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Culex quinquefasciatus: vitellogenin and their proteases


A recent study of the vitellogenic process of Culex quinquefasciatus (Cardoso et al., 2010) opened some questions that we intend to answer in this project. 1. It is well known in several insects that yolk granules also carry the proenzymes that will hydrolyze vitellin during embryogenesis. We have already established by mass spectrometry the presence of two cathepsins B and a cathepsin L in egg extract of Cx. quinquefasciatus and partially characterized the transcriptional profile and activity of cathepsins B (Moura et al., 2012). Now we intend to improve this last analysis and to characterize the activity and the transcriptional profile of cathepsin L as well as to determine their synthesis location(s) and their routes of accumulation in the oocyte. 2. Repeated analyzes of the vitellogenin transcriptional profile suggest an abundant RNA production in the vitellogenic ovaries of Cx. quinquefasciatus from 36 h post blood meal. We intend to confirm this fact by in situ hybridation. Another approach to be adopted to improve the vitellogenin characterization will be its purification from vitellogenic ovaries by chromatographic procedures and the production of polyclonal antibodies for immunocharacterization. (AU)

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
MOURA, ALEXANDRE S.; CARDOSO, ANDRE F.; COSTA-DA-SILVA, ANDRE L.; WINTER, CARLOS E.; TANIA BIJOVSKY, A.. Two Cathepsins B Are Responsible for the Yolk Protein Hydrolysis in Culex quinquefasciatus. PLoS One, v. 10, n. 2, . (10/51241-0, 13/09211-4)
MARTINS, LARISSA A.; FOGACA, ANDREA C.; TANIA BIJOVSKY, A.; CARBALLAR-LEJARAZU, REBECA; MARINOTTI, OSVALDO; CARDOSO, ANDRE F.. Culex quinquefasciatus Storage Proteins. PLoS One, v. 8, n. 10, . (10/51241-0, 13/09211-4)

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