The Solution Structure of the Adhesion Protein Bd37 from Babesia divergens Reveals Structural Homology with Eukaryotic Proteins Involved in Membrane Trafficking
Babesia divergens is the Apicomplexa agent of the bovine babesiosis in Europe: this infection leads to growth and lactation decrease, so that economical losses due to this parasite are sufficient to require the development of a vaccine. The major surface antigen of B. divergens has been described as...
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| Veröffentlicht in: | Journal of molecular biology 2008-01, Vol.375 (2), p.409-424 |
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| creator | Delbecq, Stéphane Auguin, Daniel Yang, Yin-Shan Löhr, Frank Arold, Stefan Schetters, Theo Précigout, Eric Gorenflot, André Roumestand, Christian |
| description | Babesia divergens is the Apicomplexa agent of the bovine babesiosis in Europe: this infection leads to growth and lactation decrease, so that economical losses due to this parasite are sufficient to require the development of a vaccine. The major surface antigen of B. divergens has been described as a 37 kDa protein glycosyl phosphatidyl inositol (GPI)-anchored at the surface of the merozoite. The immuno-prophylactic potential of Bd37 has been demonstrated, and we present here the high-resolution solution structure of the 27 kDa structured core of Bd37 (Δ-Bd37) using NMR spectroscopy. A model for the whole protein has been obtained using additional small angle X-ray scattering (SAXS) data. The knowledge of the 3D structure of Bd37 allowed the precise epitope mapping of antibodies on its surface. Interestingly, the geometry of Δ-Bd37 reveals an intriguing similarity with the exocyst subunit Exo84p C-terminal region, an eukaryotic protein that has a direct implication in vesicle trafficking. This strongly suggests that Apicomplexa have developed in parallel molecular machines similar in structure and function to the ones used for endo- and exocytosis in eukaryotic cells. |
| doi_str_mv | 10.1016/j.jmb.2007.08.019 |
| format | Article |
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The major surface antigen of B. divergens has been described as a 37 kDa protein glycosyl phosphatidyl inositol (GPI)-anchored at the surface of the merozoite. The immuno-prophylactic potential of Bd37 has been demonstrated, and we present here the high-resolution solution structure of the 27 kDa structured core of Bd37 (Δ-Bd37) using NMR spectroscopy. A model for the whole protein has been obtained using additional small angle X-ray scattering (SAXS) data. The knowledge of the 3D structure of Bd37 allowed the precise epitope mapping of antibodies on its surface. Interestingly, the geometry of Δ-Bd37 reveals an intriguing similarity with the exocyst subunit Exo84p C-terminal region, an eukaryotic protein that has a direct implication in vesicle trafficking. This strongly suggests that Apicomplexa have developed in parallel molecular machines similar in structure and function to the ones used for endo- and exocytosis in eukaryotic cells.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/j.jmb.2007.08.019</identifier><identifier>PMID: 18035372</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Alleles ; Amino Acid Sequence ; Animals ; Antigens, Protozoan ; Antigens, Protozoan - chemistry ; Antigens, Protozoan - genetics ; Antigens, Protozoan - metabolism ; Apicomplexa ; Babesia ; Babesia - chemistry ; Babesia divergens ; Biochemistry, Molecular Biology ; Cell Membrane ; Cell Membrane - physiology ; Circular Dichroism ; Disulfides ; Disulfides - chemistry ; Epitopes ; Erythrocytes ; Erythrocytes - metabolism ; Eukaryotic Cells ; Eukaryotic Cells - chemistry ; Glutathione Transferase ; Glutathione Transferase - metabolism ; GPI-anchored protein ; Life Sciences ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Transport ; Protozoan Proteins ; Protozoan Proteins - analysis ; Protozoan Proteins - chemistry ; Protozoan Proteins - genetics ; Protozoan Proteins - metabolism ; Recombinant Proteins ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; recombinant vaccine ; Scattering, Small Angle ; Sequence Homology, Amino Acid ; Structure-Activity Relationship ; surface antigen ; vesicle