2015
DOI: 10.1016/j.jinsphys.2015.05.002
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Digestive proteases in bodies and faeces of the two-spotted spider mite, Tetranychus urticae

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Cited by 59 publications
(66 citation statements)
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“…The hydrolysis of dietary proteins in spider mites relies on cysteine (cathepsin B-, cathepsin L-and legumainlike) and aspartyl (cathepsin D-like) proteases and aminopeptidases (Carrillo et al, 2011;Santamaria et al, 2015a). Our results indicate that T. evansi has a similar digestive proteolytic profile, hydrolyzing specific substrates for cathepsin D, cathepsin B, cathepsin L and legumain proteases and aminopeptidases.…”
Section: Discussionmentioning
confidence: 73%
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“…The hydrolysis of dietary proteins in spider mites relies on cysteine (cathepsin B-, cathepsin L-and legumainlike) and aspartyl (cathepsin D-like) proteases and aminopeptidases (Carrillo et al, 2011;Santamaria et al, 2015a). Our results indicate that T. evansi has a similar digestive proteolytic profile, hydrolyzing specific substrates for cathepsin D, cathepsin B, cathepsin L and legumain proteases and aminopeptidases.…”
Section: Discussionmentioning
confidence: 73%
“…Digestion of dietary proteins relies on cysteine and aspartyl proteases and aminopeptidases (Santamaria et al, 2015a) and that of dietary carbohydrates on glycosidases (Nisbet and Billingsley, 2000). The genome of T. urticae has been sequenced (Grbic et al, 2011) and specific expansions have been found for gene families involved in digestion and detoxification processes, which may be involved in the capability of T. urticae to cope with the varying nutrients and defense compounds of different host plants.…”
Section: Mite Pestsmentioning
confidence: 99%
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