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Antigenic and immunogenic properties of a chimera of two immunodominant African swine fever virus proteins

ARCHIVES OF VIROLOGY 2001年第9期146卷 1681-1691页

作者： Barderas, MG Rodríguez, F Gómez-Puertas, P Avilés, M Beitia, F Alonso, C Escribano, JM INIA Dept Biotecnol Madrid 28040 Spain INIA Dept Protecc Vegetal Madrid 28040 Spain

A chimera of the two immunodominant African swine fever (ASF) virus proteins p54 and p30 was constructed by insertion of the gene CP204L into a Not I restriction site of E183L gene. The resulting chimeric protein p54/30, expressed by a recombinant baculovirus in insect cells and in Trichoplusia ni larvae, retained antigenic determinants present in both proteins and reacted in Western blot with a collection of sera from inapparent ASF virus carrier pigs. Remarkably, pigs immunized with the chimeric protein developed neutralizing antibodies and survived the challenge with a virulent African swine fever virus, presenting a reduction of about two logs in maximum viremia titers with respect to control pigs. In conclusion, this study revealed that the constructed chimeric protein may have utility as a serological diagnostic reagent and for further immunological studies that may provide new insights on mechanisms of protective immunity to ASFV.

关键词：非洲猪瘟/诊断非洲猪瘟/预防和控制非洲猪瘟/病毒学非洲猪瘟病毒/免疫学抗体病毒/血液杆状病毒科/遗传学杆状病毒科/代谢细胞培养的免疫印迹法免疫显性表位/遗传学免疫显性表位/免疫学免疫显性表位/代谢巨噬细胞肺泡/病毒学蛾/病毒学中和试验磷蛋白类/遗传学磷蛋白类/免疫学磷蛋白类/代谢重组融合蛋白质类/遗传学重组融合蛋白质类/免疫学重组融合蛋白质类/代谢斜纹夜蛾属猪接种病毒蛋白质类/遗传学病毒蛋白质类/免疫学病毒蛋白质类/代谢病毒结构蛋白质类/遗传学病毒结构蛋白质类/免疫学病毒结构蛋白质类/代谢病毒疫苗/遗传学病毒疫苗/免疫学动物

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Presentation of antigenic sites from foot-and-mouth disease virus on the surface of baculovirus and in the membrane of infected cells

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ARCHIVES OF VIROLOGY 2000年第9期145卷 1815-1828页

作者： Tami, C Farber, M Palma, EL Taboga, O INTA CICVyA Inst Biotecnol Buenos Aires DF Argentina

We describe the construction of recombinant baculoviruses displaying on their surface and in the membrane of infected cells the small, immunodominant antigenic site (site A) or the large polyprotein (P1) coding for the four structural proteins of foot-and-mouth disease virus (FMDV). The coding sequences were inserted in the amino-terminus of gp64, the major glycoprotein of the baculovirus Autographa californica nuclear polyhedrosis virus (AcNPV). Following infection of insect cells with the recombinant baculoviruses, the cellular localization of the chimaeric proteins as well as their presence in the surface of extracellular viruses was assessed by immunofluorescence microscopy and Western blot. The antigenicity of the recombinant viruses was studied by competitive ELISAs, which showed that although both recombinant viruses were able to compete with FMDV-specific monoclonal antibodies (MAbs), their patterns of reactivity were different. The results suggest that this eukaryotic display system could be an alternative method of presentation of foreign antigens in a multimeric form as a new approach to biosynthetic vaccines.

关键词：抗原病毒/遗传学抗原病毒/免疫学抗原病毒/代谢结合部位印迹法蛋白质病毒壳体/遗传学病毒壳体/免疫学病毒壳体/代谢衣壳蛋白质类细胞系细胞膜/病毒学酶联免疫吸附测定荧光抗体技术核多角体病毒属/遗传学核多角体病毒属/代谢细小RNA病毒科/遗传学细小RNA病毒科/免疫学重组融合蛋白质类/代谢转化遗传病毒融合蛋白质类/遗传学病毒融合蛋白质类/代谢病毒结构蛋白质类/遗传学病毒结构蛋白质类/免疫学病毒结构蛋白质类/代谢动物

