Loading…

Comprehensive Proteomics Analysis of the Hemolymph Composition of Sugar-Fed Aedes aegypti Female and Male Mosquitoes

In arthropods, hemolymph carries immune cells and solubilizes and transports nutrients, hormones, and other molecules that are involved in diverse physiological processes including immunity, metabolism, and reproduction. However, despite such physiological importance, little is known about its compo...

Full description

Saved in:
Bibliographic Details
Published in:Journal of proteome research 2024-04, Vol.23 (4), p.1471-1487
Main Authors: Alvarenga, Patricia H., Alves e Silva, Thiago Luiz, Suzuki, Motoshi, Nardone, Glenn, Cecilio, Pedro, Vega-Rodriguez, Joel, Ribeiro, Jose M.C., Andersen, John F.
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites cdi_FETCH-LOGICAL-a299t-bddccbec9ca19f216ebb64bd619cf1d5dc3b1639c1d31b610d9eb7a475e7052c3
container_end_page 1487
container_issue 4
container_start_page 1471
container_title Journal of proteome research
container_volume 23
creator Alvarenga, Patricia H.
Alves e Silva, Thiago Luiz
Suzuki, Motoshi
Nardone, Glenn
Cecilio, Pedro
Vega-Rodriguez, Joel
Ribeiro, Jose M.C.
Andersen, John F.
description In arthropods, hemolymph carries immune cells and solubilizes and transports nutrients, hormones, and other molecules that are involved in diverse physiological processes including immunity, metabolism, and reproduction. However, despite such physiological importance, little is known about its composition. We applied mass spectrometry-based label-free quantification approaches to study the proteome of hemolymph perfused from sugar-fed female and male Aedes aegypti mosquitoes. A total of 1403 proteins were identified, out of which 447 of them were predicted to be extracellular. In both sexes, almost half of these extracellular proteins were predicted to be involved in defense/immune response, and their relative abundances (based on their intensity-based absolute quantification, iBAQ) were 37.9 and 33.2%, respectively. Interestingly, among them, 102 serine proteases/serine protease-homologues were identified, with almost half of them containing CLIP regulatory domains. Moreover, proteins belonging to families classically described as chemoreceptors, such as odorant-binding proteins (OBPs) and chemosensory proteins (CSPs), were also highly abundant in the hemolymph of both sexes. Our data provide a comprehensive catalogue of A. aegypti hemolymph basal protein content, revealing numerous unexplored targets for future research on mosquito physiology and disease transmission. It also provides a reference for future studies on the effect of blood meal and infection on hemolymph composition.
doi_str_mv 10.1021/acs.jproteome.3c00918
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_3034245827</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3034245827</sourcerecordid><originalsourceid>FETCH-LOGICAL-a299t-bddccbec9ca19f216ebb64bd619cf1d5dc3b1639c1d31b610d9eb7a475e7052c3</originalsourceid><addsrcrecordid>eNqFkEtPwzAQhC0E4v0TQD5ySfHGdVIfq4oCEggk4Bz5saFGSRyyCVL_PSktXDntSDszq_0YuwAxAZHCtXE0-Wi72GOscSKdEBpme-wYlFSJ1CLf_9UzLY_YCdGHEKByIQ_ZkZypPJMajlm_iHXb4QobCl_In7eFwRGfN6ZaUyAeS96vkN9hHat13a74JhIp9CE2m-XL8G66ZImez9EjcYPv67YPfIm1qZCbxvPHjXiM9DmEPiKdsYPSVITnu3nK3pY3r4u75OHp9n4xf0hMqnWfWO-ds-i0M6DLFDK0Nptan4F2JXjlnbQwvuHAS7AZCK_R5maaK8yFSp08ZVfb3pHT54DUF3Ugh1VlGowDFVLIaTpVszQfrWprdV0k6rAs2i7UplsXIIoN8GIEXvwBL3bAx9zl7sRga_R_qV_CowG2hp98HLoRK_1T-g2gwpP4</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>3034245827</pqid></control><display><type>article</type><title>Comprehensive Proteomics Analysis of the Hemolymph Composition of Sugar-Fed Aedes aegypti Female and Male Mosquitoes</title><source>American Chemical Society:Jisc Collections:American Chemical Society Read &amp; Publish Agreement 2022-2024 (Reading list)</source><creator>Alvarenga, Patricia H. ; Alves e Silva, Thiago Luiz ; Suzuki, Motoshi ; Nardone, Glenn ; Cecilio, Pedro ; Vega-Rodriguez, Joel ; Ribeiro, Jose M.C. ; Andersen, John F.