An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines
► Tetanus toxoid important conjugation for carbohydrate vaccines. ► Physical nature in solution needs elucidating. ► Sedimentation velocity shows small (∼14%) dimerization. ► Dimers not in reversible equilibrium. ► Overall asymmetric conformation. Tetanus toxoid protein has been characterized with r...
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| Veröffentlicht in: | Carbohydrate polymers 2012-11, Vol.90 (4), p.1831-1835 |
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| creator | Abdelhameed, Ali Saber Morris, Gordon A. Adams, Gary G. Rowe, Arthur J. Laloux, Olivier Cerny, Louis Bonnier, Benjamin Duvivier, Pierre Conrath, Karel Lenfant, Christophe Harding, Stephen E. |
| description | ► Tetanus toxoid important conjugation for carbohydrate vaccines. ► Physical nature in solution needs elucidating. ► Sedimentation velocity shows small (∼14%) dimerization. ► Dimers not in reversible equilibrium. ► Overall asymmetric conformation.
Tetanus toxoid protein has been characterized with regard oligomeric state and hydrodynamic (low-resolution) shape, important parameters with regard its use in glycoconjugate vaccines. From sedimentation velocity and sedimentation equilibrium analysis in the analytical ultracentrifuge tetanus toxoid protein is shown to be mostly monomeric in solution (∼86%) with approximately 14% dimer. The relative proportions do not appear to change significantly with concentration, suggesting the two components are not in reversible equilibrium. Hydrodynamic solution conformation studies based on high precision viscometry, combined with sedimentation data show the protein to be slightly extended conformation in solution with an aspect ratio ∼3. The asymmetric structure presents a greater surface area for conjugation with polysaccharide than a more globular structure, underpinning its popular choice as a conjugation protein for glycoconjugate vaccines. |
| doi_str_mv | 10.1016/j.carbpol.2012.07.032 |
| format | Article |
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Tetanus toxoid protein has been characterized with regard oligomeric state and hydrodynamic (low-resolution) shape, important parameters with regard its use in glycoconjugate vaccines. From sedimentation velocity and sedimentation equilibrium analysis in the analytical ultracentrifuge tetanus toxoid protein is shown to be mostly monomeric in solution (∼86%) with approximately 14% dimer. The relative proportions do not appear to change significantly with concentration, suggesting the two components are not in reversible equilibrium. Hydrodynamic solution conformation studies based on high precision viscometry, combined with sedimentation data show the protein to be slightly extended conformation in solution with an aspect ratio ∼3. The asymmetric structure presents a greater surface area for conjugation with polysaccharide than a more globular structure, underpinning its popular choice as a conjugation protein for glycoconjugate vaccines.</description><identifier>ISSN: 0144-8617</identifier><identifier>EISSN: 1879-1344</identifier><identifier>DOI: 10.1016/j.carbpol.2012.07.032</identifier><identifier>PMID: 22944454</identifier><identifier>CODEN: CAPOD8</identifier><language>eng</language><publisher>Kidlington: Elsevier Ltd</publisher><subject>Analytical ultracentrifugation ; Analytical, structural and metabolic biochemistry ; Applied sciences ; Biological and medical sciences ; Chromatography, Gel ; Exact sciences and technology ; Fundamental and applied biological sciences. Psychology ; Glycoconjugates ; Hydrodynamics ; Miscellaneous ; Molecular Weight ; Natural polymers ; Physicochemistry of polymers ; polysaccharides ; Protein Multimerization ; Proteins ; Scattering, Small Angle ; Solution conformation ; surface area ; tetanus ; Tetanus Toxoid - chemistry ; Ultracentrifugation ; vaccines ; Vaccines, Conjugate - chemistry ; viscometry ; Viscosity</subject><ispartof>Carbohydrate polymers, 2012-11, Vol.90 (4), p.1831-1835</ispartof><rights>2012 Elsevier Ltd</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2012 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c419t-8db4d8f8ab5c985d41a2735e6cb3d5bd567a543ad5e5464625cdbf9f77bd72563</citedby><cites>FETCH-LOGICAL-c419t-8db4d8f8ab5c985d41a2735e6cb3d5bd567a543ad5e5464625cdbf9f77bd72563</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.carbpol.2012.07.032$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26341752$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22944454$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Abdelhameed, Ali Saber</creatorcontrib><creatorcontrib>Morris, Gordon A.</creatorcontrib><creatorcontrib>Adams, Gary G.</creatorcontrib><creatorcontrib>Rowe, Arthur J.</creatorcontrib><creatorcontrib>Laloux, Olivier</creatorcontrib><creatorcontrib>Cerny, Louis</creatorcontrib><creatorcontrib>Bonnier, Benjamin</creatorcontrib><creatorcontrib>Duvivier, Pierre</creatorcontrib><creatorcontrib>Conrath, Karel</creatorcontrib><creatorcontrib>Lenfant, Christophe</creatorcontrib><creatorcontrib>Harding, Stephen E.</creatorcontrib><title>An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines</title><title>Carbohydrate polymers</title><addtitle>Carbohydr Polym</addtitle><description>► Tetanus toxoid important conjugation for carbohydrate vaccines. ► Physical nature in solution needs elucidating. ► Sedimentation velocity shows small (∼14%) dimerization. ► Dimers not in reversible equilibrium. ► Overall asymmetric conformation.