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Epitope-tagging approach to determine the stoichiometry of the structural and nonstructural proteins in the virus particles: Amount of Vpr in relation to Gag in HIV-1

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VIROLOGY 2000年第2期268卷 364-371页

作者： Singh, SP Lai, D Cartas, M Serio, D Murali, R Kalyanaraman, VS Srinivasan, A Thomas Jefferson Univ Kimmel Canc Ctr Dept Microbiol & Immunol Philadelphia PA 19107 USA Univ Penn Dept Pathol & Lab Med Philadelphia PA 19104 USA Adv Biosci Labs Inc Kensington MD 20895 USA

We used an epitope-tagging approach to determine the ratio of Gag (structural) to Vpr (nonstructural) in the virus particles directed by human immunodeficiency virus type 1. For this purpose, chimeric Gag and Vpr expression plasmids were constructed with the Flag epitope (DYKDDDDK), and the sequences corresponding to the chimeric protein were Introduced into human immunodeficiency virus type 1 proviral DNA (NL4-3) to determine the ratio in the virus particles when these proteins are expressed in cis. In addition, NL4-3 DNA was modified to disrupt Vpr synthesis to determine the extent of incorporation of Vpr-FL when it is expressed in trans through a heterologous promoter, The analysis of virus particles generated by transfection of proviral DNA into RD cells indicated that (1) the ratio of Gag to Vpr in virus particles, when Vpr-FL is expressed in cis (in the context of proviral DNA), is in the range of 150-200:1 (14-18 molecules of Vpr per virion) and (2) the expression of Vpr-FL in trans showed efficient incorporation with a Gag to Vpr ratio of 5-7:1 (392-550 molecules of Vpr). These results suggest that the presence of the same epitope on different viral proteins may provide an accurate comparison of these proteins in the virus particles. (C) 2000 Academic Press.

关键词：表位作图/方法表位/代谢基因产物 vpr/生物合成基因产物 vpr/遗传学基因产物 vpr/免疫学基因产物 vpr/代谢 HIV核心蛋白质p24/生物合成 HIV核心蛋白质p24/遗传学 HIV核心蛋白质p24/免疫学 HIV核心蛋白质p24/代谢肽类/遗传学肽类/免疫学肽类/代谢质粒/化学合成质粒/免疫学肿瘤细胞培养的病毒非结构蛋白质类/生物合成病毒非结构蛋白质类/遗传学病毒非结构蛋白质类/免疫学病毒非结构蛋白质类/代谢病毒结构蛋白质类/生物合成病毒结构蛋白质类/遗传学病毒结构蛋白质类/免疫学病毒结构蛋白质类/代谢病毒粒子/遗传学病毒粒子/代谢人类

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Identification and characterization of a structural protein of hepatitis B virus: A polymerase and surface fusion protein encoded by a spliced RNA

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VIROLOGY 2000年第2期275卷 398-410页

作者： Huang, HL Jeng, KS Hu, CP Tsai, CH Lo, SJ Chang, CM Natl Yang Ming Univ Sch Life Sci Inst Microbiol & Immunol Taipei 112 Taiwan Natl Hlth Res Inst Div Mol & Genom Med Res Taipei 115 Taiwan Vet Gen Hosp Dept Med Res Taipei 112 Taiwan

The hepatitis B virus (HBV) genome is known to contain four conserved and overlapped open reading frames (ORFs) encoding the viral core, polymerase (P), surface (S), and X proteins. Whether HBV encodes other proteins has long been a major interest in the field. Using P-32-labeling of an introduced protein kinase A site attached to the N- or C-terminus of the HBV polymerase gene, a 43-kDa P-S fusion protein was detected in cell lysate, secreted virions, and 22-nm subviral particles. Immunobiochemical studies showed that the 43-kDa protein contains the epitopes of the N-terminus of polymerase and most parts of the surface proteins This 43-kDa protein was shown to be a glycoprotein, similar to the surface protein. RT-PCR and sequence analyses identified a spliced mRNA which was derived from pregenomic RNA with a deletion of 454 nucleotides (nt) from nt 2447 to 2902. This splice event creates a P-S fusion ORF This finding is consistent with the result obtained from an immunobiochemical study. Mutations at the splice donor or acceptor site on the HBV genome abrogated the production of the 43-kDa protein. These mutants had no effect on viral replication in transfected HuH-7 cells. However, this P-S fusion protein is able to substitute for the LS protein in Virion maturation. On the basis of these results, we conclude that the 43-kDa protein is a polymerase-surface fusion protein encoded by a spliced RNA Similar to the LS protein, the 43-kDa P-S fusion protein is a structural protein of HBV and might play a role in the HBV life cycle. (C) 2000 Academic Press.

