Characterization of the adult Aedes aegypti early midgut peritrophic matrix proteome using LC-MS.

The Aedes aegypti mosquito is the principal vector of arboviruses such as dengue, chikungunya, yellow fever, and Zika virus. These arboviruses are transmitted during adult female mosquito bloodfeeding. While these viruses must transverse the midgut to replicate, the blood meal must also reach the mi...

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Main Authors: Shavonn R Whiten, W Keith Ray, Richard F Helm, Zach N Adelman
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2018-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC5865745?pdf=render
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spelling doaj-9adf8c0eb50c451f94cc5c484a7968522020-11-25T01:45:53ZengPublic Library of Science (PLoS)PLoS ONE1932-62032018-01-01133e019473410.1371/journal.pone.0194734Characterization of the adult Aedes aegypti early midgut peritrophic matrix proteome using LC-MS.Shavonn R WhitenW Keith RayRichard F HelmZach N AdelmanThe Aedes aegypti mosquito is the principal vector of arboviruses such as dengue, chikungunya, yellow fever, and Zika virus. These arboviruses are transmitted during adult female mosquito bloodfeeding. While these viruses must transverse the midgut to replicate, the blood meal must also reach the midgut to be digested, absorbed, or excreted, as aggregation of blood meal metabolites can be toxic to the female mosquito midgut. The midgut peritrophic matrix (PM), a semipermeable extracellular layer comprised of chitin fibrils, glycoproteins, and proteoglycans, is one such mechanism of protection for the mosquito midgut. However, this structure has not been characterized for adult female Ae. aegypti. We conducted a mass spectrometry based proteomic analysis to identify proteins that comprise or are associated with the adult female Ae. aegypti early midgut PM. Altogether, 474 unique proteins were identified, with 115 predicted as secreted. GO-term enrichment analysis revealed an abundance of serine-type proteases and several known and novel intestinal mucins. In addition, approximately 10% of the peptides identified corresponded to known salivary proteins, indicating Ae. aegypti mosquitoes extensively swallow their own salivary secretions. However, the physiological relevance of this remains unclear, and further studies are needed to determine PM proteins integral for midgut protection from blood meal derived toxicity and pathogen protection. Finally, we describe substantial discordance between previously described transcriptionally changes observed in the midgut in response to a bloodmeal and the presence of the corresponding protein in the PM. Data are available via ProteomeXchange with identifier PXD007627.http://europepmc.org/articles/PMC5865745?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Shavonn R Whiten
W Keith Ray
Richard F Helm
Zach N Adelman
spellingShingle Shavonn R Whiten
W Keith Ray
Richard F Helm
Zach N Adelman
Characterization of the adult Aedes aegypti early midgut peritrophic matrix proteome using LC-MS.
PLoS ONE
author_facet Shavonn R Whiten
W Keith Ray
Richard F Helm
Zach N Adelman
author_sort Shavonn R Whiten
title Characterization of the adult Aedes aegypti early midgut peritrophic matrix proteome using LC-MS.
title_short Characterization of the adult Aedes aegypti early midgut peritrophic matrix proteome using LC-MS.
title_full Characterization of the adult Aedes aegypti early midgut peritrophic matrix proteome using LC-MS.
title_fullStr Characterization of the adult Aedes aegypti early midgut peritrophic matrix proteome using LC-MS.
title_full_unstemmed Characterization of the adult Aedes aegypti early midgut peritrophic matrix proteome using LC-MS.
title_sort characterization of the adult aedes aegypti early midgut peritrophic matrix proteome using lc-ms.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2018-01-01
description The Aedes aegypti mosquito is the principal vector of arboviruses such as dengue, chikungunya, yellow fever, and Zika virus. These arboviruses are transmitted during adult female mosquito bloodfeeding. While these viruses must transverse the midgut to replicate, the blood meal must also reach the midgut to be digested, absorbed, or excreted, as aggregation of blood meal metabolites can be toxic to the female mosquito midgut. The midgut peritrophic matrix (PM), a semipermeable extracellular layer comprised of chitin fibrils, glycoproteins, and proteoglycans, is one such mechanism of protection for the mosquito midgut. However, this structure has not been characterized for adult female Ae. aegypti. We conducted a mass spectrometry based proteomic analysis to identify proteins that comprise or are associated with the adult female Ae. aegypti early midgut PM. Altogether, 474 unique proteins were identified, with 115 predicted as secreted. GO-term enrichment analysis revealed an abundance of serine-type proteases and several known and novel intestinal mucins. In addition, approximately 10% of the peptides identified corresponded to known salivary proteins, indicating Ae. aegypti mosquitoes extensively swallow their own salivary secretions. However, the physiological relevance of this remains unclear, and further studies are needed to determine PM proteins integral for midgut protection from blood meal derived toxicity and pathogen protection. Finally, we describe substantial discordance between previously described transcriptionally changes observed in the midgut in response to a bloodmeal and the presence of the corresponding protein in the PM. Data are available via ProteomeXchange with identifier PXD007627.
url http://europepmc.org/articles/PMC5865745?pdf=render
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