Loading…
Expression and Characterization of Recombinant, Tetrameric and Enzymatically Active Influenza Neuraminidase for the Setup of an Enzyme-Linked Lectin-Based Assay
Developing a universal influenza vaccine that induces broad spectrum and longer-term immunity has become an important potentially achievable target in influenza vaccine research and development. Hemagglutinin (HA) and neuraminidase (NA) are the two major influenza virus antigens. Although antibody r...
Saved in:
| Published in: | PloS one 2015-08, Vol.10 (8), p.e0135474-e0135474 |
|---|---|
| Main Authors: | , , , , , , , , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites 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-c758t-9615072984ddd496652cfd0efd17fb75359a87bb257162b1b972015d102b11013 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c758t-9615072984ddd496652cfd0efd17fb75359a87bb257162b1b972015d102b11013 |
| container_end_page | e0135474 |
| container_issue | 8 |
| container_start_page | e0135474 |
| container_title | PloS one |
| container_volume | 10 |
| creator | Prevato, Marua Ferlenghi, Ilaria Bonci, Alessandra Uematsu, Yasushi Anselmi, Giulia Giusti, Fabiola Bertholet, Sylvie Legay, Francois Telford, John Laird Settembre, Ethan C Maione, Domenico Cozzi, Roberta |
| description | Developing a universal influenza vaccine that induces broad spectrum and longer-term immunity has become an important potentially achievable target in influenza vaccine research and development. Hemagglutinin (HA) and neuraminidase (NA) are the two major influenza virus antigens. Although antibody responses against influenza virus are mainly directed toward HA, NA is reported to be more genetically stable; hence NA-based vaccines have the potential to be effective for longer time periods. NA-specific immunity has been shown to limit the spread of influenza virus, thus reducing disease symptoms and providing cross-protection against heterosubtypic viruses in mouse challenge experiments. The production of large quantities of highly pure and stable NA could be beneficial for the development of new antivirals, subunit-based vaccines, and novel diagnostic tools. In this study, recombinant NA (rNA) was produced in mammalian cells at high levels from both swine A/California/07/2009 (H1N1) and avian A/turkey/Turkey/01/2005 (H5N1) influenza viruses. Biochemical, structural, and immunological characterizations revealed that the soluble rNAs produced are tetrameric, enzymatically active and immunogenic, and finally they represent good alternatives to conventionally used sources of NA in the Enzyme-Linked Lectin Assay (ELLA). |
| doi_str_mv | 10.1371/journal.pone.0135474 |
| format | article |
| fullrecord | <record><control><sourceid>gale_plos_</sourceid><recordid>TN_cdi_plos_journals_1708528784</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A425761752</galeid><doaj_id>oai_doaj_org_article_b36f2c6624fd43618d895857a88d9b2b</doaj_id><sourcerecordid>A425761752</sourcerecordid><originalsourceid>FETCH-LOGICAL-c758t-9615072984ddd496652cfd0efd17fb75359a87bb257162b1b972015d102b11013</originalsourceid><addsrcrecordid>eNqNk99u0zAUxiMEYmPwBggiISGQaImd-E9ukEo1oFLFpG1wazn2SeuR2MVOpnVPw6PitN3Uol2gXCQ-_p3POZ_PSZKXKBujnKGPV673VjbjlbMwzlBOClY8So5RmeMRxVn-eO_7KHkWwlWWkZxT-jQ5whTzjDJ2nPw5vVl5CME4m0qr0-lSeqk68OZWdkPQ1ek5KNdWxkrbfUgvofOyjftqw5_a23UbSSWbZp1OVGeuIZ3ZuunB3sr0O_SRNtZoGSCtnU-7JaQX0PWrQVnarQCM5sb-Ap3OISrY0edI63QSglw_T57UsgnwYvc-SX58Ob2cfhvNz77OppP5SDHCu1FJEckYLnmhtS5KSglWtc6g1ojVFSM5KSVnVYUJQxRXqCoZzhDRKIsLFO07SV5vdVeNC2JnbhCIZZxgzngRidmW0E5eiZU3rfRr4aQRm4DzCyF9dKIBUeW0xopSXNS6yCnimpeEEyY512WFq6j1aXdaX7WgFdjoanMgerhjzVIs3LUoSF7ieI8nybudgHe_ewidaE1Q0DTSgus3_x0bIud8qOzNP-jD1e2ohYwFGFu7eK4aRMWkiK5RxAiO1PgBKj4aWqNiJ9Ymxg8S3h8kRKaDm24h-xDE7OL8_9mzn4fs2z12CbLplsE1_dCz4RAstqDyLgQP9b3JKBPDIN25IYZBErtBimmv9i_oPulucvK_luAZMw</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1708528784</pqid></control><display><type>article</type><title>Expression