Loading…
Mosquito cell line glycoproteins: an unsuitable model system for the Plasmodium ookinete-mosquito midgut interaction?
BACKGROUND: Mosquito midgut glycoproteins may act as key recognition sites for the invading malarial ookinete. Effective transmission blocking strategies require the identification of novel target molecules. We have partially characterised the surface glycoproteins of two cell lines from two mosquit...
Saved in:
Published in: | Parasites & vectors 2010-03, Vol.3 (1), p.22-22 |
---|---|
Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-b665t-853ff1072288cefe12cb3fb74cce1e6d476faa706e65a8bbe399dc757db08cc43 |
---|---|
cites | |
container_end_page | 22 |
container_issue | 1 |
container_start_page | 22 |
container_title | Parasites & vectors |
container_volume | 3 |
creator | Wilkins, Simon Billingsley, Peter F |
description | BACKGROUND: Mosquito midgut glycoproteins may act as key recognition sites for the invading malarial ookinete. Effective transmission blocking strategies require the identification of novel target molecules. We have partially characterised the surface glycoproteins of two cell lines from two mosquito species; Anopheles stephensi and Anopheles gambiae, and investigated the binding of Plasmodium berghei ookinetes to carbohydrate ligands on the cells. Cell line extracts were run on SDS-PAGE gels and carbohydrate moieties determined by blotting against a range of biotinylated lectins. In addition, specific glycosidases were used to cleave the oligosaccharides. RESULTS: An. stephensi 43 and An. gambiae 55 cell line glycoproteins expressed oligosaccharides containing oligomannose and hybrid oligosaccharides, with and without α1-6 core fucosylation; N-linked oligosaccharides with terminal Galβ1-3GalNAc or GalNAcβ1-3Gal; O-linked α/βGalNAc. An. stephensi 43 cell line glycoproteins also expressed N-linked Galβ1-4R and O-linked Galβ1-3GalNAc. Although P. berghei ookinetes bound to both mosquito cell lines, binding could not be inhibited by GlcNAc, GalNAc or Galactose. CONCLUSIONS: Anopheline cell lines displayed a limited range of oligosaccharides. Differences between the glycosylation patterns of the cell lines and mosquito midgut epithelial cells could be a factor why ookinetes did not bind in a carbohydrate inhibitable manner. Anopheline cell lines are not suitable as a potential model system for carbohydrate-mediated adhesion of Plasmodium ookinetes. |
doi_str_mv | 10.1186/1756-3305-3-22 |
format | article |
fullrecord | <record><control><sourceid>gale_doaj_</sourceid><recordid>TN_cdi_doaj_primary_oai_doaj_org_article_da3eb99ee20c4fcaa9be0943e87891c6</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A225103689</galeid><doaj_id>oai_doaj_org_article_da3eb99ee20c4fcaa9be0943e87891c6</doaj_id><sourcerecordid>A225103689</sourcerecordid><originalsourceid>FETCH-LOGICAL-b665t-853ff1072288cefe12cb3fb74cce1e6d476faa706e65a8bbe399dc757db08cc43</originalsourceid><addsrcrecordid>eNp1kktv1DAQgCMEoqVw5QgRHBCHFD8S2-kBtKp4rFQEovRsOc449ZLEW9tB7L_HYdtVF4p8sDXz-bM1M1n2FKNjjAV7g3nFCkpRVdCCkHvZ4S5w_9b5IHsUwgohhuqKPcwOCKJUoIodZtNnF64mG12uoe_z3o6Qd_1Gu7V3EewYTnI15tMYEqOaHvLBtdDnYRMiDLlxPo-XkH_tVUgJOw25cz-SI0Ix3IgH23ZTzO0YwSsdrRvfPc4eGNUHeHK9H2UXH95_P_1UnH35uDxdnBUNY1UsREWNwYgTIoQGA5johpqGl1oDBtaWnBmlOGLAKiWaBmhdt5pXvG2Q0LqkR9ly622dWsm1t4PyG-mUlX8CzndS-Wh1D7JVFJq6BiBIl0YrVTeA6pKC4KLGmiXX261rPTUDtBrG6FW_J93PjPZSdu6nJIJhxmbBYitorPuPYD-j3SDnFsq5hZJKQpLj1fUnvLuaIEQ52DB3To3gpiA5pTUtGeeJfPEXuXKTH1O1ZY1ISQnHOEEvt1CnUgnsaFx6WM9KuSCkwogyUSfq-A4qrRYGq90Ixqb43oXXexcSE-FX7NQUglyef7tTrr0LwYPZFQQjOY_4vyV4drsPO_xmphPwfAsY5aTqvA3y4pwgXCGEhKhRSX8D1uQCBg</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>902432711</pqid></control><display><type>article</type><title>Mosquito cell line glycoproteins: an unsuitable model system for the Plasmodium ookinete-mosquito midgut interaction?