Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein
Prion disorders are infectious diseases that are characterized by the conversion of the cellular prion protein PrPC into the pathogenic isoform PrPSc. Specific antibodies that interact with the cellular prion protein have been shown to inhibit this transition. Recombinant VHHs (variable domain of dr...
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| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2010-12, Vol.66 (12), p.1644-1646 |
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| container_title | Acta crystallographica. Section F, Structural biology and crystallization communications |
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| creator | Abskharon, Romany N. N. Soror, Sameh H. Pardon, Els El Hassan, Hassan Legname, Giuseppe Steyaert, Jan Wohlkonig, Alexandre |
| description | Prion disorders are infectious diseases that are characterized by the conversion of the cellular prion protein PrPC into the pathogenic isoform PrPSc. Specific antibodies that interact with the cellular prion protein have been shown to inhibit this transition. Recombinant VHHs (variable domain of dromedary heavy‐chain antibodies) or nanobodies are single‐domain antibodies, making them the smallest antigen‐binding fragments. A specific nanobody (Nb_PrP_01) was raised against mouse PrPC. A crystallization condition for this recombinant nanobody was identified using high‐throughput screening. The crystals were optimized using streak‐seeding and the hanging‐drop method. The crystals belonged to the orthorhombic space group P212121, with unit‐cell parameters a = 30.04, b = 37.15, c = 83.00 Å, and diffracted to 1.23 Å resolution using synchrotron radiation. The crystal structure of this specific nanobody against PrPC together with the known PrPC structure may help in understanding the PrPC/PrPSc transition mechanism. |
| doi_str_mv | 10.1107/S1744309110042168 |
| format | Article |
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N. ; Soror, Sameh H. ; Pardon, Els ; El Hassan, Hassan ; Legname, Giuseppe ; Steyaert, Jan ; Wohlkonig, Alexandre</creator><creatorcontrib>Abskharon, Romany N. N. ; Soror, Sameh H. ; Pardon, Els ; El Hassan, Hassan ; Legname, Giuseppe ; Steyaert, Jan ; Wohlkonig, Alexandre</creatorcontrib><description>Prion disorders are infectious diseases that are characterized by the conversion of the cellular prion protein PrPC into the pathogenic isoform PrPSc. Specific antibodies that interact with the cellular prion protein have been shown to inhibit this transition. Recombinant VHHs (variable domain of dromedary heavy‐chain antibodies) or nanobodies are single‐domain antibodies, making them the smallest antigen‐binding fragments. A specific nanobody (Nb_PrP_01) was raised against mouse PrPC. A crystallization condition for this recombinant nanobody was identified using high‐throughput screening. The crystals were optimized using streak‐seeding and the hanging‐drop method. The crystals belonged to the orthorhombic space group P212121, with unit‐cell parameters a = 30.04, b = 37.15, c = 83.00 Å, and diffracted to 1.23 Å resolution using synchrotron radiation. The crystal structure of this specific nanobody against PrPC together with the known PrPC structure may help in understanding the PrPC/PrPSc transition mechanism.</description><identifier>ISSN: 1744-3091</identifier><identifier>EISSN: 1744-3091</identifier><identifier>EISSN: 2053-230X</identifier><identifier>DOI: 10.1107/S1744309110042168</identifier><identifier>PMID: 21139215</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>Animals ; Antibodies - chemistry ; Camelidae ; Chromatography, Gel ; Crystallization ; Crystallization Communications ; Crystallography, X-Ray ; Mice ; nanobodies ; Prion Proteins ; prions ; Prions - chemistry ; Prions - immunology ; Protein Structure, Tertiary ; PrPC ; PrPSc ; Synchrotrons ; X-Ray Diffraction</subject><ispartof>Acta crystallographica. 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The crystal structure of this specific nanobody against PrPC together with the known PrPC structure may help in understanding the PrPC/PrPSc transition mechanism.