and Characterization of Recombinant, Tetrameric and Enzymatically Active Influenza Neuraminidase for the Setup of an Enzyme-Linked Lectin-Based Assay</title><source>Publicly Available Content Database</source><source>PubMed Central</source><creator>Prevato, Marua ; Ferlenghi, Ilaria ; Bonci, Alessandra ; Uematsu, Yasushi ; Anselmi, Giulia ; Giusti, Fabiola ; Bertholet, Sylvie ; Legay, Francois ; Telford, John Laird ; Settembre, Ethan C ; Maione, Domenico ; Cozzi, Roberta</creator><contributor>Ye, Zhiping</contributor><creatorcontrib>Prevato, Marua ; Ferlenghi, Ilaria ; Bonci, Alessandra ; Uematsu, Yasushi ; Anselmi, Giulia ; Giusti, Fabiola ; Bertholet, Sylvie ; Legay, Francois ; Telford, John Laird ; Settembre, Ethan C ; Maione, Domenico ; Cozzi, Roberta ; Ye, Zhiping</creatorcontrib><description>Developing a universal influenza vaccine that induces broad spectrum and longer-term immunity has become an important potentially achievable target in influenza vaccine research and development. Hemagglutinin (HA) and neuraminidase (NA) are the two major influenza virus antigens. Although antibody responses against influenza virus are mainly directed toward HA, NA is reported to be more genetically stable; hence NA-based vaccines have the potential to be effective for longer time periods. NA-specific immunity has been shown to limit the spread of influenza virus, thus reducing disease symptoms and providing cross-protection against heterosubtypic viruses in mouse challenge experiments. The production of large quantities of highly pure and stable NA could be beneficial for the development of new antivirals, subunit-based vaccines, and novel diagnostic tools. In this study, recombinant NA (rNA) was produced in mammalian cells at high levels from both swine A/California/07/2009 (H1N1) and avian A/turkey/Turkey/01/2005 (H5N1) influenza viruses. Biochemical, structural, and immunological characterizations revealed that the soluble rNAs produced are tetrameric, enzymatically active and immunogenic, and finally they represent good alternatives to conventionally used sources of NA in the Enzyme-Linked Lectin Assay (ELLA).</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0135474</identifier><identifier>PMID: 26280677</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Animal experimentation ; Animals ; Antibodies, Viral - immunology ; Antibody Formation - immunology ; Antigens ; Antigens, Viral - immunology ; Antiviral agents ; Avian influenza ; Birds ; Cell Line ; Chemical properties ; Cross Protection - immunology ; Cross Reactions - immunology ; Cross-protection ; Design ; Development and progression ; Diagnostic software ; Diagnostic systems ; Disease control ; Enzyme-Linked Immunospot Assay - methods ; Enzymes ; Exo-a-sialidase ; Female ; Gene expression ; Hemagglutinin Glycoproteins, Influenza Virus - immunology ; Hemagglutinins ; Immunity ; Immunogenicity ; Immunoglobulins ; Immunology ; Infections ; Influenza ; Influenza A Virus, H1N1 Subtype - immunology ; Influenza A Virus, H5N1 Subtype - immunology ; Influenza in Birds - immunology ; Influenza vaccines ; Influenza Vaccines - immunology ; Lectins ; Lectins - immunology ; Livestock ; Mammalian cells ; Mice ; Microscopy ; Molecular biology ; Neuraminidase - immunology ; Orthomyxoviridae Infections - immunology ; Pandemics ; R&D ; Recombinant Proteins - immunology ; Research & development ; Ribonucleic acid ; RNA ; Swine ; Swine flu ; Vaccines ; Viral infections ; Viral Proteins - immunology ; Virology ; Viruses</subject><ispartof>PloS one, 2015-08, Vol.10 (8), p.e0135474-e0135474</ispartof><rights>COPYRIGHT 2015 Public Library of Science</rights><rights>2015 Prevato et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2015 Prevato et al 2015 Prevato et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-9615072984ddd496652cfd0efd17fb75359a87bb257162b1b972015d102b11013</citedby><cites>FETCH-LOGICAL-c758t-9615072984ddd496652cfd0efd17fb75359a87bb257162b1b972015d102b11013</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1708528784/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1708528784?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,886,25755,27926,27927,37014,37015,44592,53793,53795,75128</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26280677$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Ye, Zhiping</contributor><creatorcontrib>Prevato, Marua</creatorcontrib><creatorcontrib>Ferlenghi, Ilaria</creatorcontrib><creatorcontrib>Bonci, Alessandra</creatorcontrib><creatorcontrib>Uematsu, Yasushi</creatorcontrib><creatorcontrib>Anselmi, Giulia</creatorcontrib><creatorcontrib>Giusti, Fabiola</creatorcontrib><creatorcontrib>Bertholet, Sylvie</creatorcontrib><creatorcontrib>Legay, Francois</creatorcontrib><creatorcontrib>Telford, John Laird</creatorcontrib><creatorcontrib>Settembre, Ethan C</creatorcontrib><creatorcontrib>Maione, Domenico</creatorcontrib><creatorcontrib>Cozzi, Roberta</creatorcontrib><title>Expression and Characterization of Recombinant, Tetrameric and Enzymatically Active Influenza Neuraminidase for the Setup of an Enzyme-Linked Lectin-Based Assay</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Developing a universal influenza vaccine that induces broad spectrum and longer-term immunity has become an important potentially achievable target in influenza vaccine research and development. Hemagglutinin (HA) and neuraminidase (NA) are the two major influenza virus antigens. Although antibody responses against influenza virus are mainly directed toward HA, NA is reported to be more genetically stable; hence NA-based vaccines have the potential to be effective for longer time periods. NA-specific immunity has been shown to limit the spread of influenza virus, thus reducing disease symptoms and providing cross-protection against heterosubtypic viruses in mouse challenge experiments. The production of large quantities of highly pure and stable NA could be beneficial for the development of new antivirals, subunit-based vaccines, and novel diagnostic tools. In this study, recombinant NA (rNA) was produced in mammalian cells at high levels from both swine A/California/07/2009 (H1N1) and avian A/turkey/Turkey/01/2005 (H5N1) influenza viruses. Biochemical, structural, and immunological characterizations revealed that the soluble rNAs produced are tetrameric, enzymatically active and immunogenic, and finally they represent good alternatives to conventionally used sources of NA in the Enzyme-Linked Lectin Assay (ELLA).