</title><source>Publicly Available Content Database</source><source>PubMed Central</source><creator>Wilkins, Simon ; Billingsley, Peter F</creator><creatorcontrib>Wilkins, Simon ; Billingsley, Peter F</creatorcontrib><description>BACKGROUND: Mosquito midgut glycoproteins may act as key recognition sites for the invading malarial ookinete. Effective transmission blocking strategies require the identification of novel target molecules. We have partially characterised the surface glycoproteins of two cell lines from two mosquito species; Anopheles stephensi and Anopheles gambiae, and investigated the binding of Plasmodium berghei ookinetes to carbohydrate ligands on the cells. Cell line extracts were run on SDS-PAGE gels and carbohydrate moieties determined by blotting against a range of biotinylated lectins. In addition, specific glycosidases were used to cleave the oligosaccharides. RESULTS: An. stephensi 43 and An. gambiae 55 cell line glycoproteins expressed oligosaccharides containing oligomannose and hybrid oligosaccharides, with and without α1-6 core fucosylation; N-linked oligosaccharides with terminal Galβ1-3GalNAc or GalNAcβ1-3Gal; O-linked α/βGalNAc. An. stephensi 43 cell line glycoproteins also expressed N-linked Galβ1-4R and O-linked Galβ1-3GalNAc. Although P. berghei ookinetes bound to both mosquito cell lines, binding could not be inhibited by GlcNAc, GalNAc or Galactose. CONCLUSIONS: Anopheline cell lines displayed a limited range of oligosaccharides. Differences between the glycosylation patterns of the cell lines and mosquito midgut epithelial cells could be a factor why ookinetes did not bind in a carbohydrate inhibitable manner. Anopheline cell lines are not suitable as a potential model system for carbohydrate-mediated adhesion of Plasmodium ookinetes.</description><identifier>ISSN: 1756-3305</identifier><identifier>EISSN: 1756-3305</identifier><identifier>DOI: 10.1186/1756-3305-3-22</identifier><identifier>PMID: 20338056</identifier><language>eng</language><publisher>England: Springer-Verlag</publisher><subject>adhesion ; Anopheles gambiae ; Anopheles stephensi ; Carbohydrates ; Care and treatment ; epithelial cells ; Galactose ; Glycoproteins ; glycosidases ; glycosylation ; Health aspects ; hybrids ; Lectins ; Ligands ; Malaria ; midgut ; Mosquitoes ; oligosaccharides ; ookinetes ; Parasites ; Physiological aspects ; Plasmodium berghei ; polyacrylamide gel electrophoresis ; Standard deviation ; Vaccines</subject><ispartof>Parasites & vectors, 2010-03, Vol.3 (1), p.22-22</ispartof><rights>COPYRIGHT 2010 BioMed Central Ltd.</rights><rights>2010 Wilkins and Billingsley; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</rights><rights>Copyright ©2010 Wilkins and Billingsley; licensee BioMed Central Ltd. 2010 Wilkins and Billingsley; licensee BioMed Central Ltd.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-b665t-853ff1072288cefe12cb3fb74cce1e6d476faa706e65a8bbe399dc757db08cc43</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2861666/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/902432711?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20338056$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wilkins, Simon</creatorcontrib><creatorcontrib>Billingsley, Peter F</creatorcontrib><title>Mosquito cell line glycoproteins: an unsuitable model system for the Plasmodium ookinete-mosquito midgut interaction?</title><title>Parasites & vectors</title><addtitle>Parasit Vectors</addtitle><description>BACKGROUND: Mosquito midgut glycoproteins may act as key recognition sites for the invading malarial ookinete. Effective transmission blocking strategies require the identification of novel target molecules. We have partially characterised the surface glycoproteins of two cell lines from two mosquito species; Anopheles stephensi and Anopheles gambiae, and investigated the binding of Plasmodium berghei ookinetes to carbohydrate ligands on the cells. Cell line extracts were run on SDS-PAGE gels and carbohydrate moieties determined by blotting against a range of biotinylated lectins. In addition, specific glycosidases were used to cleave the oligosaccharides. RESULTS: An. stephensi 43 and An. gambiae 55 cell line glycoproteins expressed oligosaccharides containing oligomannose and hybrid oligosaccharides, with and without α1-6 core fucosylation; N-linked oligosaccharides