ADP binding by the Culex quinquefasciatus mosquito D7 salivary protein enhances blood feeding on mammals.

Nature Communications
Ines Martin-MartinEric Calvo

Abstract

During blood-feeding, mosquito saliva is injected into the skin to facilitate blood meal acquisition. D7 proteins are among the most abundant components of the mosquito saliva. Here we report the ligand binding specificity and physiological relevance of two D7 long proteins from Culex quinquefasciatus mosquito, the vector of filaria parasites or West Nile viruses. CxD7L2 binds biogenic amines and eicosanoids. CxD7L1 exhibits high affinity for ADP and ATP, a binding capacity not reported in any D7. We solve the crystal structure of CxD7L1 in complex with ADP to 1.97 Å resolution. The binding pocket lies between the two protein domains, whereas all known D7s bind ligands either within the N- or the C-terminal domains. We demonstrate that these proteins inhibit hemostasis in ex vivo and in vivo experiments. Our results suggest that the ADP-binding function acquired by CxD7L1 evolved to enhance blood-feeding in mammals, where ADP plays a key role in platelet aggregation.

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Datasets Mentioned

BETA
AF420270

Methods Mentioned

BETA
size exclusion chromatography
electrophoresis
isothermal titration calorimetry
transfection
PCR
enzyme-linked immunosorbent assay
ELISA
biopsies
biopsy

Software Mentioned

Imaris
Phaser
Coot
CFX Maestro
PyMOL graphics system
Phenix
Chimera
BLASTp
UCSF Chimera
GraphPad Prism

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