Porcine reproductive and respiratory syndrome virus attachment is mediated by the N-terminal domain of the sialoadhesin receptor
Sialoadhesin (Sn) is an important receptor for viral attachment and internalization of porcine reproductive and respiratory syndrome virus (PRRSV) to porcine alveolar macrophages (PAM). To investigate whether the N-terminal domain of Sn is sufficient and/or necessary for PRRSV attachment, we constru...
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| Veröffentlicht in: | Veterinary microbiology 2010-07, Vol.143 (2), p.371-378 |
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| creator | An, Tong-Qing Tian, Zhi-Jun He, Yun-Xia Xiao, Yan Jiang, Yi-Feng Peng, Jin-Mei Zhou, Yan-Jun Liu, Di Tong, Guang-Zhi |
| description | Sialoadhesin (Sn) is an important receptor for viral attachment and internalization of porcine reproductive and respiratory syndrome virus (PRRSV) to porcine alveolar macrophages (PAM). To investigate whether the N-terminal domain of Sn is sufficient and/or necessary for PRRSV attachment, we constructed a series of truncated fragments of porcine Sn and expressed these in the non-permissive PK15 cell line. The first 150 amino acids comprising the entire first domain of the Sn N-terminal region was necessary for PRRSV binding to cells, and the N-terminal domain alone was sufficient for virus attachment. The attachment of PRRSV to PAM cells was inhibited by polyclonal anti-serum against the N-terminal region of porcine Sn in a dose-dependent manner. The present study demonstrates that the first domain at the N-terminus of Sn mediates PRRSV attachment to PAM cells and contributes to better understanding the interaction between PRRSV and its host cells. |
| doi_str_mv | 10.1016/j.vetmic.2009.11.006 |
| format | Article |
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To investigate whether the N-terminal domain of Sn is sufficient and/or necessary for PRRSV attachment, we constructed a series of truncated fragments of porcine Sn and expressed these in the non-permissive PK15 cell line. The first 150 amino acids comprising the entire first domain of the Sn N-terminal region was necessary for PRRSV binding to cells, and the N-terminal domain alone was sufficient for virus attachment. The attachment of PRRSV to PAM cells was inhibited by polyclonal anti-serum against the N-terminal region of porcine Sn in a dose-dependent manner. The present study demonstrates that the first domain at the N-terminus of Sn mediates PRRSV attachment to PAM cells and contributes to better understanding the interaction between PRRSV and its host cells.</description><identifier>ISSN: 0378-1135</identifier><identifier>EISSN: 1873-2542</identifier><identifier>DOI: 10.1016/j.vetmic.2009.11.006</identifier><identifier>PMID: 19969429</identifier><identifier>CODEN: VMICDQ</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Animals ; binding capacity ; Binding domain ; binding sites ; biochemical mechanisms ; Biological and medical sciences ; cell adhesion ; cell lines ; Cells, Cultured ; Core Binding Factors ; Fundamental and applied biological sciences. Psychology ; Gene Deletion ; gene expression ; genes ; host-pathogen relationships ; immune system ; immunoglobulins ; in vitro studies ; infection ; macrophages ; Macrophages, Alveolar - physiology ; Macrophages, Alveolar - virology ; membrane glycoproteins ; Membrane Glycoproteins - physiology ; Microbiology ; Miscellaneous ; Models, Molecular ; mutation ; pathogenesis ; porcine reproductive and respiratory syndrome ; Porcine reproductive and respiratory syndrome virus ; Porcine reproductive and respiratory syndrome virus (PRRSV) ; Porcine respiratory and reproductive syndrome virus ; Porcine respiratory and reproductive syndrome virus - physiology ; Protein Binding ; Protein Conformation ; pulmonary alveoli ; Receptor ; receptors ; Receptors, Immunologic - physiology ; Sialic Acid Binding Ig-like Lectin 1 ; sialic acids ; Sialoadhesin ; sialoadhesin receptor ; Swine ; Virology ; Virus Attachment</subject><ispartof>Veterinary microbiology, 2010-07, Vol.143 (2), p.371-378</ispartof><rights>2009 Elsevier B.V.