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

Ines Martin-Martin, Andrew Paige, Paola Carolina Valenzuela Leon, Apostolos G. Gittis, Olivia Kern, Brian Bonilla, Andrezza Campos Chagas, Sundar Ganesan, Leticia Barion Smith, David N. Garboczi and Eric Calvo ()
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Ines Martin-Martin: National Institutes of Health
Andrew Paige: National Institutes of Health
Paola Carolina Valenzuela Leon: National Institutes of Health
Apostolos G. Gittis: National Institutes of Health
Olivia Kern: National Institutes of Health
Brian Bonilla: National Institutes of Health
Andrezza Campos Chagas: National Institutes of Health
Sundar Ganesan: National Institutes of Health
Leticia Barion Smith: National Institutes of Health
David N. Garboczi: National Institutes of Health
Eric Calvo: National Institutes of Health

Nature Communications, 2020, vol. 11, issue 1, 1-15

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-16665-z

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