Proteomics

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Mosquito-Derived Anophelin Sulfoproteins are Potent Anti-Thrombotics


ABSTRACT: we first expressed AAa and AAg in a eukaryotic system to investigate whether the proteins could be sulfated in vivo. For this purpose we used insect cells as a model of the Anopheles mosquito. Specifically, codon-optimized sequences encoding AAa and AAg were designed as N-terminal fusions with the honeybee mellitin signal sequence in order to direct the recombinant proteins to the secretion pathway and were expressed in Trichoplusia ni insect cells. Following expression, the cell medium containing the secreted proteins was analyzed by nanoliquid chromatography coupled to tandem mass spectrometry (nanoLC-MS/MS).

INSTRUMENT(S): Orbitrap Fusion ETD

ORGANISM(S): Anopheles Albimanus Anopheles Gambiae (african Malaria Mosquito)

SUBMITTER: Benjamin Parker  

LAB HEAD: Benjamin Parker

PROVIDER: PXD008240 | Pride | 2018-08-30

REPOSITORIES: Pride

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Publications


The anophelins are small protein thrombin inhibitors that are produced in the salivary glands of the <i>Anopheles</i> mosquito to fulfill a vital role in blood feeding. A bioinformatic analysis of anophelin sequences revealed the presence of conserved tyrosine residues in an acidic environment that were predicted to be post-translationally sulfated <i>in vivo</i>. To test this prediction, insect cell expression of two anophelin proteins, from <i>Anopheles albimanus</i> and <i>Anopheles gambiae</  ...[more]

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