Comparison of self-processing of foot-and-mouth disease virus leader proteinase and porcine reproductive and respiratory syndrome virus leader proteinase nsp1α.
Virology
; 443(2): 271-7, 2013 Sep 01.
Article
em En
| MEDLINE
| ID: mdl-23756127
ABSTRACT
The foot-and-mouth disease virus leader proteinase (Lb(pro)) cleaves itself off the nascent viral polyprotein. NMR studies on the monomeric variant Lb(pro) L200F provide structural evidence for intramolecular self-processing. (15)N-HSQC measurements of Lb(pro) L200F showed specifically shifted backbone signals in the active and substrate binding sites compared to the monomeric variant sLb(pro), lacking six C-terminal residues. This indicates transient intramolecular interactions between the C-terminal extension (CTE) of one molecule and its own active site. Contrastingly, the porcine reproductive and respiratory syndrome virus (PRRSV) leader proteinase nsp1α, with a papain-like fold like Lb(pro), stably binds its own CTE. Parts of the ß-sheet domains but none of the α-helical domains of Lb(pro) and nsp1α superimpose; consequently, the α-helical domain of nsp1α is oriented differently relative to its ß-sheet domain. This provides a large interaction surface for the CTE with the globular domain, stabilising the intramolecular complex. Consequently, self-processing inactivates nsp1α but not Lb(pro).
Palavras-chave
Active site; C-terminal extension; CTE; FMDV; Foot-and-mouth disease virus; Lb(pro); Leader proteinase; Non-structural protein; PRRSV; Papain-like cysteine proteinase; Polyprotein processing; Porcine reproductive and respiratory syndrome virus; Protein fold; Shortened leader proteinase (lacking 6 C-terminal amino acids); Substrate binding; Wildtype; nsp; sLb(pro); wt
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Endopeptidases
/
Proteínas não Estruturais Virais
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Vírus da Síndrome Respiratória e Reprodutiva Suína
/
Vírus da Febre Aftosa
Limite:
Animals
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article