</rights><rights>2015 INIST-CNRS</rights><rights>(c) 2009 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c513t-ddce65a61b18e48044ce6c37931eb7ded6bcd7c67b93936c04610d56befcb3833</citedby><cites>FETCH-LOGICAL-c513t-ddce65a61b18e48044ce6c37931eb7ded6bcd7c67b93936c04610d56befcb3833</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.vetmic.2009.11.006$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22862088$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19969429$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>An, Tong-Qing</creatorcontrib><creatorcontrib>Tian, Zhi-Jun</creatorcontrib><creatorcontrib>He, Yun-Xia</creatorcontrib><creatorcontrib>Xiao, Yan</creatorcontrib><creatorcontrib>Jiang, Yi-Feng</creatorcontrib><creatorcontrib>Peng, Jin-Mei</creatorcontrib><creatorcontrib>Zhou, Yan-Jun</creatorcontrib><creatorcontrib>Liu, Di</creatorcontrib><creatorcontrib>Tong, Guang-Zhi</creatorcontrib><title>Porcine reproductive and respiratory syndrome virus attachment is mediated by the N-terminal domain of the sialoadhesin receptor</title><title>Veterinary microbiology</title><addtitle>Vet Microbiol</addtitle><description>Sialoadhesin (Sn) is an important receptor for viral attachment and internalization of porcine reproductive and respiratory syndrome virus (PRRSV) to porcine alveolar macrophages (PAM). To investigate whether the N-terminal domain of Sn is sufficient and/or necessary for PRRSV attachment, we constructed a series of truncated fragments of porcine Sn and expressed these in the non-permissive PK15 cell line. The first 150 amino acids comprising the entire first domain of the Sn N-terminal region was necessary for PRRSV binding to cells, and the N-terminal domain alone was sufficient for virus attachment. The attachment of PRRSV to PAM cells was inhibited by polyclonal anti-serum against the N-terminal region of porcine Sn in a dose-dependent manner. The present study demonstrates that the first domain at the N-terminus of Sn mediates PRRSV attachment to PAM cells and contributes to better understanding the interaction between PRRSV and its host cells.</description><subject>Animals</subject><subject>binding capacity</subject><subject>Binding domain</subject><subject>binding sites</subject><subject>biochemical mechanisms</subject><subject>Biological and medical sciences</subject><subject>cell adhesion</subject><subject>cell lines</subject><subject>Cells, Cultured</subject><subject>Core Binding Factors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Deletion</subject><subject>gene expression</subject><subject>genes</subject><subject>host-pathogen relationships</subject><subject>immune system</subject><subject>immunoglobulins</subject><subject>in vitro studies</subject><subject>infection</subject><subject>macrophages</subject><subject>Macrophages, Alveolar - physiology</subject><subject>Macrophages, Alveolar - virology</subject><subject>membrane glycoproteins</subject><subject>Membrane Glycoproteins - physiology</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Models, Molecular</subject><subject>mutation</subject><subject>pathogenesis</subject><subject>porcine reproductive and respiratory syndrome</subject><subject>Porcine reproductive and respiratory syndrome virus</subject><subject>Porcine reproductive and respiratory syndrome virus (PRRSV)</subject><subject>Porcine respiratory and reproductive syndrome virus</subject><subject>Porcine respiratory and