The envelope proteins of bovine leukemia virus: Purification and sequence analysis
Two proteins, termed gp60 and p30, have been purified to homogeneity from bovine leukemia virus (BLV) using controlled pore glass and reverse-phase liquid chromatography (RPLC). gp60 was shown to be a glycoprotein by identification of glucosamine on the amino acid analyzer. Antiserum prepared to gp6...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 1984-01, Vol.135 (2), p.417-427 |
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| creator | Schultz, A.M. Copeland, T.D. Oroszlanz, S. |
| description | Two proteins, termed gp60 and p30, have been purified to homogeneity from bovine leukemia virus (BLV) using controlled pore glass and reverse-phase liquid chromatography (RPLC). gp60 was shown to be a glycoprotein by identification of glucosamine on the amino acid analyzer. Antiserum prepared to gp60 recognized in addition to gp60 a 52,000-Da polypeptide in some virus preparations, but did not cross-react with p30. The amino and carboxyl termini of gp60 were found to be tryptophan and arginine, respectively, and a 38-residue amino-terminal sequence of gp60 (NH
2TrpArgXSerLeuSerLeuGlyAsnG1nGlnTrpMetThrAlaTyrAsnGlnGluAlaLysPheSerIleSerIleAspGlnIleLeuGluAlaHisAsnGlnSerProPhe-) was obtained. A 12-residue amino-terminal sequence for p30 (NH
2SerProValAlaAlaLeuThrLeuGlySerAlaLeu) was also obtained. The p30 sequence showed substantial homology to the transmembrane proteins of both types B and C retroviruses and also to a deduced sequence of the 3′ region of the
env gene of human T-cell leukemia virus. From these results and from elution behavior of these proteins on RPLC, it was concluded that gp60 and p30 are the BLV
env gene-encoded surface glycoprotein and transmembrane protein, respectively. |
| doi_str_mv | 10.1016/0042-6822(84)90197-1 |
| format | Article |
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2TrpArgXSerLeuSerLeuGlyAsnG1nGlnTrpMetThrAlaTyrAsnGlnGluAlaLysPheSerIleSerIleAspGlnIleLeuGluAlaHisAsnGlnSerProPhe-) was obtained. A 12-residue amino-terminal sequence for p30 (NH
2SerProValAlaAlaLeuThrLeuGlySerAlaLeu) was also obtained. The p30 sequence showed substantial homology to the transmembrane proteins of both types B and C retroviruses and also to a deduced sequence of the 3′ region of the
env gene of human T-cell leukemia virus. From these results and from elution behavior of these proteins on RPLC, it was concluded that gp60 and p30 are the BLV
env gene-encoded surface glycoprotein and transmembrane protein, respectively.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/0042-6822(84)90197-1</identifier><identifier>PMID: 6204444</identifier><identifier>CODEN: VIRLAX</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Biological and medical sciences ; Cell Line ; Chiroptera ; Chromatography, High Pressure Liquid ; Electrophoresis, Polyacrylamide Gel ; Epitopes - analysis ; Fundamental and applied biological sciences. Psychology ; Glycoproteins - isolation & purification ; Immune Sera ; Kidney ; Leukemia Virus, Bovine - analysis ; Lung ; Microbiology ; Morphology, structure, chemical composition, physicochemical properties ; Retroviridae - analysis ; Sheep ; Species Specificity ; Viral Envelope Proteins - isolation & purification ; Virology</subject><ispartof>Virology (New York, N.Y.), 1984-01, Vol.135 (2), p.417-427</ispartof><rights>1984</rights><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-8f4c91d33367346f1f4d86ea496ab99b9305a79d5993ae28c9b8b3f4265424413</citedby><cites>FETCH-LOGICAL-c409t-8f4c91d33367346f1f4d86ea496ab99b9305a79d5993ae28c9b8b3f4265424413</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0042-6822(84)90197-1$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9690486$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6204444$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schultz, A.M.</creatorcontrib><creatorcontrib>Copeland, T.D.</creatorcontrib><creatorcontrib>Oroszlanz, S.</creatorcontrib><creatorcontrib>Empresa de Pesquisa Agropecuaria do Estado do Rio de Janeiro, Niteroi (Brazil)</creatorcontrib><title>The envelope proteins of bovine leukemia virus: Purification and sequence analysis</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Two proteins, termed gp60 and p30, have been purified to homogeneity from bovine leukemia virus (BLV) using controlled pore glass and reverse-phase liquid chromatography (RPLC). gp60 was shown to be a glycoprotein by identification of glucosamine on the amino acid analyzer. Antiserum prepared to gp60 recognized in addition to gp60 a 52,000-Da polypeptide in some virus preparations, but did not cross-react with p30. The amino and carboxyl termini of gp60 were found to be tryptophan and arginine, respectively, and a 38-residue amino-terminal sequence of gp60 (NH
2TrpArgXSerLeuSerLeuGlyAsnG1nGlnTrpMetThrAlaTyrAsnGlnGluAlaLysPheSerIleSerIleAspGlnIleLeuGluAlaHisAsnGlnSerProPhe-) was obtained. A 12-residue amino-terminal sequence for p30 (NH
2SerProValAlaAlaLeuThrLeuGlySerAlaLeu) was also obtained. The p30 sequence showed substantial homology to the transmembrane proteins of both types B and C retroviruses and also to a deduced sequence of the 3′ region of the
env gene of human T-cell leukemia virus. From these results and from elution behavior of these proteins on RPLC, it was concluded that gp60 and p30 are the BLV