</description><subject>Animals</subject><subject>Antibodies - chemistry</subject><subject>Camelidae</subject><subject>Chromatography, Gel</subject><subject>Crystallization</subject><subject>Crystallization Communications</subject><subject>Crystallography, X-Ray</subject><subject>Mice</subject><subject>nanobodies</subject><subject>Prion Proteins</subject><subject>prions</subject><subject>Prions - chemistry</subject><subject>Prions - immunology</subject><subject>Protein Structure, Tertiary</subject><subject>PrPC</subject><subject>PrPSc</subject><subject>Synchrotrons</subject><subject>X-Ray Diffraction</subject><issn>1744-3091</issn><issn>1744-3091</issn><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1vEzEQhlcIREvgB3BBljhwWvCsvy9IbUQbpPAhWr5OluO1i8vuOtiblvDrcZQQFTj0YnvGz_t6xlNVjwE_B8DixRkISglWJcC0AS7vVIebVL3J3b1xPqge5HyJMSGKy_vVQQNAVAPssIrTtM6j6brwy4whDsgMLVom14U-DCat0Zc6mTVqg_fJ2B1hunUOGUWPDMpLZ4MPFn2azVAbexMKcVHWPKI-rrIrbhvVMsXRheFhdc-bLrtHu31SfTx5dT6d1fN3p6-nR_PaMsp5TZigxBMhoZHeWOlp660V2FPlvVm0VjLZgloIqqRzmDHsOba0pUItoBGCTKqXW9_latG71rphTKbTpZa-dKWjCfrvmyF80xfxSjdKSVIen1TPdgYp_li5POo-ZOu6zgyutKUlB0YIJ3A7CVwooEwW8uk_5GVcpfKdWYMgwJloJCkUbCmbYs7J-X3VgPVm7vq_uRfNk5vt7hV_Bl0AtQWuQ-fWtzvqo68nzWzKAHjR1lttyKP7udea9F1zQQTTn9-e6g9vzuZzfnyu35PfJRPJGg</recordid><startdate>201012</startdate><enddate>201012</enddate><creator>Abskharon, Romany N. N.</creator><creator>Soror, Sameh H.</creator><creator>Pardon, Els</creator><creator>El Hassan, Hassan</creator><creator>Legname, Giuseppe</creator><creator>Steyaert, Jan</creator><creator>Wohlkonig, Alexandre</creator><general>International Union of Crystallography</general><general>Wiley Subscription Services, Inc</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>7QL</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201012</creationdate><title>Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein</title><author>Abskharon, Romany N. 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N.</creatorcontrib><creatorcontrib>Soror, Sameh H.</creatorcontrib><creatorcontrib>Pardon, Els</creatorcontrib><creatorcontrib>El Hassan, Hassan</creatorcontrib><creatorcontrib>Legname, Giuseppe</creatorcontrib><creatorcontrib>Steyaert, Jan</creatorcontrib><creatorcontrib>Wohlkonig, Alexandre</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Abskharon, Romany N. N.</au><au>Soror, Sameh H.</au><au>Pardon, Els</au><au>El Hassan, Hassan</au><au>Legname, Giuseppe</au><au>Steyaert, Jan</au><au>Wohlkonig, Alexandre</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein</atitle><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle><addtitle>Acta Cryst. F</addtitle><date>2010-12</date><risdate>2010</risdate><volume>66</volume><issue>12</issue><spage>1644</spage><epage>1646</epage><pages>1644-1646</pages><issn>1744-3091</issn><eissn>1744-3091</eissn><eissn>2053-230X</eissn><abstract>Prion disorders are infectious diseases that are characterized by the conversion of the cellular prion protein PrPC into the pathogenic isoform PrPSc. Specific antibodies that interact with the cellular prion protein have been shown to inhibit this transition. Recombinant VHHs (variable domain of dromedary heavy‐chain antibodies) or nanobodies are single‐domain antibodies, making them the smallest antigen‐binding fragments. A specific nanobody (Nb_PrP_01) was raised against mouse PrPC. A crystallization condition for this recombinant nanobody was identified using high‐throughput screening. The crystals were optimized using streak‐seeding and the hanging‐drop method. 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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Animals Antibodies - chemistry Camelidae Chromatography, Gel Crystallization Crystallization Communications Crystallography, X-Ray Mice nanobodies Prion Proteins prions Prions - chemistry Prions - immunology Protein Structure, Tertiary PrPC PrPSc Synchrotrons X-Ray Diffraction |
| title | Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein |
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