reproductive syndrome virus - physiology</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>pulmonary alveoli</subject><subject>Receptor</subject><subject>receptors</subject><subject>Receptors, Immunologic - physiology</subject><subject>Sialic Acid Binding Ig-like Lectin 1</subject><subject>sialic acids</subject><subject>Sialoadhesin</subject><subject>sialoadhesin receptor</subject><subject>Swine</subject><subject>Virology</subject><subject>Virus Attachment</subject><issn>0378-1135</issn><issn>1873-2542</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc-P1CAUxxujcWdX_wOjXMyeOj4KpXAxMRt_JRs10T0TCq8Ok7aMQCeZm3-6rJ3oTU-Ex-c94PupqmcUthSoeLXfHjFP3m4bALWldAsgHlQbKjtWNy1vHlYbYJ2sKWXtRXWZ0h4AuBLwuLqgSgnFG7Wpfn4J0foZScRDDG6x2R-RmNmVQjr4aHKIJ5JOs4thQnL0cUnE5GzsbsI5E5_IhM6bjI70J5J3SD7VGePkZzMSFybjZxKG3wfJmzEYt8NUahEtHsrwJ9WjwYwJn57Xq-ru3dtvNx_q28_vP968ua1tS1munbMoWiNoTyVyCZyXvWWdYhT7zqETvXWdFV2vmGLCAhcUXCt6HGzPJGNX1fU6t3zzx4Ip68kni-NoZgxL0h3nHbRCif-TjEMjSnqF5CtpY0gp4qAP0U8mnjQFfS9J7_UqSd9L0pTqIqm0PT9fsPQlvL9NZysFeHkGTLJmHKKZrU9_uKaRogEpC_di5QYTtPkeC3P3tQHKgEretZIW4vVKYIn26DHqZD3OtigrArJ2wf_7rb8ANaa9_Q</recordid><startdate>20100714</startdate><enddate>20100714</enddate><creator>An, Tong-Qing</creator><creator>Tian, Zhi-Jun</creator><creator>He, Yun-Xia</creator><creator>Xiao, Yan</creator><creator>Jiang, Yi-Feng</creator><creator>Peng, Jin-Mei</creator><creator>Zhou, Yan-Jun</creator><creator>Liu, Di</creator><creator>Tong, Guang-Zhi</creator><general>Elsevier B.V</general><general>Amsterdam; New York: Elsevier</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><scope>7U9</scope><scope>H94</scope></search><sort><creationdate>20100714</creationdate><title>Porcine reproductive and respiratory syndrome virus attachment is mediated by the N-terminal domain of the sialoadhesin receptor</title><author>An, Tong-Qing ; Tian, Zhi-Jun ; He, Yun-Xia ; Xiao, Yan ; Jiang, Yi-Feng ; Peng, Jin-Mei ; Zhou, Yan-Jun ; Liu, Di ; Tong, Guang-Zhi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c513t-ddce65a61b18e48044ce6c37931eb7ded6bcd7c67b93936c04610d56befcb3833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Animals</topic><topic>binding capacity</topic><topic>Binding domain</topic><topic>binding sites</topic><topic>biochemical mechanisms</topic><topic>Biological and medical sciences</topic><topic>cell adhesion</topic><topic>cell lines</topic><topic>Cells, Cultured</topic><topic>Core Binding Factors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Deletion</topic><topic>gene expression</topic><topic>genes</topic><topic>host-pathogen relationships</topic><topic>immune system</topic><topic>immunoglobulins</topic><topic>in vitro studies</topic><topic>infection</topic><topic>macrophages</topic><topic>Macrophages, Alveolar - physiology</topic><topic>Macrophages, Alveolar - virology</topic><topic>membrane glycoproteins</topic><topic>Membrane Glycoproteins - physiology</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Models, Molecular</topic><topic>mutation</topic><topic>pathogenesis</topic><topic>porcine reproductive and respiratory syndrome</topic><topic>Porcine reproductive and respiratory syndrome virus</topic><topic>Porcine reproductive and respiratory syndrome virus (PRRSV)</topic><topic>Porcine respiratory and reproductive syndrome virus</topic><topic>Porcine respiratory and reproductive syndrome virus - physiology</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>pulmonary alveoli</topic><topic>Receptor</topic><topic>receptors</topic><topic>Receptors, Immunologic - physiology</topic><topic>Sialic Acid Binding Ig-like Lectin 1</topic><topic>sialic acids</topic><topic>Sialoadhesin</topic><topic>sialoadhesin receptor</topic><topic>Swine</topic><topic>Virology</topic><topic>Virus