env gene-encoded surface glycoprotein and transmembrane protein, respectively.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell Line</subject><subject>Chiroptera</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Epitopes - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins - isolation & purification</subject><subject>Immune Sera</subject><subject>Kidney</subject><subject>Leukemia Virus, Bovine - analysis</subject><subject>Lung</subject><subject>Microbiology</subject><subject>Morphology, structure, chemical composition, physicochemical properties</subject><subject>Retroviridae - analysis</subject><subject>Sheep</subject><subject>Species Specificity</subject><subject>Viral Envelope Proteins - isolation & purification</subject><subject>Virology</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kF1rFDEUhkNR2m3tP6iSCyl6MTWZnMkkXghS_IJCxbbXIZM5qdHZyZrMLPTfm3GXvTQ34XCevHl5CLng7IozLt8xBnUlVV2_UfBWM67bih-RFWdaVkwAf0ZWB-SEnOb8i5W5bdkxOZY1g3JW5Mf9T6Q4bnGIG6SbFCcMY6bR0y5uw4h0wPk3roOl25Dm_J5-n1PwwdkpxJHasacZ_8w4OiyDHZ5yyC_Ic2-HjOf7-4w8fP50f_21urn98u36403lgOmpUh6c5r0QQrYCpOceeiXRgpa207rTgjW21X2jtbBYK6c71QkPtWygBuDijFzuckvrUiFPZh2yw2GwI8Y5G8U5NLytCwg70KWYc0JvNimsbXoynJlFpVk8mcWTUWD-qTRL_st9_tytsT882rsr-9f7vc3ODj7Z0YV8wLTUDJQs2Ksd5m009jEV5OGOa9WUT0uUKMCHHYBF1jZgMtmFxWgfErrJ9DH8v-hfx8aXuA</recordid><startdate>19840101</startdate><enddate>19840101</enddate><creator>Schultz, A.M.</creator><creator>Copeland, T.D.</creator><creator>Oroszlanz, S.</creator><general>Elsevier Inc</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></search><sort><creationdate>19840101</creationdate><title>The envelope proteins of bovine leukemia virus: Purification and sequence analysis</title><author>Schultz, A.M. ; Copeland, T.D. ; Oroszlanz, S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-8f4c91d33367346f1f4d86ea496ab99b9305a79d5993ae28c9b8b3f4265424413</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell Line</topic><topic>Chiroptera</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Epitopes - analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins - isolation & purification</topic><topic>Immune Sera</topic><topic>Kidney</topic><topic>Leukemia Virus, Bovine - analysis</topic><topic>Lung</topic><topic>Microbiology</topic><topic>Morphology, structure, chemical composition, physicochemical properties</topic><topic>Retroviridae - analysis</topic><topic>Sheep</topic><topic>Species Specificity</topic><topic>Viral Envelope Proteins - isolation & purification</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schultz, A.M.</creatorcontrib><creatorcontrib>Copeland, T.D.</creatorcontrib><creatorcontrib>Oroszlanz, S.</creatorcontrib><creatorcontrib>Empresa de Pesquisa Agropecuaria do Estado do Rio de Janeiro, Niteroi (Brazil)</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><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schultz, A.M.</au><au>Copeland, T.D.</au><au>Oroszlanz, S.</au><aucorp>Empresa de Pesquisa Agropecuaria do Estado do Rio de Janeiro, Niteroi (Brazil)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The envelope proteins of bovine leukemia virus: Purification and sequence analysis</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>1984-01-01</date><risdate>1984</risdate><volume>135</volume><issue>2</issue><spage>417</spage><epage>427</epage><pages>417-427</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><coden>VIRLAX</coden><abstract>Two proteins, termed gp60 and p30, have been purified to homogeneity from bovine leukemia virus (BLV) using controlled pore glass and reverse-phase liquid chromatography (RPLC). gp60 was shown to be a glycoprotein by identification of glucosamine on the amino acid analyzer. Antiserum prepared to gp60 recognized in addition to gp60 a 52,000-Da polypeptide in some virus preparations, but did not cross-react with p30. The amino and carboxyl termini of gp60 were found to be tryptophan and arginine, respectively, and a 38-residue amino-terminal sequence of gp60 (NH
2TrpArgXSerLeuSerLeuGlyAsnG1nGlnTrpMetThrAlaTyrAsnGlnGluAlaLysPheSerIleSerIleAspGlnIleLeuGluAlaHisAsnGlnSerProPhe-) was obtained. A 12-residue amino-terminal sequence for p30 (NH
2SerProValAlaAlaLeuThrLeuGlySerAlaLeu) was also obtained. The p30 sequence showed substantial homology to the transmembrane proteins of both types B and C retroviruses and also to a deduced sequence of the 3′ region of the
env gene of human T-cell leukemia virus. From these results and from elution behavior of these proteins on RPLC, it was concluded that gp60 and p30 are the BLV
env gene-encoded surface glycoprotein and transmembrane protein, respectively.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>6204444</pmid><doi>10.1016/0042-6822(84)90197-1</doi><tpages>11</tpages></addata></record> |
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| ispartof | Virology (New York, N.Y.), 1984-01, Vol.135 (2), p.417-427 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; EZB-FREE-00999 freely available EZB journals |
| subjects | Amino Acid Sequence Animals Biological and medical sciences Cell Line Chiroptera Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel Epitopes - analysis Fundamental and applied biological sciences. Psychology Glycoproteins - isolation & purification Immune Sera Kidney Leukemia Virus, Bovine - analysis Lung Microbiology Morphology, structure, chemical composition, physicochemical properties Retroviridae - analysis Sheep Species Specificity Viral Envelope Proteins - isolation & purification Virology |
| title | The envelope proteins of bovine leukemia virus: Purification and sequence analysis |
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