Immunological evaluation of Escherichia coli-derived hepatitis C virus second envelope protein (E2) variants
: Two variants of the hepatitis C virus (HCV) E2 envelope protein, lacking the C‐terminal domain and comprising amino acids 458–650 (E2A) and 382–605 (E2C), respectively, were efficiently produced in BL21 (DE3) Escherichia coli cells. E2A and E2C were used to immunize mice. The E2C variant induced t...
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description | : Two variants of the hepatitis C virus (HCV) E2 envelope protein, lacking the C‐terminal domain and comprising amino acids 458–650 (E2A) and 382–605 (E2C), respectively, were efficiently produced in BL21 (DE3) Escherichia coli cells. E2A and E2C were used to immunize mice. The E2C variant induced the maximal mean antibody titer. Anti‐E2C mouse sera reacted mainly with E2 synthetic peptides covering the 70 amino acid N‐terminal region of the E2 protein. Moreover, a panel of anti‐HCV positive human sera recognized only the E2C protein (28.2%) and the synthetic peptide covering the HVR‐1 of the E2 protein (23.1%). These data indicate the existence of an immunologically relevant region in the HVR‐1 of the HCV E2 protein. |
doi_str_mv | 10.1034/j.1399-3011.2001.00795.x |
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E2A and E2C were used to immunize mice. The E2C variant induced the maximal mean antibody titer. Anti‐E2C mouse sera reacted mainly with E2 synthetic peptides covering the 70 amino acid N‐terminal region of the E2 protein. Moreover, a panel of anti‐HCV positive human sera recognized only the E2C protein (28.2%) and the synthetic peptide covering the HVR‐1 of the E2 protein (23.1%). These data indicate the existence of an immunologically relevant region in the HVR‐1 of the HCV E2 protein.</description><identifier>ISSN: 1397-002X</identifier><identifier>EISSN: 1399-3011</identifier><identifier>DOI: 10.1034/j.1399-3011.2001.00795.x</identifier><identifier>PMID: 11576328</identifier><language>eng</language><publisher>Copenhagen, Denmark: Munksgaard International Publishers</publisher><subject>Animals ; anti-HCV ; Antigen-Antibody Reactions - immunology ; E2 protein ; Escherichia coli - genetics ; Escherichia coli ; Hepatitis C Antibodies - immunology ; Humans ; immune recognition ; Immune Sera - immunology ; Mice ; Peptides - chemical synthesis ; Peptides - immunology ; Recombinant Proteins - genetics ; Recombinant Proteins - immunology ; Recombinant Proteins - isolation & purification ; synthetic peptides ; Viral Envelope Proteins - genetics ; Viral Envelope Proteins - immunology ; Viral Envelope Proteins - isolation & purification ; Viral Proteins - immunology</subject><ispartof>The journal of peptide research, 2001-09, Vol.58 (3), p.221-228</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4035-308c6e9c3abeeea75979971009997dec4d8a4847303b2d62bb139f67c1fb7e8c3</citedby><cites>FETCH-LOGICAL-c4035-308c6e9c3abeeea75979971009997dec4d8a4847303b2d62bb139f67c1fb7e8c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1034%2Fj.1399-3011.2001.00795.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1034%2Fj.1399-3011.2001.00795.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11576328$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dueñas-Carrera, S.</creatorcontrib><creatorcontrib>Viña, A.</creatorcontrib><creatorcontrib>Garay, H.E.</creatorcontrib><creatorcontrib>Reyes, O.</creatorcontrib><creatorcontrib>Alvarez-Lajonchere, L.</creatorcontrib><creatorcontrib>Guerra, I.</creatorcontrib><creatorcontrib>González, L.J.</creatorcontrib><creatorcontrib>Morales, J.</creatorcontrib><title>Immunological evaluation of Escherichia coli-derived hepatitis C virus second envelope protein (E2) variants</title><title>The journal of peptide research</title><addtitle>J Pept Res</addtitle><description>: Two variants of the hepatitis C virus (HCV) E2 envelope protein, lacking the C‐terminal domain and comprising amino acids 458–650 (E2A) and 382–605 (E2C), respectively, were efficiently produced in BL21 (DE3) Escherichia coli cells. E2A and E2C were used to immunize mice. The E2C variant induced the maximal mean antibody titer. Anti‐E2C mouse sera reacted mainly with E2 synthetic peptides covering the 70 amino acid N‐terminal region of the E2 protein. Moreover, a panel of anti‐HCV positive human sera recognized only the E2C protein (28.2%) and the synthetic peptide covering the HVR‐1 of the E2 protein (23.1%). These data indicate the existence of an immunologically relevant region in the HVR‐1 of the HCV E2 protein.