</creator><creatorcontrib>Alvarenga, Patricia H. ; Alves e Silva, Thiago Luiz ; Suzuki, Motoshi ; Nardone, Glenn ; Cecilio, Pedro ; Vega-Rodriguez, Joel ; Ribeiro, Jose M.C. ; Andersen, John F.</creatorcontrib><description>In arthropods, hemolymph carries immune cells and solubilizes and transports nutrients, hormones, and other molecules that are involved in diverse physiological processes including immunity, metabolism, and reproduction. However, despite such physiological importance, little is known about its composition. We applied mass spectrometry-based label-free quantification approaches to study the proteome of hemolymph perfused from sugar-fed female and male Aedes aegypti mosquitoes. A total of 1403 proteins were identified, out of which 447 of them were predicted to be extracellular. In both sexes, almost half of these extracellular proteins were predicted to be involved in defense/immune response, and their relative abundances (based on their intensity-based absolute quantification, iBAQ) were 37.9 and 33.2%, respectively. Interestingly, among them, 102 serine proteases/serine protease-homologues were identified, with almost half of them containing CLIP regulatory domains. Moreover, proteins belonging to families classically described as chemoreceptors, such as odorant-binding proteins (OBPs) and chemosensory proteins (CSPs), were also highly abundant in the hemolymph of both sexes. Our data provide a comprehensive catalogue of A. aegypti hemolymph basal protein content, revealing numerous unexplored targets for future research on mosquito physiology and disease transmission. It also provides a reference for future studies on the effect of blood meal and infection on hemolymph composition.</description><identifier>ISSN: 1535-3893</identifier><identifier>ISSN: 1535-3907</identifier><identifier>EISSN: 1535-3907</identifier><identifier>DOI: 10.1021/acs.jproteome.3c00918</identifier><identifier>PMID: 38576391</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Aedes - metabolism ; Animals ; Carbohydrates ; Female ; Hemolymph - metabolism ; Humans ; Male ; Proteomics ; Sugars - metabolism</subject><ispartof>Journal of proteome research, 2024-04, Vol.23 (4), p.1471-1487</ispartof><rights>Not subject to U.S. Copyright. Published 2024 by American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-a299t-bddccbec9ca19f216ebb64bd619cf1d5dc3b1639c1d31b610d9eb7a475e7052c3</cites><orcidid>0000-0002-2236-6308</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38576391$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Alvarenga, Patricia H.</creatorcontrib><creatorcontrib>Alves e Silva, Thiago Luiz</creatorcontrib><creatorcontrib>Suzuki, Motoshi</creatorcontrib><creatorcontrib>Nardone, Glenn</creatorcontrib><creatorcontrib>Cecilio, Pedro</creatorcontrib><creatorcontrib>Vega-Rodriguez, Joel</creatorcontrib><creatorcontrib>Ribeiro, Jose M.C.</creatorcontrib><creatorcontrib>Andersen, John F.