with terminal Galβ1-3GalNAc or GalNAcβ1-3Gal; O-linked α/βGalNAc. An. stephensi 43 cell line glycoproteins also expressed N-linked Galβ1-4R and O-linked Galβ1-3GalNAc. Although P. berghei ookinetes bound to both mosquito cell lines, binding could not be inhibited by GlcNAc, GalNAc or Galactose. CONCLUSIONS: Anopheline cell lines displayed a limited range of oligosaccharides. Differences between the glycosylation patterns of the cell lines and mosquito midgut epithelial cells could be a factor why ookinetes did not bind in a carbohydrate inhibitable manner. Anopheline cell lines are not suitable as a potential model system for carbohydrate-mediated adhesion of Plasmodium ookinetes.</description><subject>adhesion</subject><subject>Anopheles gambiae</subject><subject>Anopheles stephensi</subject><subject>Carbohydrates</subject><subject>Care and treatment</subject><subject>epithelial cells</subject><subject>Galactose</subject><subject>Glycoproteins</subject><subject>glycosidases</subject><subject>glycosylation</subject><subject>Health aspects</subject><subject>hybrids</subject><subject>Lectins</subject><subject>Ligands</subject><subject>Malaria</subject><subject>midgut</subject><subject>Mosquitoes</subject><subject>oligosaccharides</subject><subject>ookinetes</subject><subject>Parasites</subject><subject>Physiological aspects</subject><subject>Plasmodium berghei</subject><subject>polyacrylamide gel electrophoresis</subject><subject>Standard deviation</subject><subject>Vaccines</subject><issn>1756-3305</issn><issn>1756-3305</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNp1kktv1DAQgCMEoqVw5QgRHBCHFD8S2-kBtKp4rFQEovRsOc449ZLEW9tB7L_HYdtVF4p8sDXz-bM1M1n2FKNjjAV7g3nFCkpRVdCCkHvZ4S5w_9b5IHsUwgohhuqKPcwOCKJUoIodZtNnF64mG12uoe_z3o6Qd_1Gu7V3EewYTnI15tMYEqOaHvLBtdDnYRMiDLlxPo-XkH_tVUgJOw25cz-SI0Ix3IgH23ZTzO0YwSsdrRvfPc4eGNUHeHK9H2UXH95_P_1UnH35uDxdnBUNY1UsREWNwYgTIoQGA5johpqGl1oDBtaWnBmlOGLAKiWaBmhdt5pXvG2Q0LqkR9ly622dWsm1t4PyG-mUlX8CzndS-Wh1D7JVFJq6BiBIl0YrVTeA6pKC4KLGmiXX261rPTUDtBrG6FW_J93PjPZSdu6nJIJhxmbBYitorPuPYD-j3SDnFsq5hZJKQpLj1fUnvLuaIEQ52DB3To3gpiA5pTUtGeeJfPEXuXKTH1O1ZY1ISQnHOEEvt1CnUgnsaFx6WM9KuSCkwogyUSfq-A4qrRYGq90Ixqb43oXXexcSE-FX7NQUglyef7tTrr0LwYPZFQQjOY_4vyV4drsPO_xmphPwfAsY5aTqvA3y4pwgXCGEhKhRSX8D1uQCBg</recordid><startdate>20100325</startdate><enddate>20100325</enddate><creator>Wilkins, Simon</creator><creator>Billingsley, Peter F</creator><general>Springer-Verlag</general><general>BioMed Central Ltd</general><general>BioMed Central</general><general>BMC</general><scope>FBQ</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope><scope>3V.</scope><scope>7SN</scope><scope>7SS</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>H95</scope><scope>K9.</scope><scope>L.G</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20100325</creationdate><title>Mosquito cell line glycoproteins: an unsuitable model system for the Plasmodium ookinete-mosquito midgut interaction?</title><author>Wilkins, Simon ; Billingsley, Peter F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-b665t-853ff1072288cefe12cb3fb74cce1e6d476faa706e65a8bbe399dc757db08cc43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>adhesion</topic><topic>Anopheles gambiae</topic><topic>Anopheles stephensi</topic><topic>Carbohydrates</topic><topic>Care and treatment</topic><topic>epithelial cells</topic><topic>Galactose</topic><topic>Glycoproteins</topic><topic>glycosidases</topic><topic>glycosylation</topic><topic>Health aspects</topic><topic>hybrids</topic><topic>Lectins</topic><topic>Ligands</topic><topic>Malaria</topic><topic>midgut</topic><topic>Mosquitoes</topic><topic>oligosaccharides</topic><topic>ookinetes</topic><topic>Parasites</topic><topic>Physiological aspects</topic><topic>Plasmodium berghei</topic><topic>polyacrylamide gel electrophoresis</topic><topic>Standard deviation</topic><topic>Vaccines</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wilkins, Simon</creatorcontrib><creatorcontrib>Billingsley, Peter F</creatorcontrib><collection>AGRIS</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale in Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Publicly Available Content Database</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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Directory of Open Access Journals</collection><jtitle>Parasites & vectors</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wilkins, Simon</au><au>Billingsley, Peter F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mosquito cell line glycoproteins: an unsuitable model system for the Plasmodium ookinete-mosquito midgut interaction?