L(pro) L143A self-processed efficiently at the L(pro)/VP4 cleavage site containing P2 phenylalanine, whereas the L143M variant did not. L(pro) L143A self-processing at the eIF4GII sequence AspPheGly*ArgGlnThr was improved but showed more-extensive aberrant processing. Residue 143 in L(pro) is occupied only by leucine and methionine in all sequenced FMDV serotypes, implying that these bulky side chains are one determinant of the restricted specificity of L(pro).

Entities:  

Mesh：

Substances：

Year:  2008        PMID： 18305051      PMCID： PMC2293068          DOI： 10.1128/JVI.02077-07

Source DB:  PubMed          Journal:  J Virol        ISSN： 0022-538X            Impact factor:   5.103


  16 in total

1.  Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro.

Authors:  W Glaser; T Skern
Journal:  FEBS Lett       Date:  2000-09-01       Impact factor: 4.124

Review 2.  Global epidemiology and prospects for control of foot-and-mouth disease.

Authors:  R P Kitching
Journal:  Curr Top Microbiol Immunol       Date:  2005       Impact factor: 4.291

3.  Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for self-processing and eIF4G recognition.

Authors:  A Guarné; J Tormo; R Kirchweger; D Pfistermueller; I Fita; T Skern
Journal:  EMBO J       Date:  1998-12-15       Impact factor: 11.598

Review 4.  Revised definition of substrate binding sites of papain-like cysteine proteases.

Authors:  D Turk; G Guncar; M Podobnik; B Turk
Journal:  Biol Chem       Date:  1998-02       Impact factor: 3.915

5.  All foot and mouth disease virus serotypes initiate protein synthesis at two separate AUGs.

Authors:  D V Sangar; S E Newton; D J Rowlands; B E Clarke
Journal:  Nucleic Acids Res       Date:  1987-04-24       Impact factor: 16.971

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

Authors:  M Medina; E Domingo; J K Brangwyn; G J Belsham
Journal:  Virology       Date:  1993-05       Impact factor: 3.616

7.  Foot-and-mouth disease virus leader proteinase: purification of the Lb form and determination of its cleavage site on eIF-4 gamma.

Authors:  R Kirchweger; E Ziegler; B J Lamphear; D Waters; H D Liebig; W Sommergruber; F Sobrino; C Hohenadl; D Blaas; R E Rhoads
Journal:  J Virol       Date:  1994-09       Impact factor: 5.103

8.  Functional analysis of the two alternative translation initiation sites of foot-and-mouth disease virus.

Authors:  X Cao; I E Bergmann; R Füllkrug; E Beck
Journal:  J Virol       Date:  1995-01       Impact factor: 5.103

9.  Comparative genomics of foot-and-mouth disease virus.

Authors:  C Carrillo; E R Tulman; G Delhon; Z Lu; A Carreno; A Vagnozzi; G F Kutish; D L Rock
Journal:  J Virol       Date:  2005-05       Impact factor: 5.103

10.  Foot-and-mouth disease virus leader proteinase: specificity at the P2 and P3 positions and comparison with other papain-like enzymes.

Authors:  Elisabeth Kuehnel; Regina Cencic; Nicole Foeger; Tim Skern
Journal:  Biochemistry       Date:  2004-09-14       Impact factor: 3.162
View more
  7 in total

1.  A conserved domain in the leader proteinase of foot-and-mouth disease virus is required for proper subcellular localization and function.

Authors:  Teresa de los Santos; Fayna Diaz-San Segundo; James Zhu; Marla Koster; Camila C A Dias; Marvin J Grubman
Journal:  J Virol       Date:  2008-12-03       Impact factor: 5.103

2.  Gemin5 proteolysis reveals a novel motif to identify L protease targets.

Authors:  David Piñeiro; Jorge Ramajo; Shelton S Bradrick; Encarnación Martínez-Salas
Journal:  Nucleic Acids Res       Date:  2012-02-22       Impact factor: 16.971

3.  Genomic Changes in an Attenuated ZB Strain of Foot-and-Mouth Disease Virus Serotype Asia1 and Comparison with Its Virulent Parental Strain.

Authors:  Aiguo Xin; Mingwang Zhu; Zhenqi Peng; Qi Hu; Chenhong Shi; Defang Liao; Jihua Wang; Huachun Li
Journal:  Int J Genomics       Date:  2014-10-19       Impact factor: 2.326

4.  Dissecting distinct proteolytic activities of FMDV Lpro implicates cleavage and degradation of RLR signaling proteins, not its deISGylase/DUB activity, in type I interferon suppression.

Authors:  Linda J Visser; Chiara Aloise; Kirby N Swatek; Gisselle N Medina; Karin M Olek; Huib H Rabouw; Raoul J de Groot; Martijn A Langereis; Teresa de Los Santos; David Komander; Tim Skern; Frank J M van Kuppeveld
Journal:  PLoS Pathog       Date:  2020-07-15       Impact factor: 6.823

Review 5.  Uncovering targets of the Leader protease: Linking RNA-mediated pathways and antiviral defense.

Authors:  Margarita Saiz; Encarnacion Martinez-Salas
Journal:  Wiley Interdiscip Rev RNA       Date:  2021-02-18       Impact factor: 9.957

6.  Comparison of self-processing of foot-and-mouth disease virus leader proteinase and porcine reproductive and respiratory syndrome virus leader proteinase nsp1α.

Authors:  Jutta Steinberger; Georg Kontaxis; Chiara Rancan; Tim Skern
Journal:  Virology       Date:  2013-06-04       Impact factor: 3.616

7.  Foot-and-mouth disease virus leader proteinase: structural insights into the mechanism of intermolecular cleavage.

Authors:  Jutta Steinberger; Irina Grishkovskaya; Regina Cencic; Luiz Juliano; Maria A Juliano; Tim Skern
Journal:  Virology       Date:  2014-09-19       Impact factor: 3.616
  7 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.