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Human single chain monoclonal antibody that recognizes matrix protein of heterologous influenza A virus subtypes
Matrix protein (M1) is predominant and has pivotal role in the influenza A virus replication and assembly. It is therefore an attractive target for antiviral drugs, siRNA studies, and therapeutic antibodies. Nevertheless, therapeutic antibody that interferes with the M1 multiplex function has never...
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Published in: | Journal of virological methods 2009-07, Vol.159 (1), p.105-111 |
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creator | Poungpair, Ornnuthchar Chaicumpa, Wanpen Kulkeaw, Kasem Maneewatch, Santi Thueng-in, Kanyarat Srimanote, Potjanee Tongtawe, Pongsri Songserm, Thaweesak Lekcharoensuk, Porntippa Tapchaisri, Pramuan |
description | Matrix protein (M1) is predominant and has pivotal role in the influenza A virus replication and assembly. It is therefore an attractive target for antiviral drugs, siRNA studies, and therapeutic antibodies. Nevertheless, therapeutic antibody that interferes with the M1 multiplex function has never been developed. In this study, human single monoclonal antibody fragments (HuScFvs) to M1 were generated. Full length recombinant M1 (rM1) was produced from cDNA prepared from genome of highly pathogenic avian influenza virus, A/H5N1. The rM1 was used as an antigen in phage bio-panning to select phage clones displaying HuScFv from a human antibody phage display library. Several phage clones displaying HuScFv bound to the rM1 and harboring the respective
huscfv gene inserts were isolated. RFLP experiments revealed multiple DNA banding patterns which indicated epitope/affinity diversity of the HuScFv. The HuScFv were tested for their binding to native M1 of homologous and heterologous influenza A viruses using ELISA as well as incorporating immunostaining and immunofluorescence studies with infected MDCK cells. One such protein produced from a selected phage clone blocked binding of M1 to viral RNA. The HuScFv in their
in vivo functional format, e.g. cell-penetrating molecules, should be developed and tested as a broad spectrum anti-A/influenza. |
doi_str_mv | 10.1016/j.jviromet.2009.03.010 |
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huscfv gene inserts were isolated. RFLP experiments revealed multiple DNA banding patterns which indicated epitope/affinity diversity of the HuScFv. The HuScFv were tested for their binding to native M1 of homologous and heterologous influenza A viruses using ELISA as well as incorporating immunostaining and immunofluorescence studies with infected MDCK cells. One such protein produced from a selected phage clone blocked binding of M1 to viral RNA. The HuScFv in their
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huscfv gene inserts were isolated. RFLP experiments revealed multiple DNA banding patterns which indicated epitope/affinity diversity of the HuScFv. The HuScFv were tested for their binding to native M1 of homologous and heterologous influenza A viruses using ELISA as well as incorporating immunostaining and immunofluorescence studies with infected MDCK cells. One such protein produced from a selected phage clone blocked binding of M1 to viral RNA. The HuScFv in their
in vivo functional format, e.g. cell-penetrating molecules, should be developed and tested as a broad spectrum anti-A/influenza.</description><subject>A/H5N1</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibodies, Viral - immunology</subject><subject>Antibody Specificity</subject><subject>Avian influenza virus</subject><subject>Biological and medical sciences</subject><subject>Dogs</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Immunoglobulin Subunits - immunology</subject><subject>In Situ Hybridization, Fluorescence</subject><subject>Influenza A</subject><subject>Influenza A virus</subject><subject>Influenza A virus - immunology</subject><subject>Influenza A virus - metabolism</subject><subject>Matrix protein (M1)</subject><subject>Mice</subject><subject>Microbiology</subject><subject>Peptide Library</subject><subject>Phage display</subject><subject>Rabbits</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - immunology</subject><subject>ScFv</subject><subject>Techniques used in virology</subject><subject>Viral Matrix Proteins - biosynthesis</subject><subject>Viral Matrix Proteins - immunology</subject><subject>Virology</subject><issn>0166-0934</issn><issn>1879-0984</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNqFkc1u1DAURi0EokPbV6i8gd0E_yfZUVWFIlXqpqwtx7mZ8cixB9upmD49LjPAsitfWeezP92D0BUlDSVUfd41uyeX4gylYYT0DeENoeQNWtGu7dek78RbtKqgqjMXZ-hDzjtCiGw5f4_OaC8E6yRfof3dMpuAswsbD9hujQt4jiFaH4Px2ITihjgecNmaghPYuAnuGTKeTUnuF96nWKBG4oS3UCBFHzdxydiFyS8Qng2-xrVnvcnLUA57yBfo3WR8hsvTeY5-fL19vLlb3z98-35zfb-2grVl3bW8FUR0LUxcjqbvpKR9ra8GSoeBdEIq0XZMgLVmmJhhohsZWCMoAPRA-Tn6dHy3Vvy5QC56dtmC9yZAbahVy6RqCXkVZH-WxmUF1RG0KeacYNL75GaTDpoS_SJF7_RfKfpFiiZcVyk1eHX6YRlmGP_HThYq8PEEmGyNn5IJ1uV_HKNScK5U5b4cOaiLe3KQdLYOgoXRVTVFj9G91uU3Bkiwdg</recordid><startdate>20090701</startdate><enddate>20090701</enddate><creator>Poungpair, Ornnuthchar</creator><creator>Chaicumpa, Wanpen</creator><creator>Kulkeaw, Kasem</creator><creator>Maneewatch, Santi</creator><creator>Thueng-in, Kanyarat</creator><creator>Srimanote, Potjanee</creator><creator>Tongtawe, Pongsri</creator><creator>Songserm, Thaweesak</creator><creator>Lekcharoensuk, Porntippa</creator><creator>Tapchaisri, Pramuan</creator><general>Elsevier