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Aedes albopictus D7 Salivary Protein Prevents Host Hemostasis and Inflammation

Mosquitoes inject saliva into the host skin to facilitate blood meal acquisition through active compounds that prevent hemostasis. D7 proteins are among the most abundant components of the mosquito saliva and act as scavengers of biogenic amines and eicosanoids. Several members of the D7 family have...

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Autores principales: Martin-Martin, Ines, Smith, Leticia Barion, Chagas, Andrezza Campos, Sá-Nunes, Anderson, Shrivastava, Gaurav, Valenzuela-Leon, Paola Carolina, Calvo, Eric
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7601585/
https://www.ncbi.nlm.nih.gov/pubmed/32992542
http://dx.doi.org/10.3390/biom10101372
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author Martin-Martin, Ines
Smith, Leticia Barion
Chagas, Andrezza Campos
Sá-Nunes, Anderson
Shrivastava, Gaurav
Valenzuela-Leon, Paola Carolina
Calvo, Eric
author_facet Martin-Martin, Ines
Smith, Leticia Barion
Chagas, Andrezza Campos
Sá-Nunes, Anderson
Shrivastava, Gaurav
Valenzuela-Leon, Paola Carolina
Calvo, Eric
author_sort Martin-Martin, Ines
collection PubMed
description Mosquitoes inject saliva into the host skin to facilitate blood meal acquisition through active compounds that prevent hemostasis. D7 proteins are among the most abundant components of the mosquito saliva and act as scavengers of biogenic amines and eicosanoids. Several members of the D7 family have been characterized at the biochemical level; however, none have been studied thus far in Aedes albopictus, a permissive vector for several arboviruses that causes extensive human morbidity and mortality. Here, we report the binding capabilities of a D7 long form protein from Ae. albopictus (AlboD7L1) by isothermal titration calorimetry and compared its model structure with previously solved D7 structures. The physiological function of AlboD7L1 was demonstrated by ex vivo platelet aggregation and in vivo leukocyte recruitment experiments. AlboD7L1 binds host hemostasis agonists, including biogenic amines, leukotrienes, and the thromboxane A2 analog U-46619. AlboD7L1 protein model predicts binding of biolipids through its N-terminal domain, while the C-terminal domain binds biogenic amines. We demonstrated the biological function of AlboD7L1 as an inhibitor of both platelet aggregation and cell recruitment of neutrophils and eosinophils. Altogether, this study reinforces the physiological relevance of the D7 salivary proteins as anti-hemostatic and anti-inflammatory molecules that help blood feeding in mosquitoes.
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spelling pubmed-76015852020-11-01 Aedes albopictus D7 Salivary Protein Prevents Host Hemostasis and Inflammation Martin-Martin, Ines Smith, Leticia Barion Chagas, Andrezza Campos Sá-Nunes, Anderson Shrivastava, Gaurav Valenzuela-Leon, Paola Carolina Calvo, Eric Biomolecules Article Mosquitoes inject saliva into the host skin to facilitate blood meal acquisition through active compounds that prevent hemostasis. D7 proteins are among the most abundant components of the mosquito saliva and act as scavengers of biogenic amines and eicosanoids. Several members of the D7 family have been characterized at the biochemical level; however, none have been studied thus far in Aedes albopictus, a permissive vector for several arboviruses that causes extensive human morbidity and mortality. Here, we report the binding capabilities of a D7 long form protein from Ae. albopictus (AlboD7L1) by isothermal titration calorimetry and compared its model structure with previously solved D7 structures. The physiological function of AlboD7L1 was demonstrated by ex vivo platelet aggregation and in vivo leukocyte recruitment experiments. AlboD7L1 binds host hemostasis agonists, including biogenic amines, leukotrienes, and the thromboxane A2 analog U-46619. AlboD7L1 protein model predicts binding of biolipids through its N-terminal domain, while the C-terminal domain binds biogenic amines. We demonstrated the biological function of AlboD7L1 as an inhibitor of both platelet aggregation and cell recruitment of neutrophils and eosinophils. Altogether, this study reinforces the physiological relevance of the D7 salivary proteins as anti-hemostatic and anti-inflammatory molecules that help blood feeding in mosquitoes. MDPI 2020-09-27 /pmc/articles/PMC7601585/ /pubmed/32992542 http://dx.doi.org/10.3390/biom10101372 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Martin-Martin, Ines
Smith, Leticia Barion
Chagas, Andrezza Campos
Sá-Nunes, Anderson
Shrivastava, Gaurav
Valenzuela-Leon, Paola Carolina
Calvo, Eric
Aedes albopictus D7 Salivary Protein Prevents Host Hemostasis and Inflammation
title Aedes albopictus D7 Salivary Protein Prevents Host Hemostasis and Inflammation
title_full Aedes albopictus D7 Salivary Protein Prevents Host Hemostasis and Inflammation
title_fullStr Aedes albopictus D7 Salivary Protein Prevents Host Hemostasis and Inflammation
title_full_unstemmed Aedes albopictus D7 Salivary Protein Prevents Host Hemostasis and Inflammation
title_short Aedes albopictus D7 Salivary Protein Prevents Host Hemostasis and Inflammation
title_sort aedes albopictus d7 salivary protein prevents host hemostasis and inflammation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7601585/
https://www.ncbi.nlm.nih.gov/pubmed/32992542
http://dx.doi.org/10.3390/biom10101372
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