</description><subject>Animal experimentation</subject><subject>Animals</subject><subject>Antibodies, Viral - immunology</subject><subject>Antibody Formation - immunology</subject><subject>Antigens</subject><subject>Antigens, Viral - immunology</subject><subject>Antiviral agents</subject><subject>Avian influenza</subject><subject>Birds</subject><subject>Cell Line</subject><subject>Chemical properties</subject><subject>Cross Protection - immunology</subject><subject>Cross Reactions - immunology</subject><subject>Cross-protection</subject><subject>Design</subject><subject>Development and progression</subject><subject>Diagnostic software</subject><subject>Diagnostic systems</subject><subject>Disease control</subject><subject>Enzyme-Linked Immunospot Assay - methods</subject><subject>Enzymes</subject><subject>Exo-a-sialidase</subject><subject>Female</subject><subject>Gene expression</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - immunology</subject><subject>Hemagglutinins</subject><subject>Immunity</subject><subject>Immunogenicity</subject><subject>Immunoglobulins</subject><subject>Immunology</subject><subject>Infections</subject><subject>Influenza</subject><subject>Influenza A Virus, H1N1 Subtype - immunology</subject><subject>Influenza A Virus, H5N1 Subtype - immunology</subject><subject>Influenza in Birds - immunology</subject><subject>Influenza vaccines</subject><subject>Influenza Vaccines - immunology</subject><subject>Lectins</subject><subject>Lectins - immunology</subject><subject>Livestock</subject><subject>Mammalian cells</subject><subject>Mice</subject><subject>Microscopy</subject><subject>Molecular biology</subject><subject>Neuraminidase - immunology</subject><subject>Orthomyxoviridae Infections - immunology</subject><subject>Pandemics</subject><subject>R&D</subject><subject>Recombinant Proteins - immunology</subject><subject>Research & development</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>Swine</subject><subject>Swine flu</subject><subject>Vaccines</subject><subject>Viral infections</subject><subject>Viral Proteins - immunology</subject><subject>Virology</subject><subject>Viruses</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNqNk99u0zAUxiMEYmPwBggiISGQaImd-E9ukEo1oFLFpG1wazn2SeuR2MVOpnVPw6PitN3Uol2gXCQ-_p3POZ_PSZKXKBujnKGPV673VjbjlbMwzlBOClY8So5RmeMRxVn-eO_7KHkWwlWWkZxT-jQ5whTzjDJ2nPw5vVl5CME4m0qr0-lSeqk68OZWdkPQ1ek5KNdWxkrbfUgvofOyjftqw5_a23UbSSWbZp1OVGeuIZ3ZuunB3sr0O_SRNtZoGSCtnU-7JaQX0PWrQVnarQCM5sb-Ap3OISrY0edI63QSglw_T57UsgnwYvc-SX58Ob2cfhvNz77OppP5SDHCu1FJEckYLnmhtS5KSglWtc6g1ojVFSM5KSVnVYUJQxRXqCoZzhDRKIsLFO07SV5vdVeNC2JnbhCIZZxgzngRidmW0E5eiZU3rfRr4aQRm4DzCyF9dKIBUeW0xopSXNS6yCnimpeEEyY512WFq6j1aXdaX7WgFdjoanMgerhjzVIs3LUoSF7ieI8nybudgHe_ewidaE1Q0DTSgus3_x0bIud8qOzNP-jD1e2ohYwFGFu7eK4aRMWkiK5RxAiO1PgBKj4aWqNiJ9Ymxg8S3h8kRKaDm24h-xDE7OL8_9mzn4fs2z12CbLplsE1_dCz4RAstqDyLgQP9b3JKBPDIN25IYZBErtBimmv9i_oPulucvK_luAZMw</recordid><startdate>20150817</startdate><enddate>20150817</enddate><creator>Prevato, Marua</creator><creator>Ferlenghi, Ilaria</creator><creator>Bonci, Alessandra</creator><creator>Uematsu, Yasushi</creator><creator>Anselmi, Giulia</creator><creator>Giusti, Fabiola</creator><creator>Bertholet, Sylvie</creator><creator>Legay, Francois</creator><creator>Telford, John Laird</creator><creator>Settembre, Ethan C</creator><creator>Maione, Domenico</creator><creator>Cozzi, Roberta</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20150817</creationdate><title>Expression and Characterization of Recombinant, Tetrameric and Enzymatically Active Influenza Neuraminidase for the Setup of an Enzyme-Linked Lectin-Based Assay</title><author>Prevato, Marua ; Ferlenghi, Ilaria ; Bonci, Alessandra ; Uematsu, Yasushi ; Anselmi, Giulia ; Giusti, Fabiola ; Bertholet, Sylvie ; Legay, Francois ; Telford, John Laird ; Settembre, Ethan C ; Maione, Domenico ; Cozzi, Roberta</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c758t-9615072984ddd496652cfd0efd17fb75359a87bb257162b1b972015d102b11013</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Animal experimentation</topic><topic>Animals</topic><topic>Antibodies, Viral - immunology</topic><topic>Antibody