Two Cathepsins B Are Responsible for the Yolk Protein Hydrolysis in XXXX .

@entity535 @entity3754 @entity2957 @entity71564 @entity71565
Despite the established role of @entity2957 as a vector of various neurotropic viruses, such as the Rift Valley and West Nile viruses, as well as @entity3754 , little is known regarding the organism's reproductive physiology. As in other oviparous animals, @entity71564 , the most important source of nutrients for the embryo development, is digested by intracellular proteases. Using mass spectrometry, we have identified two @entity71565 homologues partially purified by self-proteolysis of Cx. quinquefasciatus total egg extract. The transcriptional profile of these two @entity71565 homologues was determined by quantitative RT-PCR, and the enzymatic activity associated with the peptidase was determined in ovaries after female engorgement. According to the VectorBase (vectorbase.org) annotation, both @entity71565 homologues shared approximately 66% identity in their @entity535 sequences. The two @entity71565 genes are expressed simultaneously in the fat body of the vitellogenic females, and enzymatic activity was detected within the ovaries, suggesting an extra-ovarian origin. Similar to the transcriptional profile of @entity71564 , @entity71565 transcripts were shown to accumulate post-blood meal and reached their highest expression at 36 h PBM. However, while @entity71564 expression decreased drastically at 48 h PBM, the expression of the cathepsins increased until 84 h PBM, at which time the females of our colony were ready for oviposition. The similarity between their transcriptional profiles strongly suggests a role for the @entity71565 homologues in vitellin degradation.
