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© Melanie Blokesch, EPFL
Flagellated Vibrio cholerae
Publication : Fish & shellfish immunology

Vibrio aestuarianus zinc metalloprotease causes lethality in the Pacific oyster Crassostrea gigas and impairs the host cellular immune defenses

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Fish & shellfish immunology - 17 Jul 2010

Labreuche Y, Le Roux F, Henry J, Zatylny C, Huvet A, Lambert C, Soudant P, Mazel D, Nicolas JL

Link to Pubmed [PMID] – 20624467

Fish Shellfish Immunol. 2010 Nov;29(5):753-8

Extracellular products (ECPs) of the pathogenic Vibrio aestuarianus 01/32 were previously reported to display lethality in Crassostrea gigas oysters and to cause morphological changes and immunosuppression in oyster hemocytes. To identify the source of this toxicity, biochemical and genetic approaches were developed. ECP protease activity and lethality were shown to be significantly reduced following incubation with metal chelators, suggesting the involvement of a zinc metalloprotease. An open reading frame of 1836 bp encoding a 611-aa metalloprotease (designated Vam) was identified. The deduced protein sequence showed high homology to other Vibrio metalloproteases reported to be involved in pathogenicity. To further confirm the role of this enzyme in ECP toxicity, a plasmid carrying the vam gene under the control of an araC-P(BAD) expression cassette was transferred to a Vibrio splendidus related strain, LMG20012(T), previously characterized as non-pathogenic to oysters. Expression of Vam conferred a toxic phenotype to LMG20012(T) ECPs in vivo and cytotoxicity to oyster hemocytes in vitro. Collectively, these data suggest that the Vam metalloprotease is a major contributor to the toxicity induced by V. aestuarianus ECPs and is involved in the impairment of oyster hemocyte functions.

http://www.ncbi.nlm.nih.gov/pubmed/20624467