Formation - immunology</topic><topic>Antigens</topic><topic>Antigens, Viral - immunology</topic><topic>Antiviral agents</topic><topic>Avian influenza</topic><topic>Birds</topic><topic>Cell Line</topic><topic>Chemical properties</topic><topic>Cross Protection - immunology</topic><topic>Cross Reactions - immunology</topic><topic>Cross-protection</topic><topic>Design</topic><topic>Development and progression</topic><topic>Diagnostic software</topic><topic>Diagnostic systems</topic><topic>Disease control</topic><topic>Enzyme-Linked Immunospot Assay - methods</topic><topic>Enzymes</topic><topic>Exo-a-sialidase</topic><topic>Female</topic><topic>Gene expression</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus - immunology</topic><topic>Hemagglutinins</topic><topic>Immunity</topic><topic>Immunogenicity</topic><topic>Immunoglobulins</topic><topic>Immunology</topic><topic>Infections</topic><topic>Influenza</topic><topic>Influenza A Virus, H1N1 Subtype - immunology</topic><topic>Influenza A Virus, H5N1 Subtype - immunology</topic><topic>Influenza in Birds - immunology</topic><topic>Influenza vaccines</topic><topic>Influenza Vaccines - immunology</topic><topic>Lectins</topic><topic>Lectins - immunology</topic><topic>Livestock</topic><topic>Mammalian cells</topic><topic>Mice</topic><topic>Microscopy</topic><topic>Molecular biology</topic><topic>Neuraminidase - immunology</topic><topic>Orthomyxoviridae Infections - immunology</topic><topic>Pandemics</topic><topic>R&D</topic><topic>Recombinant Proteins - immunology</topic><topic>Research & development</topic><topic>Ribonucleic acid</topic><topic>RNA</topic><topic>Swine</topic><topic>Swine flu</topic><topic>Vaccines</topic><topic>Viral infections</topic><topic>Viral Proteins - immunology</topic><topic>Virology</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Prevato, Marua</creatorcontrib><creatorcontrib>Ferlenghi, Ilaria</creatorcontrib><creatorcontrib>Bonci, Alessandra</creatorcontrib><creatorcontrib>Uematsu, Yasushi</creatorcontrib><creatorcontrib>Anselmi, Giulia</creatorcontrib><creatorcontrib>Giusti, Fabiola</creatorcontrib><creatorcontrib>Bertholet, Sylvie</creatorcontrib><creatorcontrib>Legay, Francois</creatorcontrib><creatorcontrib>Telford, John Laird</creatorcontrib><creatorcontrib>Settembre, Ethan C</creatorcontrib><creatorcontrib>Maione, Domenico</creatorcontrib><creatorcontrib>Cozzi, Roberta</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Science in Context</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agriculture Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials science collection</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>Engineering collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Prevato, Marua</au><au>Ferlenghi, Ilaria</au><au>Bonci, Alessandra</au><au>Uematsu, Yasushi</au><au>Anselmi, Giulia</au><au>Giusti, Fabiola</au><au>Bertholet, Sylvie</au><au>Legay, Francois</au><au>Telford, John Laird</au><au>Settembre, Ethan C</au><au>Maione, Domenico</au><au>Cozzi, Roberta</au><au>Ye, Zhiping</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression and Characterization of Recombinant, Tetrameric and Enzymatically Active Influenza Neuraminidase for the Setup of an Enzyme-Linked Lectin-Based Assay</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2015-08-17</date><risdate>2015</risdate><volume>10</volume><issue>8</issue><spage>e0135474</spage><epage>e0135474</epage><pages>e0135474-e0135474</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Developing a universal influenza vaccine that induces broad spectrum and longer-term immunity has become an important potentially achievable