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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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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. |
format | Online Article Text |
id | pubmed-7601585 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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