Attachment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>An, Tong-Qing</creatorcontrib><creatorcontrib>Tian, Zhi-Jun</creatorcontrib><creatorcontrib>He, Yun-Xia</creatorcontrib><creatorcontrib>Xiao, Yan</creatorcontrib><creatorcontrib>Jiang, Yi-Feng</creatorcontrib><creatorcontrib>Peng, Jin-Mei</creatorcontrib><creatorcontrib>Zhou, Yan-Jun</creatorcontrib><creatorcontrib>Liu, Di</creatorcontrib><creatorcontrib>Tong, Guang-Zhi</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><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>Veterinary microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>An, Tong-Qing</au><au>Tian, Zhi-Jun</au><au>He, Yun-Xia</au><au>Xiao, Yan</au><au>Jiang, Yi-Feng</au><au>Peng, Jin-Mei</au><au>Zhou, Yan-Jun</au><au>Liu, Di</au><au>Tong, Guang-Zhi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Porcine reproductive and respiratory syndrome virus attachment is mediated by the N-terminal domain of the sialoadhesin receptor</atitle><jtitle>Veterinary microbiology</jtitle><addtitle>Vet Microbiol</addtitle><date>2010-07-14</date><risdate>2010</risdate><volume>143</volume><issue>2</issue><spage>371</spage><epage>378</epage><pages>371-378</pages><issn>0378-1135</issn><eissn>1873-2542</eissn><coden>VMICDQ</coden><abstract>Sialoadhesin (Sn) is an important receptor for viral attachment and internalization of porcine reproductive and respiratory syndrome virus (PRRSV) to porcine alveolar macrophages (PAM). To investigate whether the N-terminal domain of Sn is sufficient and/or necessary for PRRSV attachment, we constructed a series of truncated fragments of porcine Sn and expressed these in the non-permissive PK15 cell line. The first 150 amino acids comprising the entire first domain of the Sn N-terminal region was necessary for PRRSV binding to cells, and the N-terminal domain alone was sufficient for virus attachment. The attachment of PRRSV to PAM cells was inhibited by polyclonal anti-serum against the N-terminal region of porcine Sn in a dose-dependent manner. The present study demonstrates that the first domain at the N-terminus of Sn mediates PRRSV attachment to PAM cells and contributes to better understanding the interaction between PRRSV and its host cells.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>19969429</pmid><doi>10.1016/j.vetmic.2009.11.006</doi><tpages>8</tpages></addata></record> |
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| identifier | ISSN: 0378-1135 |
| ispartof | Veterinary microbiology, 2010-07, Vol.143 (2), p.371-378 |
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| subjects | Animals binding capacity Binding domain binding sites biochemical mechanisms Biological and medical sciences cell adhesion cell lines Cells, Cultured Core Binding Factors Fundamental and applied biological sciences. Psychology Gene Deletion gene expression genes host-pathogen relationships immune system immunoglobulins in vitro studies infection macrophages Macrophages, Alveolar - physiology Macrophages, Alveolar - virology membrane glycoproteins Membrane Glycoproteins - physiology Microbiology Miscellaneous Models, Molecular mutation pathogenesis porcine reproductive and respiratory syndrome Porcine reproductive and respiratory syndrome virus Porcine reproductive and respiratory syndrome virus (PRRSV) Porcine respiratory and reproductive syndrome virus Porcine respiratory and reproductive syndrome virus - physiology Protein Binding Protein Conformation pulmonary alveoli Receptor receptors Receptors, Immunologic - physiology Sialic Acid Binding Ig-like Lectin 1 sialic acids Sialoadhesin sialoadhesin receptor Swine Virology Virus Attachment |
| title | Porcine reproductive and respiratory syndrome virus attachment is mediated by the N-terminal domain of the sialoadhesin receptor |
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