Tetanus toxoid protein has been characterized with regard oligomeric state and hydrodynamic (low-resolution) shape, important parameters with regard its use in glycoconjugate vaccines. From sedimentation velocity and sedimentation equilibrium analysis in the analytical ultracentrifuge tetanus toxoid protein is shown to be mostly monomeric in solution (∼86%) with approximately 14% dimer. The relative proportions do not appear to change significantly with concentration, suggesting the two components are not in reversible equilibrium. Hydrodynamic solution conformation studies based on high precision viscometry, combined with sedimentation data show the protein to be slightly extended conformation in solution with an aspect ratio ∼3. The asymmetric structure presents a greater surface area for conjugation with polysaccharide than a more globular structure, underpinning its popular choice as a conjugation protein for glycoconjugate vaccines.</description><subject>Analytical ultracentrifugation</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Applied sciences</subject><subject>Biological and medical sciences</subject><subject>Chromatography, Gel</subject><subject>Exact sciences and technology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoconjugates</subject><subject>Hydrodynamics</subject><subject>Miscellaneous</subject><subject>Molecular Weight</subject><subject>Natural polymers</subject><subject>Physicochemistry of polymers</subject><subject>polysaccharides</subject><subject>Protein Multimerization</subject><subject>Proteins</subject><subject>Scattering, Small Angle</subject><subject>Solution conformation</subject><subject>surface area</subject><subject>tetanus</subject><subject>Tetanus Toxoid - chemistry</subject><subject>Ultracentrifugation</subject><subject>vaccines</subject><subject>Vaccines, Conjugate - chemistry</subject><subject>viscometry</subject><subject>Viscosity</subject><issn>0144-8617</issn><issn>1879-1344</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAQgC0EotvCTwB8QeolwW8nJ1RVvKRKHKBny7EnW6-SeLGdiuXX49UucGQuI42-eegbhF5R0lJC1btd62wa9nFqGaGsJbolnD1BG9rpvqFciKdoQ6gQTaeovkCXOe9IDUXJc3TBWC-EkGKD5psF23yYZygpOGwXj_MUtg9lOmAfZkjhF9RSSasrawI8xoTLA-ACxS5rxiX-jMHjfYoFwoLXXOmat9PBRReX3bq1BfCjdS4skF-gZ6OdMrw85yt0__HD99vPzd3XT19ub-4aJ2hfms4PwndjZwfp-k56QS3TXIJyA_dy8FJpKwW3XoIUSigmnR_GftR68JpJxa_Q9WluvevHCrmYOWQH02QXiGs2lPCOaMpIV1F5Ql2KOScYzT6F2aZDhczRtNmZs2lzNG2INtV07Xt9XrEOM_i_XX_UVuDtGbDZ2WlMdnEh_-MUF1TL46A3J2600dhtqsz9t7pJ1W9JyqWsxPsTAVXZY4BksguwOPAhgSvGx_CfY38DQrGqbw</recordid><startdate>20121106</startdate><enddate>20121106</enddate><creator>Abdelhameed, Ali Saber</creator><creator>Morris, Gordon A.</creator><creator>Adams, Gary G.</creator><creator>Rowe, Arthur J.</creator><creator>Laloux, Olivier</creator><creator>Cerny, Louis</creator><creator>Bonnier, Benjamin</creator><creator>Duvivier, Pierre</creator><creator>Conrath, Karel</creator><creator>Lenfant, Christophe</creator><creator>Harding, Stephen E.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><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></search><sort><creationdate>20121106</creationdate><title>An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines</title><author>Abdelhameed, Ali Saber ; Morris, Gordon A. ; Adams, Gary G. ; Rowe, Arthur J. ; Laloux, Olivier ; Cerny, Louis ; Bonnier, Benjamin ; Duvivier, Pierre ; Conrath, Karel ; Lenfant, Christophe ; Harding, Stephen E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c419t-8db4d8f8ab5c985d41a2735e6cb3d5bd567a543ad5e5464625cdbf9f77bd72563</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Analytical ultracentrifugation</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Applied sciences</topic><topic>Biological and medical sciences</topic><topic>Chromatography, Gel</topic><topic>Exact sciences and technology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoconjugates</topic><topic>Hydrodynamics</topic><topic>Miscellaneous</topic><topic>Molecular Weight</topic><topic>Natural polymers</topic><topic>Physicochemistry of polymers</topic><topic>polysaccharides</topic><topic>Protein Multimerization</topic><topic>Proteins</topic><topic>Scattering, Small Angle</topic><topic>Solution conformation</topic><topic>surface area</topic><topic>tetanus</topic><topic>Tetanus Toxoid - chemistry</topic><topic>Ultracentrifugation</topic><topic>vaccines</topic><topic>Vaccines, Conjugate - chemistry</topic><topic>viscometry</topic><topic>Viscosity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Abdelhameed, Ali Saber</creatorcontrib><creatorcontrib>Morris, Gordon A.