Proteolytic processing in African swine fever virus: evidence for a new structural polyprotein, pp62
We have identified an open reading frame (ORF), CP530R, within the EcoRI C' fragment of the African swine fever virus (ASFV) genome that encodes a polyprotein of 62 kDa (pp62). Antisera raised against different regions of ORF CP530R recognized a polypeptide of 62 kDa in ASFV-infected cells duri...
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| Veröffentlicht in: | Journal of Virology 1997-08, Vol.71 (8), p.5799-5804 |
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| creator | Simon-Mateo, C Andres, G Almazan, F Vinuela, E |
| description | We have identified an open reading frame (ORF), CP530R, within the EcoRI C' fragment of the African swine fever virus (ASFV) genome that encodes a polyprotein of 62 kDa (pp62). Antisera raised against different regions of ORF CP530R recognized a polypeptide of 62 kDa in ASFV-infected cells during the late phase of virus replication, after the onset of viral DNA synthesis. Pulse-chase experiments showed that polyprotein pp62 is posttranslationally processed to give rise to two proteins of 35 kDa (p35) and 15 kDa (p15). This proteolytic processing was found to take place at the consensus sequence Gly-Gly-X through an ordered cascade of proteolytic cleavages like that which also occurs with ASFV polyprotein pp220 (C. Simon-Mateo, G. Andres, and E. Vinuela, EMBO J. 12:2977-2987, 1993). Immunofluorescence studies showed that polyprotein pp62 is localized in the viral factories. In addition, immunoprecipitation analysis of purified virus particles showed that mature products p35 and p15 are major structural proteins. According to these results, polyprotein processing represents an essential strategy for the maturation of ASFV structural proteins. |
| doi_str_mv | 10.1128/JVI.71.8.5799-5804.1997 |
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Antisera raised against different regions of ORF CP530R recognized a polypeptide of 62 kDa in ASFV-infected cells during the late phase of virus replication, after the onset of viral DNA synthesis. Pulse-chase experiments showed that polyprotein pp62 is posttranslationally processed to give rise to two proteins of 35 kDa (p35) and 15 kDa (p15). This proteolytic processing was found to take place at the consensus sequence Gly-Gly-X through an ordered cascade of proteolytic cleavages like that which also occurs with ASFV polyprotein pp220 (C. Simon-Mateo, G. Andres, and E. Vinuela, EMBO J. 12:2977-2987, 1993). Immunofluorescence studies showed that polyprotein pp62 is localized in the viral factories. In addition, immunoprecipitation analysis of purified virus particles showed that mature products p35 and p15 are major structural proteins. According to these results, polyprotein processing represents an essential strategy for the maturation of ASFV structural proteins.</description><identifier>ISSN: 0022-538X</identifier><identifier>EISSN: 1098-5514</identifier><identifier>DOI: 10.1128/JVI.71.8.5799-5804.1997</identifier><identifier>PMID: 9223468</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>African swine fever virus ; African Swine Fever Virus - genetics ; African Swine Fever Virus - metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Cercopithecus aethiops ; Molecular Sequence Data ; Molecular Weight ; Open Reading Frames ; proteinas ; proteine ; proteins ; proteolisis ; proteolyse ; proteolysis ; Vero Cells ; Viral Structural Proteins - analysis ; Viral Structural Proteins - metabolism ; virus de la peste porcina africana ; virus peste porcine africaine</subject><ispartof>Journal of Virology, 1997-08, Vol.71 (8), p.5799-5804</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c477t-509f5a06e712ae0f383a4b631c26a328ddc9e8c44fd8592ee27978c303030a7b3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC191834/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC191834/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,725,778,782,883,27911,27912,53778,53780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9223468$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Simon-Mateo, C</creatorcontrib><creatorcontrib>Andres, G</creatorcontrib><creatorcontrib>Almazan, F</creatorcontrib><creatorcontrib>Vinuela, E</creatorcontrib><creatorcontrib>University of Gent, Gent, Belgium</creatorcontrib><title>Proteolytic processing in African swine fever virus: evidence for a new structural polyprotein, pp62</title><title>Journal of Virology</title><addtitle>J Virol</addtitle><description>We have identified an open reading frame (ORF), CP530R, within the EcoRI C' fragment of the African swine fever virus (ASFV) genome that encodes a polyprotein of 62 kDa (pp62). Antisera raised against different regions of ORF CP530R recognized a polypeptide of 62 kDa in ASFV-infected cells during the late phase of virus replication, after the onset of viral DNA synthesis. Pulse-chase experiments showed that polyprotein pp62 is posttranslationally processed to give rise to two proteins of 35 kDa (p35) and 15 kDa (p15). This proteolytic processing was found to take place at the consensus sequence Gly-Gly-X through an ordered cascade of proteolytic cleavages like that which also occurs with ASFV polyprotein pp220 (C. Simon-Mateo, G. Andres, and E. Vinuela, EMBO J. 12:2977-2987, 1993). Immunofluorescence studies showed that polyprotein pp62 is localized in the viral factories. In addition, immunoprecipitation analysis of purified virus particles showed that mature products p35 and p15 are major structural proteins. According to these results, polyprotein processing represents an essential strategy for the maturation of ASFV structural proteins.