</creatorcontrib><title>Comprehensive Proteomics Analysis of the Hemolymph Composition of Sugar-Fed Aedes aegypti Female and Male Mosquitoes</title><title>Journal of proteome research</title><addtitle>J. Proteome Res</addtitle><description>In arthropods, hemolymph carries immune cells and solubilizes and transports nutrients, hormones, and other molecules that are involved in diverse physiological processes including immunity, metabolism, and reproduction. However, despite such physiological importance, little is known about its composition. We applied mass spectrometry-based label-free quantification approaches to study the proteome of hemolymph perfused from sugar-fed female and male Aedes aegypti mosquitoes. A total of 1403 proteins were identified, out of which 447 of them were predicted to be extracellular. In both sexes, almost half of these extracellular proteins were predicted to be involved in defense/immune response, and their relative abundances (based on their intensity-based absolute quantification, iBAQ) were 37.9 and 33.2%, respectively. Interestingly, among them, 102 serine proteases/serine protease-homologues were identified, with almost half of them containing CLIP regulatory domains. Moreover, proteins belonging to families classically described as chemoreceptors, such as odorant-binding proteins (OBPs) and chemosensory proteins (CSPs), were also highly abundant in the hemolymph of both sexes. Our data provide a comprehensive catalogue of A. aegypti hemolymph basal protein content, revealing numerous unexplored targets for future research on mosquito physiology and disease transmission. It also provides a reference for future studies on the effect of blood meal and infection on hemolymph composition.</description><subject>Aedes - metabolism</subject><subject>Animals</subject><subject>Carbohydrates</subject><subject>Female</subject><subject>Hemolymph - metabolism</subject><subject>Humans</subject><subject>Male</subject><subject>Proteomics</subject><subject>Sugars - metabolism</subject><issn>1535-3893</issn><issn>1535-3907</issn><issn>1535-3907</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><recordid>eNqFkEtPwzAQhC0E4v0TQD5ySfHGdVIfq4oCEggk4Bz5saFGSRyyCVL_PSktXDntSDszq_0YuwAxAZHCtXE0-Wi72GOscSKdEBpme-wYlFSJ1CLf_9UzLY_YCdGHEKByIQ_ZkZypPJMajlm_iHXb4QobCl_In7eFwRGfN6ZaUyAeS96vkN9hHat13a74JhIp9CE2m-XL8G66ZImez9EjcYPv67YPfIm1qZCbxvPHjXiM9DmEPiKdsYPSVITnu3nK3pY3r4u75OHp9n4xf0hMqnWfWO-ds-i0M6DLFDK0Nptan4F2JXjlnbQwvuHAS7AZCK_R5maaK8yFSp08ZVfb3pHT54DUF3Ugh1VlGowDFVLIaTpVszQfrWprdV0k6rAs2i7UplsXIIoN8GIEXvwBL3bAx9zl7sRga_R_qV_CowG2hp98HLoRK_1T-g2gwpP4</recordid><startdate>20240405</startdate><enddate>20240405</enddate><creator>Alvarenga, Patricia H.</creator><creator>Alves e Silva, Thiago Luiz</creator><creator>Suzuki, Motoshi</creator><creator>Nardone, Glenn</creator><creator>Cecilio, Pedro</creator><creator>Vega-Rodriguez, Joel</creator><creator>Ribeiro, Jose M.C.</creator><creator>Andersen, John F.</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-2236-6308</orcidid></search><sort><creationdate>20240405</creationdate><title>Comprehensive Proteomics Analysis of the Hemolymph Composition of Sugar-Fed Aedes aegypti Female and Male Mosquitoes</title><author>Alvarenga, Patricia H. ; Alves e Silva, Thiago Luiz ; Suzuki, Motoshi ; Nardone, Glenn ; Cecilio, Pedro ; Vega-Rodriguez, Joel ; Ribeiro, Jose M.C. ; Andersen, John F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a299t-bddccbec9ca19f216ebb64bd619cf1d5dc3b1639c1d31b610d9eb7a475e7052c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Aedes - metabolism</topic><topic>Animals</topic><topic>Carbohydrates</topic><topic>Female</topic><topic>Hemolymph - metabolism</topic><topic>Humans</topic><topic>Male</topic><topic>Proteomics</topic><topic>Sugars - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Alvarenga, Patricia H.</creatorcontrib><creatorcontrib>Alves e Silva, Thiago Luiz</creatorcontrib><creatorcontrib>Suzuki, Motoshi</creatorcontrib><creatorcontrib>Nardone, Glenn</creatorcontrib><creatorcontrib>Cecilio, Pedro</creatorcontrib><creatorcontrib>Vega-Rodriguez, Joel</creatorcontrib><creatorcontrib>Ribeiro, Jose M.C.</creatorcontrib><creatorcontrib>Andersen, John F.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of proteome research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Alvarenga, Patricia H.