The Apoptogenic Toxin AIP56 Is a Metalloprotease A-B Toxin that Cleaves NF-kappa b P65

• Tipo: Artigo em Revista Científica Internacional
• Data: 2013

Autores

silva, ds (Autor) ICBAS; pereira, lmg (Autor) Outra; moreira, ar (Autor) Outra; ferreira-da-silva, f (Autor) Outra; brito, rm (Autor) Outra; faria, tq (Autor) Outra; zornetta, i (Autor) Outra; montecucco, c (Autor) Outra; oliveira, p (Autor) ICBAS; azevedo, je (Autor) ICBAS; pereira, pjb (Autor) Outra; macedo-ribeiro, s (Autor) Outra; do vale, a (Autor) Outra; dos santos, nms (Autor) Outra

Revista

Título: PLoS Pathogens

ISSN: 1553-7366

Editora: Public Library of Science

Indexação

ISI Web of Knowledge - 25 Citações

Scopus - 26 Citações

Classificação Científica

FOS: Ciências exactas e naturais

Outras Informações

ID Authenticus: P-006-EER

DOI: 10.1371/journal.ppat.1003128

Abstract (EN): AIP56 (apoptosis-inducing protein of 56 kDa) is a major virulence factor of Photobacterium damselae piscicida (Phdp), a Gram-negative pathogen that causes septicemic infections, which are among the most threatening diseases in mariculture. The toxin triggers apoptosis of host macrophages and neutrophils through a process that, in vivo, culminates with secondary necrosis of the apoptotic cells contributing to the necrotic lesions observed in the diseased animals. Here, we show that AIP56 is a NF-kappa B p65-cleaving zinc-metalloprotease whose catalytic activity is required for the apoptogenic effect. Most of the bacterial effectors known to target NF-kappa B are type III secreted effectors. In contrast, we demonstrate that AIP56 is an A-B toxin capable of acting at distance, without requiring contact of the bacteria with the target cell. We also show that the N-terminal domain cleaves NF-kappa B at the Cys(39)-Glu(40) peptide bond and that the C-terminal domain is involved in binding and internalization into the cytosol.

Idioma: Inglês

Tipo (Avaliação Docente): Científica