</description><subject>African swine fever virus</subject><subject>African Swine Fever Virus - genetics</subject><subject>African Swine Fever Virus - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Cercopithecus aethiops</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Open Reading Frames</subject><subject>proteinas</subject><subject>proteine</subject><subject>proteins</subject><subject>proteolisis</subject><subject>proteolyse</subject><subject>proteolysis</subject><subject>Vero Cells</subject><subject>Viral Structural Proteins - analysis</subject><subject>Viral Structural Proteins - metabolism</subject><subject>virus de la peste porcina africana</subject><subject>virus peste porcine africaine</subject><issn>0022-538X</issn><issn>1098-5514</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV9rFDEUxQdR6rb6EdT44pMz5u8kKfhQStVKQUErvoVs5s5uymwyJjOz9Ns7wy7FPsl9CNxzzo8bTlG8IbgihKoPX39dV5JUqhJS61IozCuitXxSrAjWqhSC8KfFCmNKS8HU7-fFac53GBPOa35SnGhKGa_Vqmi-pzhA7O4H71CfooOcfdggH9BFm7yzAeW9D4BamCChyacxnyOYfAPBzduYkEUB9igPaXTDmGyH-hnXL1gf3qO-r-mL4llruwwvj-9Zcfvp6ufll_Lm2-fry4ub0nEph1Jg3QqLa5CEWsAtU8zydc2Io7VlVDWN06Ac522jhKYAVGqpHMPLWLlmZ8XHA7cf1ztoHIRhvsf0ye9sujfRevNYCX5rNnEyRBPF-Jx_d8yn-GeEPJidzw66zgaIYzZSEyaopP81khozURM9G-XB6FLMOUH7cAzBZinS3E3eSGKUWYo0S5FmKXJOvvr3Lw-5Y3Oz_vagb_1mu_cJjM27x7TZ8_rgaW00dpN8Nrc_Fjomggih2F-kLrDY</recordid><startdate>19970801</startdate><enddate>19970801</enddate><creator>Simon-Mateo, C</creator><creator>Andres, G</creator><creator>Almazan, F</creator><creator>Vinuela, E</creator><general>American Society for Microbiology</general><scope>FBQ</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>7U9</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19970801</creationdate><title>Proteolytic processing in African swine fever virus: evidence for a new structural polyprotein, pp62</title><author>Simon-Mateo, C ; Andres, G ; Almazan, F ; Vinuela, E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c477t-509f5a06e712ae0f383a4b631c26a328ddc9e8c44fd8592ee27978c303030a7b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>African swine fever virus</topic><topic>African Swine Fever Virus - genetics</topic><topic>African Swine Fever Virus - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Cercopithecus aethiops</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Open Reading Frames</topic><topic>proteinas</topic><topic>proteine</topic><topic>proteins</topic><topic>proteolisis</topic><topic>proteolyse</topic><topic>proteolysis</topic><topic>Vero Cells</topic><topic>Viral Structural Proteins - analysis</topic><topic>Viral Structural Proteins - metabolism</topic><topic>virus de la peste porcina africana</topic><topic>virus peste porcine africaine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Simon-Mateo, C</creatorcontrib><creatorcontrib>Andres, G</creatorcontrib><creatorcontrib>Almazan, F</creatorcontrib><creatorcontrib>Vinuela, E</creatorcontrib><creatorcontrib>University of Gent, Gent, Belgium</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of Virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Simon-Mateo, C</au><au>Andres, G</au><au>Almazan, F</au><au>Vinuela, E</au><aucorp>University of Gent, Gent, Belgium</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteolytic processing in African swine fever virus: evidence for a new structural polyprotein, pp62</atitle><jtitle>Journal of Virology</jtitle><addtitle>J Virol</addtitle><date>1997-08-01</date><risdate>1997</risdate><volume>71</volume><issue>8</issue><spage>5799</spage><epage>5804</epage><pages>5799-5804</pages><issn>0022-538X</issn><eissn>1098-5514</eissn><abstract>We have identified an open reading frame (ORF), CP530R, within the EcoRI C' fragment of the African swine fever virus (ASFV) genome that encodes a polyprotein of 62 kDa (pp62). Antisera raised against different regions of ORF CP530R recognized a polypeptide of 62 kDa in ASFV-infected cells during the late phase of virus replication, after the onset of viral DNA synthesis. Pulse-chase experiments showed that polyprotein pp62 is posttranslationally processed to give rise to two proteins of 35 kDa (p35) and 15 kDa (p15). This proteolytic processing was found to take place at the consensus sequence Gly-Gly-X through an ordered cascade of proteolytic cleavages like that which also occurs with ASFV polyprotein pp220 (C. Simon-Mateo, G. Andres, and E. Vinuela, EMBO J. 12:2977-2987, 1993). Immunofluorescence studies showed that polyprotein pp62 is localized in the viral factories. In addition, immunoprecipitation analysis of purified virus particles showed that mature products p35 and p15 are major structural proteins. According to these results, polyprotein processing represents an essential strategy for the maturation of ASFV structural proteins.</abstract><cop>United States</cop><pub>American Society for Microbiology</pub><pmid>9223468</pmid><doi>10.1128/JVI.71.8.5799-5804.1997</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | African swine fever virus African Swine Fever Virus - genetics African Swine Fever Virus - metabolism Amino Acid Sequence Animals Base Sequence Cercopithecus aethiops Molecular Sequence Data Molecular Weight Open Reading Frames proteinas proteine proteins proteolisis proteolyse proteolysis Vero Cells Viral Structural Proteins - analysis Viral Structural Proteins - metabolism virus de la peste porcina africana virus peste porcine africaine |
| title | Proteolytic processing in African swine fever virus: evidence for a new structural polyprotein, pp62 |
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