</atitle><jtitle>Parasites & vectors</jtitle><addtitle>Parasit Vectors</addtitle><date>2010-03-25</date><risdate>2010</risdate><volume>3</volume><issue>1</issue><spage>22</spage><epage>22</epage><pages>22-22</pages><issn>1756-3305</issn><eissn>1756-3305</eissn><abstract>BACKGROUND: Mosquito midgut glycoproteins may act as key recognition sites for the invading malarial ookinete. Effective transmission blocking strategies require the identification of novel target molecules. We have partially characterised the surface glycoproteins of two cell lines from two mosquito species; Anopheles stephensi and Anopheles gambiae, and investigated the binding of Plasmodium berghei ookinetes to carbohydrate ligands on the cells. Cell line extracts were run on SDS-PAGE gels and carbohydrate moieties determined by blotting against a range of biotinylated lectins. In addition, specific glycosidases were used to cleave the oligosaccharides. RESULTS: An. stephensi 43 and An. gambiae 55 cell line glycoproteins expressed oligosaccharides containing oligomannose and hybrid oligosaccharides, with and without α1-6 core fucosylation; N-linked oligosaccharides with terminal Galβ1-3GalNAc or GalNAcβ1-3Gal; O-linked α/βGalNAc. An. stephensi 43 cell line glycoproteins also expressed N-linked Galβ1-4R and O-linked Galβ1-3GalNAc. Although P. berghei ookinetes bound to both mosquito cell lines, binding could not be inhibited by GlcNAc, GalNAc or Galactose. CONCLUSIONS: Anopheline cell lines displayed a limited range of oligosaccharides. Differences between the glycosylation patterns of the cell lines and mosquito midgut epithelial cells could be a factor why ookinetes did not bind in a carbohydrate inhibitable manner. Anopheline cell lines are not suitable as a potential model system for carbohydrate-mediated adhesion of Plasmodium ookinetes.</abstract><cop>England</cop><pub>Springer-Verlag</pub><pmid>20338056</pmid><doi>10.1186/1756-3305-3-22</doi><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1756-3305 |
ispartof | Parasites & vectors, 2010-03, Vol.3 (1), p.22-22 |
issn | 1756-3305 1756-3305 |
language | eng |
recordid | cdi_doaj_primary_oai_doaj_org_article_da3eb99ee20c4fcaa9be0943e87891c6 |
source | Publicly Available Content Database; PubMed Central |
subjects | adhesion Anopheles gambiae Anopheles stephensi Carbohydrates Care and treatment epithelial cells Galactose Glycoproteins glycosidases glycosylation Health aspects hybrids Lectins Ligands Malaria midgut Mosquitoes oligosaccharides ookinetes Parasites Physiological aspects Plasmodium berghei polyacrylamide gel electrophoresis Standard deviation Vaccines |
title | Mosquito cell line glycoproteins: an unsuitable model system for the Plasmodium ookinete-mosquito midgut interaction? |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-21T07%3A07%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_doaj_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Mosquito%20cell%20line%20glycoproteins:%20an%20unsuitable%20model%20system%20for%20the%20Plasmodium%20ookinete-mosquito%20midgut%20interaction?&rft.jtitle=Parasites%20&%20vectors&rft.au=Wilkins,%20Simon&rft.date=2010-03-25&rft.volume=3&rft.issue=1&rft.spage=22&rft.epage=22&rft.pages=22-22&rft.issn=1756-3305&rft.eissn=1756-3305&rft_id=info:doi/10.1186/1756-3305-3-22&rft_dat=%3Cgale_doaj_%3EA225103689%3C/gale_doaj_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-b665t-853ff1072288cefe12cb3fb74cce1e6d476faa706e65a8bbe399dc757db08cc43%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=902432711&rft_id=info:pmid/20338056&rft_galeid=A225103689&rfr_iscdi=true |