traffiking ; X-Ray Diffraction</subject><ispartof>Journal of molecular biology, 2008-01, Vol.375 (2), p.409-424</ispartof><rights>2007 Elsevier Ltd</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c416t-bf92c37775708cd5ec625c841a71f5353dfacdac7c8d6fbbbcaae42fc05cf5e23</citedby><cites>FETCH-LOGICAL-c416t-bf92c37775708cd5ec625c841a71f5353dfacdac7c8d6fbbbcaae42fc05cf5e23</cites><orcidid>0000-0002-2813-1219 ; 0000-0002-4082-3293 ; 0000-0003-4713-9096</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jmb.2007.08.019$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,778,782,883,3539,27907,27908,45978</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18035372$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00202881$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Delbecq, Stéphane</creatorcontrib><creatorcontrib>Auguin, Daniel</creatorcontrib><creatorcontrib>Yang, Yin-Shan</creatorcontrib><creatorcontrib>Löhr, Frank</creatorcontrib><creatorcontrib>Arold, Stefan</creatorcontrib><creatorcontrib>Schetters, Theo</creatorcontrib><creatorcontrib>Précigout, Eric</creatorcontrib><creatorcontrib>Gorenflot, André</creatorcontrib><creatorcontrib>Roumestand, Christian</creatorcontrib><title>The Solution Structure of the Adhesion Protein Bd37 from Babesia divergens Reveals Structural Homology with Eukaryotic Proteins Involved in Membrane Trafficking</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>Babesia divergens is the Apicomplexa agent of the bovine babesiosis in Europe: this infection leads to growth and lactation decrease, so that economical losses due to this parasite are sufficient to require the development of a vaccine. The major surface antigen of B. divergens has been described as a 37 kDa protein glycosyl phosphatidyl inositol (GPI)-anchored at the surface of the merozoite. The immuno-prophylactic potential of Bd37 has been demonstrated, and we present here the high-resolution solution structure of the 27 kDa structured core of Bd37 (Δ-Bd37) using NMR spectroscopy. A model for the whole protein has been obtained using additional small angle X-ray scattering (SAXS) data. The knowledge of the 3D structure of Bd37 allowed the precise epitope mapping of antibodies on its surface. Interestingly, the geometry of Δ-Bd37 reveals an intriguing similarity with the exocyst subunit Exo84p C-terminal region, an eukaryotic protein that has a direct implication in vesicle trafficking. This strongly suggests that Apicomplexa have developed in parallel molecular machines similar in structure and function to the ones used for endo- and exocytosis in eukaryotic cells.</description><subject>Alleles</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antigens, Protozoan</subject><subject>Antigens, Protozoan - chemistry</subject><subject>Antigens, Protozoan - genetics</subject><subject>Antigens, Protozoan - metabolism</subject><subject>Apicomplexa</subject><subject>Babesia</subject><subject>Babesia - chemistry</subject><subject>Babesia divergens</subject><subject>Biochemistry, Molecular Biology</subject><subject>Cell Membrane</subject><subject>Cell Membrane - physiology</subject><subject>Circular Dichroism</subject><subject>Disulfides</subject><subject>Disulfides - chemistry</subject><subject>Epitopes</subject><subject>Erythrocytes</subject><subject>Erythrocytes - metabolism</subject><subject>Eukaryotic Cells</subject><subject>Eukaryotic Cells - chemistry</subject><subject>Glutathione Transferase</subject><subject>Glutathione Transferase - metabolism</subject><subject>GPI-anchored protein</subject><subject>Life Sciences</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Transport</subject><subject>Protozoan Proteins</subject><subject>Protozoan Proteins - analysis</subject><subject>Protozoan Proteins - chemistry</subject><subject>Protozoan Proteins - genetics</subject><subject>Protozoan Proteins - metabolism</subject><subject>Recombinant Proteins</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>recombinant vaccine</subject><subject>Scattering, Small Angle</subject><subject>Sequence Homology, Amino Acid</subject><subject>Structure-Activity Relationship</subject><subject>surface antigen</subject><subject>vesicle traffiking</subject><subject>X-Ray