Evaluation of female Aedes aegypti proteome via LC-ESI-MS/MS using two protein extraction methods
Background. Proteomic analyses have broadened the horizons of vector control measures by identifying proteins associated with different biological and physiological processes and give further insight into the mosquitoes' biology, mechanism of insecticide resistance and pathogens-mosquitoes inte...
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| description | Background. Proteomic analyses have broadened the horizons of vector control measures by identifying proteins associated with different biological and physiological processes and give further insight into the mosquitoes' biology, mechanism of insecticide resistance and pathogens-mosquitoes interaction. Female Ae. aegypti ingests human blood to acquire the requisite nutrients to make eggs. During blood ingestion, female mosquitoes transmit different pathogens. Therefore, this study aimed to determine the best protein extraction method for mass spectrometry analysis which will allow a better proteome profiling for female mosquitoes.
Methods. In this present study, two protein extractions methods were performed to analyze female Ae. aegyti proteome, via TCA acetone precipitation extraction method and a commercial protein extraction reagent CytoBuster (TM). Then, protein identification was performed by LC-ESI-MS/MS and followed by functional protein annotation analysis.
Results. The CytoBuster (TM) reagent gave the highest protein yield with a mean of 475.90 its compared to TCA acetone precipitation extraction showed 283.15 mu g mean of protein. LC-ESI-MS/MS identified 1,290 and 890 proteins from the CytoBusterTM reagent and TCA acetone precipitation, respectively. When comparing the protein class categories in both methods, there were three additional categories for proteins identified using CytoBuster (TM) reagent. The proteins were related to scaffold/adaptor protein (PC00226), protein binding activity modulator (PC00095) and intercellular signal molecule (PC00207). In conclusion, the CytoBuster (TM) protein extraction reagent showed a better performance for the extraction of proteins in term of the protein yield, proteome coverage and extraction speed. |
| doi_str_mv | 10.7717/peerj.10863 |
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Methods. In this present study, two protein extractions methods were performed to analyze female Ae. aegyti proteome, via TCA acetone precipitation extraction method and a commercial protein extraction reagent CytoBuster (TM). Then, protein identification was performed by LC-ESI-MS/MS and followed by functional protein annotation analysis.
Results. The CytoBuster (TM) reagent gave the highest protein yield with a mean of 475.90 its compared to TCA acetone precipitation extraction showed 283.15 mu g mean of protein. LC-ESI-MS/MS identified 1,290 and 890 proteins from the CytoBusterTM reagent and TCA acetone precipitation, respectively. When comparing the protein class categories in both methods, there were three additional categories for proteins identified using CytoBuster (TM) reagent. The proteins were related to scaffold/adaptor protein (PC00226), protein binding activity modulator (PC00095) and intercellular signal molecule (PC00207). In conclusion, the CytoBuster (TM) protein extraction reagent showed a better performance for the extraction of proteins in term of the protein yield, proteome coverage and extraction speed.</description><identifier>ISSN: 2167-8359</identifier><identifier>EISSN: 2167-8359</identifier><identifier>DOI: 10.7717/peerj.10863</identifier><identifier>PMID: 33717682</identifier><language>eng</language><publisher>LONDON: Peerj Inc</publisher><subject>Acetone ; Aedes aegypti ; Analysis ; Biochemistry ; Culicidae ; Disease transmission ; Drug resistance in microorganisms ; Entomology ; Ethylenediaminetetraacetic acid ; Female Aedes aegypti ; Functional analysis ; Insecticides ; LC-ESI-MS/MS ; Mass spectrometry ; Mass spectroscopy ; Methods ; Mosquitoes ; Multidisciplinary Sciences ; Nutrients ; Pathogens ; Peptides ; Pesticide resistance ; Physiological aspects ; Physiology ; Protein binding ; Protein extraction methods ; Protein identification ; Proteins ; Proteomes ; Proteomics ; Reagents ; Science & Technology ; Science & Technology - Other Topics ; Scientific imaging ; Solvents</subject><ispartof>PeerJ (San Francisco, CA), 2021-03, Vol.9, p.e10863-e10863, Article 10863</ispartof><rights>2021 Shettima et al.</rights><rights>COPYRIGHT 2021 PeerJ. Ltd.</rights><rights>2021 Shettima et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021 Shettima et al. 2021 Shettima et al.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>1</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000624914800003</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c573t-1bc993502765e620b1cb284f2c61353cd9c756bea2af758afea8cbbf9cf060103</citedby><cites>FETCH-LOGICAL-c573t-1bc993502765e620b1cb284f2c61353cd9c756bea2af758afea8cbbf9cf060103</cites><orcidid>0000-0002-6944-5046</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7936558/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7936558/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2114,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33717682$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shettima, Abubakar</creatorcontrib><creatorcontrib>Ishak, Intan H.</creatorcontrib><creatorcontrib>Rais, Syahirah Hanisah Abdul</creatorcontrib><creatorcontrib>Abu Hasan, Hadura</creatorcontrib><creatorcontrib>Othman, Nurulhasanah</creatorcontrib><title>Evaluation of female Aedes aegypti proteome via LC-ESI-MS/MS using two protein extraction methods</title><title>PeerJ (San Francisco, CA)</title><addtitle>PEERJ</addtitle><addtitle>PeerJ</addtitle><description>Background. Proteomic analyses have broadened the horizons of vector control measures by identifying proteins associated with different biological and physiological processes and give further insight into the mosquitoes' biology, mechanism of insecticide resistance and pathogens-mosquitoes interaction. Female Ae. aegypti ingests human blood to acquire the requisite nutrients to make eggs. During blood ingestion, female mosquitoes transmit different pathogens. Therefore, this study aimed to determine the best protein extraction method for mass spectrometry analysis which will allow a better proteome profiling for female mosquitoes.
