Recombinant soluble low-density lipoprotein receptor fragment inhibits common cold infection
A fragment of the human low‐density lipoprotein receptor encompassing the seven ligand‐binding repeats fused to a C‐terminal oligo‐His tag was expressed in Sf9 insect cells. The melittin signal sequence encoded in the baculovirus vector led to secretion of the protein into the cell supernatant in a...
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| Veröffentlicht in: | Journal of molecular recognition 1998-01, Vol.11 (1-6), p.49-51 |
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| container_issue | 1-6 |
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| container_title | Journal of molecular recognition |
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| creator | Marlovits, Thomas C. Zechmeister, Thomas Schwihla, Herwig Ronacher, Bernhard Blaas, Dieter |
| description | A fragment of the human low‐density lipoprotein receptor encompassing the seven ligand‐binding repeats fused to a C‐terminal oligo‐His tag was expressed in Sf9 insect cells. The melittin signal sequence encoded in the baculovirus vector led to secretion of the protein into the cell supernatant in a soluble form. The receptor fragment bound its natural ligand β‐migrating very‐low‐density lipoprotein and human rhinovirus serotype 2 in non‐reducing ligand blots. Infection of all minor group human rhinovirus serotypes investigated was inhibited by the presence of the receptor fragment during viral challenge of HeLa cells. Infection is inhibited by aggregation of the virions. Copyright © 1998 John Wiley & Sons, Ltd. |
| doi_str_mv | 10.1002/(SICI)1099-1352(199812)11:1/6<49::AID-JMR388>3.0.CO;2-3 |
| format | Article |
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The melittin signal sequence encoded in the baculovirus vector led to secretion of the protein into the cell supernatant in a soluble form. The receptor fragment bound its natural ligand β‐migrating very‐low‐density lipoprotein and human rhinovirus serotype 2 in non‐reducing ligand blots. Infection of all minor group human rhinovirus serotypes investigated was inhibited by the presence of the receptor fragment during viral challenge of HeLa cells. Infection is inhibited by aggregation of the virions. 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Mol. Recognit</addtitle><description>A fragment of the human low‐density lipoprotein receptor encompassing the seven ligand‐binding repeats fused to a C‐terminal oligo‐His tag was expressed in Sf9 insect cells. The melittin signal sequence encoded in the baculovirus vector led to secretion of the protein into the cell supernatant in a soluble form. The receptor fragment bound its natural ligand β‐migrating very‐low‐density lipoprotein and human rhinovirus serotype 2 in non‐reducing ligand blots. Infection of all minor group human rhinovirus serotypes investigated was inhibited by the presence of the receptor fragment during viral challenge of HeLa cells. Infection is inhibited by aggregation of the virions. Copyright © 1998 John Wiley & Sons, Ltd.</description><subject>Animals</subject><subject>Baculoviridae - genetics</subject><subject>baculovirus</subject><subject>Cell Line</subject><subject>Common Cold - prevention & control</subject><subject>HeLa Cells</subject><subject>human rhinovirus</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>infection inhibition</subject><subject>low-density lipoprotein receptor</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - genetics</subject><subject>Peptide Fragments - pharmacology</subject><subject>receptor</subject><subject>Receptors, LDL - chemistry</subject><subject>Receptors, LDL - genetics</subject><subject>Receptors, LDL - physiology</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Rhinovirus - classification</subject><subject>Rhinovirus - drug effects</subject><subject>Rhinovirus - pathogenicity</subject><subject>Serotyping</subject><subject>Sf9</subject><subject>Solubility</subject><subject>Spodoptera</subject><issn>0952-3499</issn><issn>1099-1352</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkF9rE0EUxQdRbFr9CrJP0j5sOn92ZmeiWEq0MdIaiNpWEC6zm7s6ursTdzbUfHsnbCiCgk8Xzj33nMuPkDNGx4xSfnr8YT6dnzBqTMqE5MfMGM34CWMTdqpeZmYyOZ-_Tt9dLYXWr8SYjqeLFzwVD8jo_uYhGVEjo5gZc0AOQ_hOadxJ-pgcxI5caSpH5MsSS98UrrVtnwRfb4oak9rfpStsg-u3Se3Wft35Hl2bdFjiuvddUnX2a4PxwrXfXOH6kMSQxrdx1KsoVlj2zrdPyKPK1gGf7ucR-XTx5uP0bXq5mM2n55dpmWml09IIqyoUFSuUNZQzU5QyV_lKclsUSvAcpZK8sByz3Jq4roRhNi811dpWRhyR50NufPTnBkMPjQsl1rVt0W8CKMO0FIJH481gLDsfQocVrDvX2G4LjMIOPMAOPOwgwg4iDOCBMWCgIDMAETwM4EEAhekCOIiY_Gz_wqZocPVH7kA6Gj4PhjtX4_av3v_V_rN1r8TsdMh2ocdf99m2-wEqF7mEm_czuF5e397OLnK4Er8BCGywNQ</recordid><startdate>19980101</startdate><enddate>19980101</enddate><creator>Marlovits, Thomas C.