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Toxins 2010, 2(4), 905-918; doi:10.3390/toxins2040905
Review

AIP56: A Novel Bacterial Apoptogenic Toxin

,
 and
*
IBMC-Instituto de Biologia Molecular e Celular, Rua do Campo Alegre, 823. 4150-180 Porto, Portugal
* Author to whom correspondence should be addressed.
Received: 31 March 2010 / Revised: 16 April 2010 / Accepted: 22 April 2010 / Published: 26 April 2010
(This article belongs to the Special Issue Toxins from Aquatic Organisms)
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Abstract

Photobacterium damselae subsp. piscicida (Phdp) is a Gram-negative pathogen agent of an important fish septicemia. The key virulence factor of Phdp is the plasmid-encoded exotoxin AIP56, which is secreted by exponentially growing pathogenic strains. AIP56 has 520 amino acids including an N-terminal cleavable signal peptide of 23 amino acid residues, two cysteine residues and a zinc-binding region signature HEXXH that is typical of most zinc metallopeptidases. AIP56 induces in vitro and in vivo selective apoptosis of fish macrophages and neutrophils through a caspase-3 dependent mechanism that also involves caspase-8 and -9. In vivo, the AIP56-induced phagocyte apoptosis progresses to secondary necrosis with release of cytotoxic phagocyte molecules including neutrophil elastase. Fish injected with recombinant AIP56 die with a pathology similar to that seen in the natural infection.
Keywords: Photobacterium damselae subsp. piscicida; AIP56; AB toxin; apoptosis; secondary necrosis Photobacterium damselae subsp. piscicida; AIP56; AB toxin; apoptosis; secondary necrosis
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Silva, M.T.; Dos Santos, N.M.S.; Do Vale, A. AIP56: A Novel Bacterial Apoptogenic Toxin. Toxins 2010, 2, 905-918.

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