Methods. In this present study, two protein extractions methods were performed to analyze female Ae. aegyti proteome, via TCA acetone precipitation extraction method and a commercial protein extraction reagent CytoBuster (TM). Then, protein identification was performed by LC-ESI-MS/MS and followed by functional protein annotation analysis.
Results. The CytoBuster (TM) reagent gave the highest protein yield with a mean of 475.90 its compared to TCA acetone precipitation extraction showed 283.15 mu g mean of protein. LC-ESI-MS/MS identified 1,290 and 890 proteins from the CytoBusterTM reagent and TCA acetone precipitation, respectively. When comparing the protein class categories in both methods, there were three additional categories for proteins identified using CytoBuster (TM) reagent. The proteins were related to scaffold/adaptor protein (PC00226), protein binding activity modulator (PC00095) and intercellular signal molecule (PC00207). In conclusion, the CytoBuster (TM) protein extraction reagent showed a better performance for the extraction of proteins in term of the protein yield, proteome coverage and extraction speed.</description><subject>Acetone</subject><subject>Aedes aegypti</subject><subject>Analysis</subject><subject>Biochemistry</subject><subject>Culicidae</subject><subject>Disease transmission</subject><subject>Drug resistance in microorganisms</subject><subject>Entomology</subject><subject>Ethylenediaminetetraacetic acid</subject><subject>Female Aedes aegypti</subject><subject>Functional analysis</subject><subject>Insecticides</subject><subject>LC-ESI-MS/MS</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Methods</subject><subject>Mosquitoes</subject><subject>Multidisciplinary Sciences</subject><subject>Nutrients</subject><subject>Pathogens</subject><subject>Peptides</subject><subject>Pesticide resistance</subject><subject>Physiological aspects</subject><subject>Physiology</subject><subject>Protein binding</subject><subject>Protein extraction methods</subject><subject>Protein identification</subject><subject>Proteins</subject><subject>Proteomes</subject><subject>Proteomics</subject><subject>Reagents</subject><subject>Science & Technology</subject><subject>Science & Technology - Other Topics</subject><subject>Scientific imaging</subject><subject>Solvents</subject><issn>2167-8359</issn><issn>2167-8359</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>HGBXW</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNks1r2zAYh83YWEvX0-7DMBiF4VQf1ocvgxCyLZCyQ7azkOVXiYJtZZadrv_95KRrk7HD7IOF_LwP0vv-kuQtRhMhsLjdAXTbCUaS0xfJJcFcZJKy4uXJ-iK5DmGL4iMJR5K-Ti4ojbVckstEz_e6HnTvfJt6m1podA3pFCoIqYb1w6536a7zPfgG0r3T6XKWzVeL7G51e7dKh-Daddrf-yPj2hR-9Z02B10D_cZX4U3yyuo6wPXj9yr58Xn-ffY1W377sphNl5lhgvYZLk1RUIaI4Aw4QSU2JZG5JYZjyqipCiMYL0ETbQWT2oKWpixtYSziCCN6lSyO3srrrdp1rtHdg_LaqcOG79ZKd70zNShR5SwqUMlKmRuWyxwjoquKWku1yGl0fTq6dkPZQGWgjbeqz6Tnf1q3UWu_V6KgPKqj4OZR0PmfA4ReNS4YqGvdgh-CIgzhXBSIj-j7v9CtH7o2tkqRvBAkHgfTZ2od56Nca_3Y51GqppxRHidKRKQm_6DiW0HjjG_Burh_VvDhpGADuu43wdfDOMBwDn48gqbzIXRgn5qBkRqTqA5JVIckRvrdaf-e2D-5i4A8AvdQehuMg9bAExajyuPdcS7H1NKZ6w8Bnfmh7Z9P8j-l9DfhUPfj</recordid><startdate>20210303</startdate><enddate>20210303</enddate><creator>Shettima, Abubakar</creator><creator>Ishak, Intan H.</creator><creator>Rais, Syahirah Hanisah Abdul</creator><creator>Abu Hasan, Hadura</creator><creator>Othman, Nurulhasanah</creator><general>Peerj Inc</general><general>PeerJ. Ltd</general><general>PeerJ, Inc</general><general>PeerJ Inc</general><scope>BLEPL</scope><scope>DTL</scope><scope>HGBXW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7XB</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-6944-5046</orcidid></search><sort><creationdate>20210303</creationdate><title>Evaluation of female Aedes aegypti proteome via LC-ESI-MS/MS using two protein extraction methods</title><author>Shettima, Abubakar ; Ishak, Intan H. ; Rais, Syahirah Hanisah Abdul ; Abu Hasan, Hadura ; Othman, Nurulhasanah</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c573t-1bc993502765e620b1cb284f2c61353cd9c756bea2af758afea8cbbf9cf060103</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Acetone</topic><topic>Aedes aegypti</topic><topic>Analysis</topic><topic>Biochemistry</topic><topic>Culicidae</topic><topic>Disease transmission</topic><topic>Drug resistance in microorganisms</topic><topic>Entomology</topic><topic>Ethylenediaminetetraacetic acid</topic><topic>Female Aedes aegypti</topic><topic>Functional analysis</topic><topic>Insecticides</topic><topic>LC-ESI-MS/MS</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Methods</topic><topic>Mosquitoes</topic><topic>Multidisciplinary