关键词：天冬氨酸内肽酶类/遗传学细胞系电泳聚丙烯酰氨凝胶表位基因产物 pol/遗传学糖蛋白类/遗传学糖蛋白类/代谢糖基化肝炎表面抗原乙型/遗传学肝炎病毒乙型/遗传学肝炎病毒乙型/代谢分子量开放读码框架沉淀素试验 RNA剪接逆转录聚合酶链反应病毒融合蛋白质类/遗传学病毒融合蛋白质类/代谢病毒结构蛋白质类/遗传学病毒结构蛋白质类/代谢人类

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Virus-like particles of calicivirus as epitope carriers

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ARCHIVES OF VIROLOGY 1999年第12期144卷 2429-2439页

作者： Nagesha, HS Wang, LF Hyatt, AD CSIRO Australian Anim Hlth Lab Geelong Vic Australia

The VP60 of rabbit haemorrhagic disease virus (RHDV), when expressed in baculovirus, self-assembles into virus-like particles (VLP) which are antigenically and immunogenically indistinguishable from native virions. When the N-terminal 30 amino acid residues of VP60 were deleted and substituted by a well characterized six residue epitope from bluetongue virus capsid protein VP7 (B tag), the fusion protein retained its ability to self-assemble into VLPs. However, the size of these particles was only 27 nm, compared to 40 nm of VLPs derived from native VP60. The antigenicity of both VP60 and the Btag was retained as evident from ELISA and Western blot analyses. When Btag was fused at the C-terminus of VP60 without deletion, the fusion proteins formed VLPs of 40 nm in size and also retained their antigenicity, but the Brag antigenicity appeared weak at this fusion site.

关键词：氨基酸序列杆状病毒科/遗传学碱基序列印迹法蛋白质病毒壳体/免疫学衣壳蛋白质类细胞系酶联免疫吸附测定表位/免疫学出血病病毒兔/免疫学显微镜检查电子分子序列数据质粒/遗传学重组融合蛋白质类/免疫学斜纹夜蛾属病毒结构蛋白质类/免疫学病毒结构蛋白质类/代谢病毒粒子/免疫学病毒装配动物兔

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Sequence and initial characterization of the U_L10 (glycoprotein M) and U_L11 homologous genes of serotype 1 Marek's Disease Virus

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ARCHIVES OF VIROLOGY 1999年第9期144卷 1853-1863页

作者： Osterrieder, N Fed Res Ctr Virus Dis Anim Friedrich Loeffler Inst Inst Mol Biol D-17498 Insel Reims Germany

The nucleotide sequence of the U-L 10 (glycoprotein M) and the U-L 11 homologs of Marek's Disease Virus 1 strain GA was determined. The UL10 open reading frame encodes a type III membrane protein of 424 amino acids that contains eight hydrophobic domains and two consensus N-linked glycosylation sites. The U(L)11 homologous gene encodes an 84 amino acid polypeptide, and contains a highly conserved myristylation site at its aminoterminus. By analysis of infected-cell RNA with strand-specific RNA probes, transcription of both U(L)10 and U-L 11 in infected cells was demonstrated. Coupled in vitro transcription-translation confirmed that the U-L 10 product is a 47 kD N-glycosylated viral protein that aggregated upon boiling, whereas the U-L 11 protein exhibited a size of 12 kD after in vitro translation.

关键词：氨基酸序列细胞系鸭糖蛋白类/化学糖蛋白类/遗传学糖蛋白类/代谢疱疹病毒2型鹑鸡/化学疱疹病毒2型鹑鸡/遗传学疱疹病毒2型鹑鸡/生理学分子序列数据转录遗传病毒蛋白质类/化学病毒蛋白质类/遗传学病毒蛋白质类/代谢病毒结构蛋白质类/化学病毒结构蛋白质类/遗传学病毒结构蛋白质类/代谢动物

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