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Provedor de dados:  Inra
País:  France
Título:  Spodoptera frugiperda X-tox protein, an immune related defensin rosary, has lost the function ancestral defensins
Autores:  Destoumieux-Garzon, D.
Brehélin, M.
Bulet, B.
Boublik, Y.
Girard, P.A.
Baghdiguian, S.
Zumbihl, R.
Escoubas, J.M.
Data:  2009
Ano:  2009
Palavras-chave:  LEPIDOPTERE X-TOX PROTEIN
LEPIDOPTERA
IMMUNE-RELATED PROTEIN
ANCESTRAL DEFENSINS
SPODOPTERA FRUGIPERDA
Resumo:  Background: X-tox proteins are a family of immune-related proteins only found in Lepidoptera and characterized by imperfectly conserved tandem repeats of several defensin-like motifs. Previous phylogenetic analysis of X-tox genes supported the hypothesis that X-tox have evolved from defensins in a lineage-specific gene evolution restricted to Lepidoptera. In this paper, we performed a protein study in which we asked whether X-tox proteins have conserved the antimicrobial functions of their ancestral defensins and have evolved as defensin reservoirs.Methodology/Principal Findings: We followed the outcome of Spod-11-tox, an X-tox protein characterized in Spodoptera frugiperda, in bacteria-challenged larvae using both immunochemistry and antimicrobial assays. Three hours post infection, the Spod-11-tox protein was expressed in 80% of the two main classes of circulating hemocytes (granulocytes and plasmatocytes). Located in secretory granules of hemocytes, Spod-11-tox was never observed in contact with microorganisms entrapped within phagolyzosomes showing that Spod-11-tox is not involved in intracellular pathogen killing. In fact, the Spod-11-tox protein was found to be secreted into the hemolymph of experimentally challenged larvae. In order to determine antimicrobial properties of the Spod-11-tox protein, it was consequently fractionated according to a protocol frequently used for antimicrobial peptide purification. Over the course of purification, the anti-Spod-11-tox immunoreactivity was found to be dissociated from the antimicrobial activity. This indicates that Spod-11-tox is not processed into bioactive defensins in response to a microbial challenge.Conclusions/Significance: Altogether, our results show that X-tox proteins have not evolved as defensin reservoirs and have lost the antimicrobial properties of the ancestral insect defensins. The lepidopteran X-tox protein family will provide a valuable and tractable model to improve our knowledge on the molecular evolution of defensins, a class of innate immune effectors largely distributed over the three eukaryotic kingdoms
Tipo:  Journal Article
Idioma:  Inglês
Identificador:  http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD201095cf8004&uri=/notices/prodinra1/2010/10/

http://www.prodinra.inra.fr/prodinra/pinra/data/2010/09/PROD201095cf8004_20100914113340568.pdf
Formato:  application/pdf
Fonte:  Plos One. 2009, 4 (8) : e6795
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