Sciences</topic><topic>Nutrients</topic><topic>Pathogens</topic><topic>Peptides</topic><topic>Pesticide resistance</topic><topic>Physiological aspects</topic><topic>Physiology</topic><topic>Protein binding</topic><topic>Protein extraction methods</topic><topic>Protein identification</topic><topic>Proteins</topic><topic>Proteomes</topic><topic>Proteomics</topic><topic>Reagents</topic><topic>Science & Technology</topic><topic>Science & Technology - Other Topics</topic><topic>Scientific imaging</topic><topic>Solvents</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shettima, Abubakar</creatorcontrib><creatorcontrib>Ishak, Intan H.</creatorcontrib><creatorcontrib>Rais, Syahirah Hanisah Abdul</creatorcontrib><creatorcontrib>Abu Hasan, Hadura</creatorcontrib><creatorcontrib>Othman, Nurulhasanah</creatorcontrib><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - Science Citation Index Expanded - 2021</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Access via ProQuest (Open Access)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PeerJ (San Francisco, CA)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shettima, Abubakar</au><au>Ishak, Intan H.</au><au>Rais, Syahirah Hanisah Abdul</au><au>Abu Hasan, Hadura</au><au>Othman, Nurulhasanah</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evaluation of female Aedes aegypti proteome via LC-ESI-MS/MS using two protein extraction methods</atitle><jtitle>PeerJ (San Francisco, CA)</jtitle><stitle>PEERJ</stitle><addtitle>PeerJ</addtitle><date>2021-03-03</date><risdate>2021</risdate><volume>9</volume><spage>e10863</spage><epage>e10863</epage><pages>e10863-e10863</pages><artnum>10863</artnum><artnum>e10863</artnum><issn>2167-8359</issn><eissn>2167-8359</eissn><abstract>Background. Proteomic analyses have broadened the horizons of vector control measures by identifying proteins associated with different biological and physiological processes and give further insight into the mosquitoes' biology, mechanism of insecticide resistance and pathogens-mosquitoes interaction. Female Ae. aegypti ingests human blood to acquire the requisite nutrients to make eggs. During blood ingestion, female mosquitoes transmit different pathogens. Therefore, this study aimed to determine the best protein extraction method for mass spectrometry analysis which will allow a better proteome profiling for female mosquitoes.
Methods. In this present study, two protein extractions methods were performed to analyze female Ae. aegyti proteome, via TCA acetone precipitation extraction method and a commercial protein extraction reagent CytoBuster (TM). Then, protein identification was performed by LC-ESI-MS/MS and followed by functional protein annotation analysis.
Results. The CytoBuster (TM) reagent gave the highest protein yield with a mean of 475.90 its compared to TCA acetone precipitation extraction showed 283.15 mu g mean of protein. LC-ESI-MS/MS identified 1,290 and 890 proteins from the CytoBusterTM reagent and TCA acetone precipitation, respectively. When comparing the protein class categories in both methods, there were three additional categories for proteins identified using CytoBuster (TM) reagent. The proteins were related to scaffold/adaptor protein (PC00226), protein binding activity modulator (PC00095) and intercellular signal molecule (PC00207). In conclusion, the CytoBuster (TM) protein extraction reagent showed a better performance for the extraction of proteins in term of the protein yield, proteome coverage and extraction speed.</abstract><cop>LONDON</cop><pub>Peerj Inc</pub><pmid>33717682</pmid><doi>10.7717/peerj.10863</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0002-6944-5046</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Acetone Aedes aegypti Analysis Biochemistry Culicidae Disease transmission Drug resistance in microorganisms Entomology Ethylenediaminetetraacetic acid Female Aedes aegypti Functional analysis Insecticides LC-ESI-MS/MS Mass spectrometry Mass spectroscopy Methods Mosquitoes Multidisciplinary Sciences Nutrients Pathogens Peptides Pesticide resistance Physiological aspects Physiology Protein binding Protein extraction methods Protein identification Proteins Proteomes Proteomics Reagents Science & Technology Science & Technology - Other Topics Scientific imaging Solvents |
| title | Evaluation of female Aedes aegypti proteome via LC-ESI-MS/MS using two protein extraction methods |
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