</au><au>Alves e Silva, Thiago Luiz</au><au>Suzuki, Motoshi</au><au>Nardone, Glenn</au><au>Cecilio, Pedro</au><au>Vega-Rodriguez, Joel</au><au>Ribeiro, Jose M.C.</au><au>Andersen, John F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comprehensive Proteomics Analysis of the Hemolymph Composition of Sugar-Fed Aedes aegypti Female and Male Mosquitoes</atitle><jtitle>Journal of proteome research</jtitle><addtitle>J. Proteome Res</addtitle><date>2024-04-05</date><risdate>2024</risdate><volume>23</volume><issue>4</issue><spage>1471</spage><epage>1487</epage><pages>1471-1487</pages><issn>1535-3893</issn><issn>1535-3907</issn><eissn>1535-3907</eissn><abstract>In arthropods, hemolymph carries immune cells and solubilizes and transports nutrients, hormones, and other molecules that are involved in diverse physiological processes including immunity, metabolism, and reproduction. However, despite such physiological importance, little is known about its composition. We applied mass spectrometry-based label-free quantification approaches to study the proteome of hemolymph perfused from sugar-fed female and male Aedes aegypti mosquitoes. A total of 1403 proteins were identified, out of which 447 of them were predicted to be extracellular. In both sexes, almost half of these extracellular proteins were predicted to be involved in defense/immune response, and their relative abundances (based on their intensity-based absolute quantification, iBAQ) were 37.9 and 33.2%, respectively. Interestingly, among them, 102 serine proteases/serine protease-homologues were identified, with almost half of them containing CLIP regulatory domains. Moreover, proteins belonging to families classically described as chemoreceptors, such as odorant-binding proteins (OBPs) and chemosensory proteins (CSPs), were also highly abundant in the hemolymph of both sexes. Our data provide a comprehensive catalogue of A. aegypti hemolymph basal protein content, revealing numerous unexplored targets for future research on mosquito physiology and disease transmission. It also provides a reference for future studies on the effect of blood meal and infection on hemolymph composition.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>38576391</pmid><doi>10.1021/acs.jproteome.3c00918</doi><tpages>17</tpages><orcidid>https://orcid.org/0000-0002-2236-6308</orcidid></addata></record>
fulltext fulltext
identifier ISSN: 1535-3893
ispartof Journal of proteome research, 2024-04, Vol.23 (4), p.1471-1487
issn 1535-3893
1535-3907
1535-3907
language eng
recordid cdi_proquest_miscellaneous_3034245827
source American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)
subjects Aedes - metabolism
Animals
Carbohydrates
Female
Hemolymph - metabolism
Humans
Male
Proteomics
Sugars - metabolism
title Comprehensive Proteomics Analysis of the Hemolymph Composition of Sugar-Fed Aedes aegypti Female and Male Mosquitoes
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T02%3A13%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Comprehensive%20Proteomics%20Analysis%20of%20the%20Hemolymph%20Composition%20of%20Sugar-Fed%20Aedes%20aegypti%20Female%20and%20Male%20Mosquitoes&rft.jtitle=Journal%20of%20proteome%20research&rft.au=Alvarenga,%20Patricia%20H.&rft.date=2024-04-05&rft.volume=23&rft.issue=4&rft.spage=1471&rft.epage=1487&rft.pages=1471-1487&rft.issn=1535-3893&rft.eissn=1535-3907&rft_id=info:doi/10.1021/acs.jproteome.3c00918&rft_dat=%3Cproquest_cross%3E3034245827%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a299t-bddccbec9ca19f216ebb64bd619cf1d5dc3b1639c1d31b610d9eb7a475e7052c3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=3034245827&rft_id=info:pmid/38576391&rfr_iscdi=true