</creator><creator>Zechmeister, Thomas</creator><creator>Schwihla, Herwig</creator><creator>Ronacher, Bernhard</creator><creator>Blaas, Dieter</creator><general>John Wiley & Sons, Ltd</general><scope>BSCLL</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>19980101</creationdate><title>Recombinant soluble low-density lipoprotein receptor fragment inhibits common cold infection</title><author>Marlovits, Thomas C. ; Zechmeister, Thomas ; Schwihla, Herwig ; Ronacher, Bernhard ; Blaas, Dieter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4868-c93a6fe3f1b6a90219bc5767d52abb6327e5652ba2e47a919bf391a7c8088af93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Baculoviridae - genetics</topic><topic>baculovirus</topic><topic>Cell Line</topic><topic>Common Cold - prevention & control</topic><topic>HeLa Cells</topic><topic>human rhinovirus</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>infection inhibition</topic><topic>low-density lipoprotein receptor</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - genetics</topic><topic>Peptide Fragments - pharmacology</topic><topic>receptor</topic><topic>Receptors, LDL - chemistry</topic><topic>Receptors, LDL - genetics</topic><topic>Receptors, LDL - physiology</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Rhinovirus - classification</topic><topic>Rhinovirus - drug effects</topic><topic>Rhinovirus - pathogenicity</topic><topic>Serotyping</topic><topic>Sf9</topic><topic>Solubility</topic><topic>Spodoptera</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marlovits, Thomas C.</creatorcontrib><creatorcontrib>Zechmeister, Thomas</creatorcontrib><creatorcontrib>Schwihla, Herwig</creatorcontrib><creatorcontrib>Ronacher, Bernhard</creatorcontrib><creatorcontrib>Blaas, Dieter</creatorcontrib><collection>Istex</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>Journal of molecular recognition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Marlovits, Thomas C.</au><au>Zechmeister, Thomas</au><au>Schwihla, Herwig</au><au>Ronacher, Bernhard</au><au>Blaas, Dieter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Recombinant soluble low-density lipoprotein receptor fragment inhibits common cold infection</atitle><jtitle>Journal of molecular recognition</jtitle><addtitle>J. Mol. Recognit</addtitle><date>1998-01-01</date><risdate>1998</risdate><volume>11</volume><issue>1-6</issue><spage>49</spage><epage>51</epage><pages>49-51</pages><issn>0952-3499</issn><eissn>1099-1352</eissn><abstract>A fragment of the human low‐density lipoprotein receptor encompassing the seven ligand‐binding repeats fused to a C‐terminal oligo‐His tag was expressed in Sf9 insect cells. The melittin signal sequence encoded in the baculovirus vector led to secretion of the protein into the cell supernatant in a soluble form. The receptor fragment bound its natural ligand β‐migrating very‐low‐density lipoprotein and human rhinovirus serotype 2 in non‐reducing ligand blots. Infection of all minor group human rhinovirus serotypes investigated was inhibited by the presence of the receptor fragment during viral challenge of HeLa cells. Infection is inhibited by aggregation of the virions. 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| ispartof | Journal of molecular recognition, 1998-01, Vol.11 (1-6), p.49-51 |
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| subjects | Animals Baculoviridae - genetics baculovirus Cell Line Common Cold - prevention & control HeLa Cells human rhinovirus Humans In Vitro Techniques infection inhibition low-density lipoprotein receptor Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - pharmacology receptor Receptors, LDL - chemistry Receptors, LDL - genetics Receptors, LDL - physiology Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - pharmacology Rhinovirus - classification Rhinovirus - drug effects Rhinovirus - pathogenicity Serotyping Sf9 Solubility Spodoptera |
| title | Recombinant soluble low-density lipoprotein receptor fragment inhibits common cold infection |
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