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

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dc.contributor.authorWhiten, Shavonn R.en
dc.contributor.authorRay, W. Keithen
dc.contributor.authorHelm, Richard F.en
dc.contributor.authorAdelman, Zach N.en
dc.contributor.departmentBiochemistryen
dc.date.accessioned2019-06-05T13:02:46Zen
dc.date.available2019-06-05T13:02:46Zen
dc.date.issued2018-03-23en
dc.description.abstractThe 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.en
dc.description.notesThe mass spectrometry resources used in this work are maintained in part through funding by the Fralin Life Science Institute, the Agricultural Experiment Station Hatch Program, and the McIntire-Stennis Program at Virginia Tech. This study was supported in part by Agrilife Research, as well as by the National Institute of Allergies and Infectious Diseases of the National Institutes of Health under award number AI115138. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.en
dc.description.sponsorshipFralin Life Science Institute; Agricultural Experiment Station Hatch Program; McIntire-Stennis Program at Virginia Tech; Agrilife Research; National Institute of Allergies and Infectious Diseases of the National Institutes of Health [AI115138]en
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0194734en
dc.identifier.eissn1932-6203en
dc.identifier.issue3en
dc.identifier.othere0194734en
dc.identifier.pmid29570734en
dc.identifier.urihttp://hdl.handle.net/10919/89754en
dc.identifier.volume13en
dc.language.isoenen
dc.publisherPLOSen
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.titleCharacterization of the adult Aedes aegypti early midgut peritrophic matrix proteome using LC-MSen
dc.title.serialPLOS ONEen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten

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