</description><subject>Animals</subject><subject>anti-HCV</subject><subject>Antigen-Antibody Reactions - immunology</subject><subject>E2 protein</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli</subject><subject>Hepatitis C Antibodies - immunology</subject><subject>Humans</subject><subject>immune recognition</subject><subject>Immune Sera - immunology</subject><subject>Mice</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - immunology</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - immunology</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>synthetic peptides</subject><subject>Viral Envelope Proteins - genetics</subject><subject>Viral Envelope Proteins - immunology</subject><subject>Viral Envelope Proteins - isolation & purification</subject><subject>Viral Proteins - immunology</subject><issn>1397-002X</issn><issn>1399-3011</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEFv0zAUxy3ExMbGV5h8QnBIZseJnRw4QFvGpGrTJBDVLpbjvFAXJy52Erpvj7tW47rTe5Z__-fnH0KYkpQSll9tUsqqKmGE0jQjhKaEiKpId6_Q2fPF66deJIRkq1P0NoRNBFnG-Bt0SmkhOMvKM2Rvum7snXW_jFYWw6TsqAbjeuxavAh6Dd7otVFYO2uSJp4maPAathEaTMAzPBk_BhxAu77B0E9g3Rbw1rsBTI8_LLKPeFLeqH4IF-ikVTbAu2M9Rz--Lr7PviXLu-ub2edlonPCirh9qTlUmqkaAJQoKlFVghJSxdKAzptS5WUuGGF11vCsruNHWy40bWsBpWbn6P1hbtzizwhhkJ0JGqxVPbgxSEGjNM55BMsDqL0LwUMrt950yj9KSuTetNzIvVC5Fyr3puWTabmL0cvjG2PdQfM_eFQbgU8H4K-x8PjiwXL2ZT6PXcwnh7wJA-ye88r_llwwUcift9dy-cDn96sVlffsH4WhnQM</recordid><startdate>200109</startdate><enddate>200109</enddate><creator>Dueñas-Carrera, S.</creator><creator>Viña, A.</creator><creator>Garay, H.E.</creator><creator>Reyes, O.</creator><creator>Alvarez-Lajonchere, L.</creator><creator>Guerra, I.</creator><creator>González, L.J.</creator><creator>Morales, J.</creator><general>Munksgaard International Publishers</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>200109</creationdate><title>Immunological evaluation of Escherichia coli-derived hepatitis C virus second envelope protein (E2) variants</title><author>Dueñas-Carrera, S. ; Viña, A. ; Garay, H.E. ; Reyes, O. ; Alvarez-Lajonchere, L. ; Guerra, I. ; González, L.J. ; Morales, J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4035-308c6e9c3abeeea75979971009997dec4d8a4847303b2d62bb139f67c1fb7e8c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Animals</topic><topic>anti-HCV</topic><topic>Antigen-Antibody Reactions - immunology</topic><topic>E2 protein</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli</topic><topic>Hepatitis C Antibodies - immunology</topic><topic>Humans</topic><topic>immune recognition</topic><topic>Immune Sera - immunology</topic><topic>Mice</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - immunology</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - immunology</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>synthetic peptides</topic><topic>Viral Envelope Proteins - genetics</topic><topic>Viral Envelope Proteins - immunology</topic><topic>Viral Envelope Proteins - isolation & purification</topic><topic>Viral Proteins - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dueñas-Carrera, S.</creatorcontrib><creatorcontrib>Viña, A.</creatorcontrib><creatorcontrib>Garay, H.E.</creatorcontrib><creatorcontrib>Reyes, O.</creatorcontrib><creatorcontrib>Alvarez-Lajonchere, L.</creatorcontrib><creatorcontrib>Guerra, I.</creatorcontrib><creatorcontrib>González, L.J.</creatorcontrib><creatorcontrib>Morales, J.</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>The journal of peptide research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dueñas-Carrera, S.</au><au>Viña, A.</au><au>Garay, H.E.</au><au>Reyes, O.</au><au>Alvarez-Lajonchere, L.</au><au>Guerra, I.</au><au>González, L.J.</au><au>Morales, J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immunological evaluation of Escherichia coli-derived hepatitis C virus second envelope protein (E2) variants</atitle><jtitle>The journal of peptide research</jtitle><addtitle>J Pept Res</addtitle><date>2001-09</date><risdate>2001</risdate><volume>58</volume><issue>3</issue><spage>221</spage><epage>228</epage><pages>221-228</pages><issn>1397-002X</issn><eissn>1399-3011</eissn><abstract>: Two variants of the hepatitis C virus (HCV) E2 envelope protein, lacking the C‐terminal domain and comprising amino acids 458–650 (E2A) and 382–605 (E2C), respectively, were efficiently produced in BL21 (DE3) Escherichia coli cells. E2A and E2C were used to immunize mice. The E2C variant induced the maximal mean antibody titer. Anti‐E2C mouse sera reacted mainly with E2 synthetic peptides covering the 70 amino acid N‐terminal region of the E2 protein. Moreover, a panel of anti‐HCV positive human sera recognized only the E2C protein (28.2%) and the synthetic peptide covering the HVR‐1 of the E2 protein (23.1%). These data indicate the existence of an immunologically relevant region in the HVR‐1 of the HCV E2 protein.</abstract><cop>Copenhagen, Denmark</cop><pub>Munksgaard International Publishers</pub><pmid>11576328</pmid><doi>10.1034/j.1399-3011.2001.00795.x</doi><tpages>8</tpages></addata></record> |
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subjects | Animals anti-HCV Antigen-Antibody Reactions - immunology E2 protein Escherichia coli - genetics Escherichia coli Hepatitis C Antibodies - immunology Humans immune recognition Immune Sera - immunology Mice Peptides - chemical synthesis Peptides - immunology Recombinant Proteins - genetics Recombinant Proteins - immunology Recombinant Proteins - isolation & purification synthetic peptides Viral Envelope Proteins - genetics Viral Envelope Proteins - immunology Viral Envelope Proteins - isolation & purification Viral Proteins - immunology |
title | Immunological evaluation of Escherichia coli-derived hepatitis C virus second envelope protein (E2) variants |
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