</creatorcontrib><creatorcontrib>Adams, Gary G.</creatorcontrib><creatorcontrib>Rowe, Arthur J.</creatorcontrib><creatorcontrib>Laloux, Olivier</creatorcontrib><creatorcontrib>Cerny, Louis</creatorcontrib><creatorcontrib>Bonnier, Benjamin</creatorcontrib><creatorcontrib>Duvivier, Pierre</creatorcontrib><creatorcontrib>Conrath, Karel</creatorcontrib><creatorcontrib>Lenfant, Christophe</creatorcontrib><creatorcontrib>Harding, Stephen E.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><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>Carbohydrate polymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Abdelhameed, Ali Saber</au><au>Morris, Gordon A.</au><au>Adams, Gary G.</au><au>Rowe, Arthur J.</au><au>Laloux, Olivier</au><au>Cerny, Louis</au><au>Bonnier, Benjamin</au><au>Duvivier, Pierre</au><au>Conrath, Karel</au><au>Lenfant, Christophe</au><au>Harding, Stephen E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines</atitle><jtitle>Carbohydrate polymers</jtitle><addtitle>Carbohydr Polym</addtitle><date>2012-11-06</date><risdate>2012</risdate><volume>90</volume><issue>4</issue><spage>1831</spage><epage>1835</epage><pages>1831-1835</pages><issn>0144-8617</issn><eissn>1879-1344</eissn><coden>CAPOD8</coden><abstract>► Tetanus toxoid important conjugation for carbohydrate vaccines. ► Physical nature in solution needs elucidating. ► Sedimentation velocity shows small (∼14%) dimerization. ► Dimers not in reversible equilibrium. ► Overall asymmetric conformation.
Tetanus toxoid protein has been characterized with regard oligomeric state and hydrodynamic (low-resolution) shape, important parameters with regard its use in glycoconjugate vaccines. From sedimentation velocity and sedimentation equilibrium analysis in the analytical ultracentrifuge tetanus toxoid protein is shown to be mostly monomeric in solution (∼86%) with approximately 14% dimer. The relative proportions do not appear to change significantly with concentration, suggesting the two components are not in reversible equilibrium. Hydrodynamic solution conformation studies based on high precision viscometry, combined with sedimentation data show the protein to be slightly extended conformation in solution with an aspect ratio ∼3. The asymmetric structure presents a greater surface area for conjugation with polysaccharide than a more globular structure, underpinning its popular choice as a conjugation protein for glycoconjugate vaccines.</abstract><cop>Kidlington</cop><pub>Elsevier Ltd</pub><pmid>22944454</pmid><doi>10.1016/j.carbpol.2012.07.032</doi><tpages>5</tpages></addata></record> |
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| subjects | Analytical ultracentrifugation Analytical, structural and metabolic biochemistry Applied sciences Biological and medical sciences Chromatography, Gel Exact sciences and technology Fundamental and applied biological sciences. Psychology Glycoconjugates Hydrodynamics Miscellaneous Molecular Weight Natural polymers Physicochemistry of polymers polysaccharides Protein Multimerization Proteins Scattering, Small Angle Solution conformation surface area tetanus Tetanus Toxoid - chemistry Ultracentrifugation vaccines Vaccines, Conjugate - chemistry viscometry Viscosity |
| title | An asymmetric and slightly dimerized structure for the tetanus toxoid protein used in glycoconjugate vaccines |
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