Diffraction</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFuEzEQhlcIRNPCA3BBPiFxSBjb2bUjTmlVSKUgEA1ny2uPE6e762LvLurb9FFxlFBucLLk-ebTzPxF8YbCjAKtPuxn-7aeMQAxAzkDunhWTCjIxVRWXD4vJgCMTZnk1VlxntIeAEo-ly-LMyqBl1ywSfG42SG5Dc3Q-9CR2z4Oph8ikuBInytLu8N0qHyLoUffkUvLBXExtORS17mkifUjxi12iXzHEXWTniy6IavQhiZsH8gv3-_I9XCn40PovfnjS-SmG0MzoiVZ_gXbOuoOySZq57y58932VfHCZSm-Pr0XxY9P15ur1XT99fPN1XI9NXNa9dPaLZjhQohSgDS2RFOx0sg51YK6Mi9rnTZWG2GkrVxd10ZrnDNnoDSuRMYvivdH70436j76Nk-qgvZqtVyrw18-JjAp6Ugz--7I3sfwc8DUq9Yng02TZw9DUgJgUfHy_yCjMBfAeQbpETQxpBTRPY1AQR2yVnuVs1aHrBVIlbPOPW9P8qFu0f7tOIWbgY9HAPPdRo9RJeOxM2h9RNMrG_w_9L8BpvW8_A</recordid><startdate>20080111</startdate><enddate>20080111</enddate><creator>Delbecq, Stéphane</creator><creator>Auguin, Daniel</creator><creator>Yang, Yin-Shan</creator><creator>Löhr, Frank</creator><creator>Arold, Stefan</creator><creator>Schetters, Theo</creator><creator>Précigout, Eric</creator><creator>Gorenflot, André</creator><creator>Roumestand, Christian</creator><general>Elsevier Ltd</general><general>Elsevier</general><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>7T5</scope><scope>C1K</scope><scope>H94</scope><scope>M7N</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-2813-1219</orcidid><orcidid>https://orcid.org/0000-0002-4082-3293</orcidid><orcidid>https://orcid.org/0000-0003-4713-9096</orcidid></search><sort><creationdate>20080111</creationdate><title>The Solution Structure of the Adhesion Protein Bd37 from Babesia divergens Reveals Structural Homology with Eukaryotic Proteins Involved in Membrane Trafficking</title><author>Delbecq, Stéphane ; 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The major surface antigen of B. divergens has been described as a 37 kDa protein glycosyl phosphatidyl inositol (GPI)-anchored at the surface of the merozoite. The immuno-prophylactic potential of Bd37 has been demonstrated, and we present here the high-resolution solution structure of the 27 kDa structured core of Bd37 (Δ-Bd37) using NMR spectroscopy. A model for the whole protein has been obtained using additional small angle X-ray scattering (SAXS) data. The knowledge of the 3D structure of Bd37 allowed the precise epitope mapping of antibodies on its surface. Interestingly, the geometry of Δ-Bd37 reveals an intriguing similarity with the exocyst subunit Exo84p C-terminal region, an eukaryotic protein that has a direct implication in vesicle trafficking. This strongly suggests that Apicomplexa have developed in parallel molecular machines similar in structure and function to the ones used for endo- and exocytosis in eukaryotic cells.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>18035372</pmid><doi>10.1016/j.jmb.2007.08.019</doi><tpages>16</tpages><orcidid>https://orcid.org/0000-0002-2813-1219</orcidid><orcidid>https://orcid.org/0000-0002-4082-3293</orcidid><orcidid>https://orcid.org/0000-0003-4713-9096</orcidid></addata></record> |
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| subjects | Alleles Amino Acid Sequence Animals Antigens, Protozoan Antigens, Protozoan - chemistry Antigens, Protozoan - genetics Antigens, Protozoan - metabolism Apicomplexa Babesia Babesia - chemistry Babesia divergens Biochemistry, Molecular Biology Cell Membrane Cell Membrane - physiology Circular Dichroism Disulfides Disulfides - chemistry Epitopes Erythrocytes Erythrocytes - metabolism Eukaryotic Cells Eukaryotic Cells - chemistry Glutathione Transferase Glutathione Transferase - metabolism GPI-anchored protein Life Sciences Models, Molecular Molecular Sequence Data Mutation Nuclear Magnetic Resonance, Biomolecular Protein Binding Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Protein Transport Protozoan Proteins Protozoan Proteins - analysis Protozoan Proteins - chemistry Protozoan Proteins - genetics Protozoan Proteins - metabolism Recombinant Proteins Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism recombinant vaccine Scattering, Small Angle Sequence Homology, Amino Acid Structure-Activity Relationship surface antigen vesicle traffiking X-Ray Diffraction |
| title | The Solution Structure of the Adhesion Protein Bd37 from Babesia divergens Reveals Structural Homology with Eukaryotic Proteins Involved in Membrane Trafficking |
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