IrAE – An asparaginyl endopeptidase (legumain) in the gut of the hard tick Ixodes ricinus

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IrAE: an asparaginyl endopeptidase (legumain) in the gut of the hard tick Ixodes ricinus.

Ticks are ectoparasitic blood-feeders and important vectors for pathogens including arboviruses, rickettsiae, spirochetes and protozoa. As obligate blood-feeders, one possible strategy to retard disease transmission is disruption of the parasite's ability to digest host proteins. However, the constituent peptidases in the parasite gut and their potential interplay in the digestion of the blood ...

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The asparaginyl endopeptidase legumain after experimental stroke.

Various proteases in the brain contribute to ischemic brain injury. We investigated the involvement of the asparaginyl endopeptidase legumain after experimental stroke. On the basis of gene array studies and in situ hybridizations, we observed an increase of legumain expression in the peri-infarct area of rats after transient occlusion of the middle cerebral artery (MCAO) for 120 mins with a ma...

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Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity.

Legumain was recently discovered as a lysosomal endopeptidase in mammals [Chen, Dando, Rawlings, Brown, Young, Stevens, Hewitt, Watts and Barrett (1997) J. Biol. Chem. 272, 8090-8098], having been known previously only from plants and invertebrates. It has been shown to play a key role in processing of the C fragment of tetanus toxin for presentation by the MHC class-II system [Manoury, Hewitt,...

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Characterization of the gut-associated cathepsin D hemoglobinase from the tick Ixodes ricinus (IrCD1)

Background: Aspartic peptidase activity initiates a multienzyme hemoglobinolysis inside tick guts. Results: IrCD1 is a structurally unique hemoglobinolytic cathepsin D that is upregulated in tick gut cells during feeding. Conclusion: IrCD1 is the major intestinal aspartic peptidase of I. ricinus. Significance: Biochemical and functional characterization of IrCD1 completes our knowledge on initi...

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IrCL1 - the haemoglobinolytic cathepsin L of the hard tick, Ixodes ricinus.

Intracellular proteolysis of ingested blood proteins is a crucial physiological process in ticks. In our model tick, Ixodes ricinus, cathepsin L (IrCL1) is part of a gut-associated multi-peptidase complex; its endopeptidase activity is important in the initial phase of haemoglobinolysis. We present the functional and biochemical characterisation of this enzyme. We show, by RNA interference (RNA...

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ژورنال

عنوان ژورنال: International Journal for Parasitology

سال: 2007

ISSN: 0020-7519

DOI: 10.1016/j.ijpara.2006.12.020