DmCatD, a cathepsin D-like peptidase of the hematophagous insect Dipetalogaster maxima (Hemiptera: Reduviidae): Purification, bioinformatic analyses and the significance of its interaction with lipophorin in the internalization by developing oocytes

LEYRIA, JIMENA; FRUTTERO, LEONARDO L.; LIGABUE-BRAUN, RODRIGO; DEFFERRARI, MARINA S.; ARRESE, ESTELA L.; SOULAGES, JOSÉ L.; SETTEMBRINI, BEATRIZ P.; CARLINI, CELIA R.; CANAVOSO, LILIÁN E.

JOURNAL OF INSECT PHYSIOLOGY

PERGAMON-ELSEVIER SCIENCE LTD

Año: 2018 vol. 105 p. 28 - 28

0022-1910

mCatD, a cathepsin D-like peptidase of the hematophagous insect Dipetalogaster maxima, is synthesized by the fat body and the ovary and functions as yolk protein precursor. Functionally, DmCatD is involved in vitellin proteolysis. In this work, we purified and sequenced DmCatD, performed bioinformatic analyses and investigated the events involved in its targeting and storage in developing oocytes. By ion exchange and gel filtration chromatography, DmCatD was purified from egg homogenates and its identity was confirmed by mass spectrometry. Approximately 73% of the full-length transcript was sequenced. The phylogeny indicated that DmCatD has features which suggest its distancing from ?classical? cathepsins D. Bioinformatic analyses using a chimeric construct were employed to predict post-translational modifications. Structural modeling showed that DmCatD exhibited the expected folding for this type of enzyme, and an active site with conserved architecture. The interaction between DmCat