Characterization of a Truncated Soluble Form of the Baculovirus (AcMNPV) Major Envelope Protein Gp64
A truncated tagged form of the Autographica californica multiple nuclear polyhedrosis virus major surface glycoprotein, gp64, has been expressed using the baculovirus expression system and purified to homogeneity by immune-affinity chromatography. The protein, which is responsible for virus-cell fus...
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| Veröffentlicht in: | Protein expression and purification 2002-03, Vol.24 (2), p.196-201 |
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| creator | Lu, Weixian Chapple, Susan D Lissini, Olga Jones, Ian M |
| description | A truncated tagged form of the Autographica californica multiple nuclear polyhedrosis virus major surface glycoprotein, gp64, has been expressed using the baculovirus expression system and purified to homogeneity by immune-affinity chromatography. The protein, which is responsible for virus-cell fusion, was a trimer in solution and retained this oligomeric form at pH 5, the pH of fusion. Circular dichroism spectroscopy indicated a protein with mixed α-helix and β-sheet content that did not undergo significant change at pH 5. The soluble protein showed no detectable binding to the insect cell surface. These data suggest a novel fusion mechanism for gp64 compared to models such as the influenza HA. In a crystal screen, deglycosylated, but not glycosylated, preparations of the protein were found to form small needle-shaped crystals that may form the basis of a dedicated structural study. |
| doi_str_mv | 10.1006/prep.2001.1561 |
| format | Article |
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The protein, which is responsible for virus-cell fusion, was a trimer in solution and retained this oligomeric form at pH 5, the pH of fusion. Circular dichroism spectroscopy indicated a protein with mixed α-helix and β-sheet content that did not undergo significant change at pH 5. The soluble protein showed no detectable binding to the insect cell surface. These data suggest a novel fusion mechanism for gp64 compared to models such as the influenza HA. 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The protein, which is responsible for virus-cell fusion, was a trimer in solution and retained this oligomeric form at pH 5, the pH of fusion. Circular dichroism spectroscopy indicated a protein with mixed α-helix and β-sheet content that did not undergo significant change at pH 5. The soluble protein showed no detectable binding to the insect cell surface. These data suggest a novel fusion mechanism for gp64 compared to models such as the influenza HA. In a crystal screen, deglycosylated, but not glycosylated, preparations of the protein were found to form small needle-shaped crystals that may form the basis of a dedicated structural study.</description><subject>Baculoviridae - chemistry</subject><subject>Chromatography, Affinity</subject><subject>Circular Dichroism</subject><subject>Protein Engineering</subject><subject>Protein Folding</subject><subject>Solubility</subject><subject>Viral Fusion Proteins - chemistry</subject><issn>1046-5928</issn><issn>1096-0279</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kM9LwzAUx4Mo_r56lJxED53JmqTNcY45BX8MnF5DmrxiRtfUpB3oX2_LBp48vQfv8_3C-yB0QcmIEiJumwDNaEwIHVEu6B46pkSKhIwzuT_sTCRcjvMjdBLjqqeoIPwQHVGa8zyj6TGy008dtGkhuB_dOl9jX2KNl6GrjW7B4jdfdUUF-N6H9XBrPwHfadNVfuNCF_H1xDy_LD5u8LNe-YBn9QYq3wBeBN-Cq_G8EewMHZS6inC-m6fo_X62nD4kT6_zx-nkKTEpI20i0kJblutMaml4ZsCkRVkyIXMLkhNrSqZNDrQQNEtlxmmhtYW0sJJDyQqRnqKrbW8T_FcHsVVrFw1Ula7Bd1FllGVszGkPjragCT7GAKVqglvr8K0oUYNXNXhVg1c1eO0Dl7vmrliD_cN3Insg3wLQ_7dxEFQ0DmoD1gUwrbLe_df9C9FDh6w</recordid><startdate>20020301</startdate><enddate>20020301</enddate><creator>Lu, Weixian</creator><creator>Chapple, Susan D</creator><creator>Lissini, Olga</creator><creator>Jones, Ian M</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>20020301</creationdate><title>Characterization of a Truncated Soluble Form of the Baculovirus (AcMNPV) Major Envelope Protein Gp64</title><author>Lu, Weixian ; Chapple, Susan D ; Lissini, Olga ; Jones, Ian M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c340t-63bad48a79a9c57cec3bff4698de950dcf4ac8e1b61739751baade3bd95ef4b63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Baculoviridae - chemistry</topic><topic>Chromatography, Affinity</topic><topic>Circular Dichroism</topic><topic>Protein Engineering</topic><topic>Protein Folding</topic><topic>Solubility</topic><topic>Viral Fusion Proteins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lu, Weixian</creatorcontrib><creatorcontrib>Chapple, Susan D</creatorcontrib><creatorcontrib>Lissini, Olga</creatorcontrib><creatorcontrib>Jones, Ian M</creatorcontrib><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>Protein expression and purification</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lu, Weixian</au><au>Chapple, Susan D</au><au>Lissini, Olga</au><au>Jones, Ian M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a Truncated Soluble Form of the Baculovirus (AcMNPV) Major Envelope Protein Gp64</atitle><jtitle>Protein expression and purification</jtitle><addtitle>Protein Expr Purif</addtitle><date>2002-03-01</date><risdate>2002</risdate><volume>24</volume><issue>2</issue><spage>196</spage><epage>201</epage><pages>196-201</pages><issn>1046-5928</issn><eissn>1096-0279</eissn><abstract>A truncated tagged form of the Autographica californica multiple nuclear polyhedrosis virus major surface glycoprotein, gp64, has been expressed using the baculovirus expression system and purified to homogeneity by immune-affinity chromatography. 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| ispartof | Protein expression and purification, 2002-03, Vol.24 (2), p.196-201 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Baculoviridae - chemistry Chromatography, Affinity Circular Dichroism Protein Engineering Protein Folding Solubility Viral Fusion Proteins - chemistry |
| title | Characterization of a Truncated Soluble Form of the Baculovirus (AcMNPV) Major Envelope Protein Gp64 |
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