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Assembly and Immunogenicity of Human Papillomavirus Type 16 major capsid protein(HPV16 L1) in Pichia pastoris

Chemical Research in Chinese Universities 2007年第2期23卷 200-203页

作者： LIU Da-wei ZHANG Yu YU Xiang-hui JIANG Chun-lai CHEN Yue WU Yong-ge JIN Ying-hua NIU Jun Qu Ning LIU Ming KONG Wei Vaccine Research Center College of Life Science Jilin University Changchun 130023 P. R. China

In this study, a recombinant Pichia pastoris expression system was developed to express HPV16 L1 protein that was driven by a strong AOX1 promoter. HPV16L1 gene was cloned into vector pPICZ,αB. HPV16 L1 protein expression induced by methanol was screened by using sodium dedecyl sulfate-polyacrylamide gel electrophoresis （SDSPAGE） and Western blotting. The results indicate that the HPVl6 L1 protein is secreted by the recombinant P. pastoris, and the purified HPV16 L1 protein can self-assemble into vires-like particles（ VLPs）, which show a good immunogenicity and induces high-titer antibody in mice.

关键词： Human papillomavirus major capsid protein Recombinant Pichia pastoris Vires-like particles

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protein interactions in the murine cytomegalovirus capsid revealed by cryoEM

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protein & Cell 2013年第11期4卷 833-845页

作者： Wong HHui Qiyi Tang Hongrong Liu Ivo Atanasov Fenyong Liu Hua Zhu ZHong Zhou The California NanoSystems Institute(CNSI) University of CaliforniaLos Angeles(UCLA)Los AngelesCA 90095USA Department of Microbiology Immunology and Molecular GeneticsUCLALos AngelesCA 90095USA D epartment of Microbiology/AIDS program Ponce School of Medicine395 Zona IndustrialReparadara-2PoncePR 00716USA School of Public Health University of California at BerkeleyBerkeleyCA 94720USA Department of Microbiology and Molecular Genetics International Center for Public Health(or ICPH)Room E350D225 Warren StreetUMDNJ-New Jersey Medical SchoolNewarkNJ 07103USA Current address:College of Physics and Information Science Hunan Normal UniversityChangsha 410081China

Cytomegalovirus(CMV)is distinct among members of the Herpesviridae family for having the largest dsDNA genome(230 kb).Packaging of large dsDNA genome is known to give rise to a highly pressurized viral capsid,but molecular interactions conducive to the formation of CMV capsid resistant to pressurization have not been ***,we report a cryo electron microscopy(cryoEM)structure of the murine cytomegalovirus(MCMV)capsid at a 9.1Åresolution and describe the molecular interactions among the~3000 protein molecules in the MCMV capsid at the secondary structure *** structural elements are resolved to provide landmarks for correlating with results from sequence-based prediction and for structure-based homology *** major capsid protein(MCP)upper domain(MCPud)containsα-helices andβ-sheets conserved with those in MCPud of herpes simplex virus type 1(HSV-1),with the largest differences identifi ed as a“saddle loop”region,located at the tip of MCPud and involved in interaction with the smallest capsid protein(SCP).Interactions among the bacteriophage HK97-like fl oor domain of MCP,the middle domain of MCP,the hook and clamp domains of the triplex proteins(hoop and clamp domains of TRI-1 and clamp domain of TRI-2)contribute to the formation of a mature *** results offer a framework for understanding how cytomegalovirus uses various secondary structural elements of its capsid proteins to build a robust capsid for packaging its large dsDNA genome inside and for attach-ing unique functional tegument proteins outside.

关键词： cytomegalovirus herpes simplex virus type 1 cryo electron microscopy three-dimensional major capsid protein

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Functional Inferences of Environmental Coccolithovirus Biodiversity

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Virologica Sinica 2013年第5期28卷 291-302页

作者： Jozef I Nissimov Mark Jones Johnathan A Napier Colin B Munn Susan A Kimmance Michael J Allen Plymouth Marine Laboratory Prospect Place University of Nottingham School of BiosciencesSutton Bonington Campus Department of Biological Chemistry Rothamsted Research School of Marine Science & Engineering Plymouth University

The cosmopolitan calcifying alga Emiliania huxleyi is one of the most abundant bloom forming coccolithophore species in the oceans and plays an important role in global biogeochemical cycling. Coccolithoviruses are a major cause of coccolithophore bloom termination and have been studied in laboratory, mesocosm and open ocean studies. However, little is known about the dynamic interactions between the host and its viruses, and less is known about the natural diversity and role of functionally important genes within natural coccolithovirus communities. Here, we investigate the temporal and spatial distribution of coccolithoviruses by the use of molecular fingerprinting techniques PCR, DGGE and genomie sequencing. The natural biodiversity of the virus genes encoding the major capsid protein （MCP） and serine palmitoyltransferase （SPT） were analysed in samples obtained from the Atlantic Meridional Transect （AMT）, the North Sea and the L4 site in the Westem Channel Observatory. We discovered nine new coccolithovirus genotypes across the AMT and L4 site, with the majority of MCP sequences observed at the deep chlorophyll maximum layer of the sampled sites on the transect. We also found four new SPT gene variations in the North Sea and at L4. Their translated fragments and the full protein sequence of SPT from laboratory strains EhV-86 and EhV-99B 1 were modelled and revealed that the theoretical fold differs among strains. Variation identified in the structural distance between the two domains of the SPT protein may have an impact on the catalytic capabilities of its active site. In summary, the combined use of ＇standard＇ markers （i.e. MCP）, in combination with metabolically relevant markers （i.e. SPT） are useful in the study of the phylogeny and functional biodiversity of coccolithoviruses, and can provide an interesting intracellular insight into the evolution of these viruses and their ability to infect and replicate within their algal hosts.

关键词： Coccolithovirus major capsid protein Serine palmitoyltransferase Functional biodiversity

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