B.V</general><general>Elsevier</general><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>7T5</scope><scope>7T7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20090701</creationdate><title>Human single chain monoclonal antibody that recognizes matrix protein of heterologous influenza A virus subtypes</title><author>Poungpair, Ornnuthchar ; Chaicumpa, Wanpen ; Kulkeaw, Kasem ; Maneewatch, Santi ; Thueng-in, Kanyarat ; Srimanote, Potjanee ; Tongtawe, Pongsri ; Songserm, Thaweesak ; Lekcharoensuk, Porntippa ; Tapchaisri, Pramuan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c427t-873740487ef35da9855190576b11bb0845647824eccabf2a248d2eca41eee9e13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>A/H5N1</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibodies, Viral - immunology</topic><topic>Antibody Specificity</topic><topic>Avian influenza virus</topic><topic>Biological and medical sciences</topic><topic>Dogs</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Immunoglobulin Subunits - immunology</topic><topic>In Situ Hybridization, Fluorescence</topic><topic>Influenza A</topic><topic>Influenza A virus</topic><topic>Influenza A virus - immunology</topic><topic>Influenza A virus - metabolism</topic><topic>Matrix protein (M1)</topic><topic>Mice</topic><topic>Microbiology</topic><topic>Peptide Library</topic><topic>Phage display</topic><topic>Rabbits</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - immunology</topic><topic>ScFv</topic><topic>Techniques used in virology</topic><topic>Viral Matrix Proteins - biosynthesis</topic><topic>Viral Matrix Proteins - immunology</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Poungpair, Ornnuthchar</creatorcontrib><creatorcontrib>Chaicumpa, Wanpen</creatorcontrib><creatorcontrib>Kulkeaw, Kasem</creatorcontrib><creatorcontrib>Maneewatch, Santi</creatorcontrib><creatorcontrib>Thueng-in, Kanyarat</creatorcontrib><creatorcontrib>Srimanote, Potjanee</creatorcontrib><creatorcontrib>Tongtawe, Pongsri</creatorcontrib><creatorcontrib>Songserm, Thaweesak</creatorcontrib><creatorcontrib>Lekcharoensuk, Porntippa</creatorcontrib><creatorcontrib>Tapchaisri, Pramuan</creatorcontrib><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>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of virological methods</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Poungpair, Ornnuthchar</au><au>Chaicumpa, Wanpen</au><au>Kulkeaw, Kasem</au><au>Maneewatch, Santi</au><au>Thueng-in, Kanyarat</au><au>Srimanote, Potjanee</au><au>Tongtawe, Pongsri</au><au>Songserm, Thaweesak</au><au>Lekcharoensuk, Porntippa</au><au>Tapchaisri, Pramuan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human single chain monoclonal antibody that recognizes matrix protein of heterologous influenza A virus subtypes</atitle><jtitle>Journal of virological methods</jtitle><addtitle>J Virol Methods</addtitle><date>2009-07-01</date><risdate>2009</risdate><volume>159</volume><issue>1</issue><spage>105</spage><epage>111</epage><pages>105-111</pages><issn>0166-0934</issn><eissn>1879-0984</eissn><coden>JVMEDH</coden><abstract>Matrix protein (M1) is predominant and has pivotal role in the influenza A virus replication and assembly. It is therefore an attractive target for antiviral drugs, siRNA studies, and therapeutic antibodies. Nevertheless, therapeutic antibody that interferes with the M1 multiplex function has never been developed. In this study, human single monoclonal antibody fragments (HuScFvs) to M1 were generated. Full length recombinant M1 (rM1) was produced from cDNA prepared from genome of highly pathogenic avian influenza virus, A/H5N1. The rM1 was used as an antigen in phage bio-panning to select phage clones displaying HuScFv from a human antibody phage display library. Several phage clones displaying HuScFv bound to the rM1 and harboring the respective
huscfv gene inserts were isolated. RFLP experiments revealed multiple DNA banding patterns which indicated epitope/affinity diversity of the HuScFv. The HuScFv were tested for their binding to native M1 of homologous and heterologous influenza A viruses using ELISA as well as incorporating immunostaining and immunofluorescence studies with infected MDCK cells. One such protein produced from a selected phage clone blocked binding of M1 to viral RNA. The HuScFv in their
in vivo functional format, e.g. cell-penetrating molecules, should be developed and tested as a broad spectrum anti-A/influenza.</abstract><cop>Kidlington</cop><pub>Elsevier B.V</pub><pmid>19442853</pmid><doi>10.1016/j.jviromet.2009.03.010</doi><tpages>7</tpages></addata></record> |
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subjects | A/H5N1 Animals Antibodies, Monoclonal - immunology Antibodies, Viral - immunology Antibody Specificity Avian influenza virus Biological and medical sciences Dogs Enzyme-Linked Immunosorbent Assay Fundamental and applied biological sciences. Psychology Humans Immunoglobulin Subunits - immunology In Situ Hybridization, Fluorescence Influenza A Influenza A virus Influenza A virus - immunology Influenza A virus - metabolism Matrix protein (M1) Mice Microbiology Peptide Library Phage display Rabbits Recombinant Proteins - biosynthesis Recombinant Proteins - immunology ScFv Techniques used in virology Viral Matrix Proteins - biosynthesis Viral Matrix Proteins - immunology Virology |
title | Human single chain monoclonal antibody that recognizes matrix protein of heterologous influenza A virus subtypes |
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