target in influenza vaccine research and development. Hemagglutinin (HA) and neuraminidase (NA) are the two major influenza virus antigens. Although antibody responses against influenza virus are mainly directed toward HA, NA is reported to be more genetically stable; hence NA-based vaccines have the potential to be effective for longer time periods. NA-specific immunity has been shown to limit the spread of influenza virus, thus reducing disease symptoms and providing cross-protection against heterosubtypic viruses in mouse challenge experiments. The production of large quantities of highly pure and stable NA could be beneficial for the development of new antivirals, subunit-based vaccines, and novel diagnostic tools. In this study, recombinant NA (rNA) was produced in mammalian cells at high levels from both swine A/California/07/2009 (H1N1) and avian A/turkey/Turkey/01/2005 (H5N1) influenza viruses. Biochemical, structural, and immunological characterizations revealed that the soluble rNAs produced are tetrameric, enzymatically active and immunogenic, and finally they represent good alternatives to conventionally used sources of NA in the Enzyme-Linked Lectin Assay (ELLA).</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>26280677</pmid><doi>10.1371/journal.pone.0135474</doi><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2015-08, Vol.10 (8), p.e0135474-e0135474 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1708528784 |
| source | Publicly Available Content Database; PubMed Central |
| subjects | Animal experimentation Animals Antibodies, Viral - immunology Antibody Formation - immunology Antigens Antigens, Viral - immunology Antiviral agents Avian influenza Birds Cell Line Chemical properties Cross Protection - immunology Cross Reactions - immunology Cross-protection Design Development and progression Diagnostic software Diagnostic systems Disease control Enzyme-Linked Immunospot Assay - methods Enzymes Exo-a-sialidase Female Gene expression Hemagglutinin Glycoproteins, Influenza Virus - immunology Hemagglutinins Immunity Immunogenicity Immunoglobulins Immunology Infections Influenza Influenza A Virus, H1N1 Subtype - immunology Influenza A Virus, H5N1 Subtype - immunology Influenza in Birds - immunology Influenza vaccines Influenza Vaccines - immunology Lectins Lectins - immunology Livestock Mammalian cells Mice Microscopy Molecular biology Neuraminidase - immunology Orthomyxoviridae Infections - immunology Pandemics R&D Recombinant Proteins - immunology Research & development Ribonucleic acid RNA Swine Swine flu Vaccines Viral infections Viral Proteins - immunology Virology Viruses |
| title | Expression and Characterization of Recombinant, Tetrameric and Enzymatically Active Influenza Neuraminidase for the Setup of an Enzyme-Linked Lectin-Based Assay |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-18T09%3A26%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Expression%20and%20Characterization%20of%20Recombinant,%20Tetrameric%20and%20Enzymatically%20Active%20Influenza%20Neuraminidase%20for%20the%20Setup%20of%20an%20Enzyme-Linked%20Lectin-Based%20Assay&rft.jtitle=PloS%20one&rft.au=Prevato,%20Marua&rft.date=2015-08-17&rft.volume=10&rft.issue=8&rft.spage=e0135474&rft.epage=e0135474&rft.pages=e0135474-e0135474&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0135474&rft_dat=%3Cgale_plos_%3EA425761752%3C/gale_plos_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c758t-9615072984ddd496652cfd0efd17fb75359a87bb257162b1b972015d102b11013%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1708528784&rft_id=info:pmid/26280677&rft_galeid=A425761752&rfr_iscdi=true |