Crystal Structure of the Complex mAb 17.2 and the C-Terminal Region of Trypanosoma cruzi P2β Protein: Implications in Cross-Reactivity
Publication Date
November 01, 2011
Journal
PLOS Neglected Tropical Diseases
Authors
Juan Carlos Pizarro, Ginette Boulot, Graham A. Bentley, Karina A. Gómez, et al
Volume
5
Issue
11
Pages
e1375
DOI
http://doi.org/10.1371/journal.pntd.0001375
Publisher URL
http://journals.plos.org/plosntds/article?id=10.1371%2Fjournal.pntd.0001375
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/22069505
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3206007
Europe PMC
http://europepmc.org/abstract/MED/22069505
Web of Science
000298134000012
Scopus
82555169268
Mendeley
http://www.mendeley.com/research/crystal-structure-complex-mab-172-cterminal-region-trypanosoma-cruzi-p2%CE%B2-protein-implications-crossr
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Mendeley | Further Information

{"title"=>"Crystal structure of the complex mAb 17.2 and the C-terminal region of Trypanosoma cruzi P2β protein: Implications in cross-reactivity", "type"=>"journal", "authors"=>[{"first_name"=>"Juan Carlos", "last_name"=>"Pizarro", "scopus_author_id"=>"8404184200"}, {"first_name"=>"Ginette", "last_name"=>"Boulot", "scopus_author_id"=>"6701834356"}, {"first_name"=>"Graham A.", "last_name"=>"Bentley", "scopus_author_id"=>"7103229205"}, {"first_name"=>"Karina A.", "last_name"=>"Gómez", "scopus_author_id"=>"6701823417"}, {"first_name"=>"Johan", "last_name"=>"Hoebeke", "scopus_author_id"=>"56273457300"}, {"first_name"=>"Mireille", "last_name"=>"Hontebeyrie", "scopus_author_id"=>"36726209900"}, {"first_name"=>"Mariano J.", "last_name"=>"Levin", "scopus_author_id"=>"7402571694"}, {"first_name"=>"Cristian R.", "last_name"=>"Smulski", "scopus_author_id"=>"16302807600"}], "year"=>2011, "source"=>"PLoS Neglected Tropical Diseases", "identifiers"=>{"scopus"=>"2-s2.0-82555169268", "pmid"=>"22069505", "issn"=>"19352727", "sgr"=>"82555169268", "doi"=>"10.1371/journal.pntd.0001375", "pui"=>"363024991"}, "id"=>"d7633d87-db00-3062-9256-b5495d538b97", "abstract"=>"Patients with Chronic Chagas' Heart Disease possess high levels of antibodies against the carboxyl-terminal end of the ribosomal P2ß protein of Trypanosoma cruzi (TcP2ß). These antibodies, as well as the murine monoclonal antibody (mAb) 17.2, recognize the last 13 amino acids of TcP2ß (called the R13 epitope: EEEDDDMGFGLFD) and are able to cross-react with, and stimulate, the ß1 adrenergic receptor (ß1-AR). Indeed, the mAb 17.2 was able to specifically detect human β1-AR, stably transfected into HEK cells, by flow cytometry and to induce repolarisation abnormalities and first degree atrioventricular conduction block after passive transfer to naïve mice. To study the structural basis of this cross-reactivity, we determined the crystal structure of the Fab region of the mAb 17.2 alone at 2.31 Å resolution and in complex with the R13 peptide at 1.89 Å resolution. We identified as key contact residues on R13 peptide Glu3, Asp6 and Phe9 as was previously shown by alanine scanning. Additionally, we generated a model of human β1-AR to elucidate the interaction with anti-R13 antibodies. These data provide an understanding of the molecular basis of cross-reactive antibodies induced by chronic infection with Trypanosoma cruzi.", "link"=>"http://www.mendeley.com/research/crystal-structure-complex-mab-172-cterminal-region-trypanosoma-cruzi-p2%CE%B2-protein-implications-crossr", "reader_count"=>8, "reader_count_by_academic_status"=>{"Researcher"=>1, "Student > Ph. D. Student"=>5, "Student > Postgraduate"=>1, "Student > Master"=>1}, "reader_count_by_user_role"=>{"Researcher"=>1, "Student > Ph. D. Student"=>5, "Student > Postgraduate"=>1, "Student > Master"=>1}, "reader_count_by_subject_area"=>{"Agricultural and Biological Sciences"=>6, "Chemistry"=>1, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Chemistry"=>{"Chemistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>6}}, "reader_count_by_country"=>{"Argentina"=>1}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/719191"], "description"=>"<p>Buried surface upon complex formation, with shape complementarities (Sc) <a href=\"http://www.plosntds.org/article/info:doi/10.1371/journal.pntd.0001375#pntd.0001375-Lawrence1\" target=\"_blank\">[50]</a> and number of contacts observed between the mAb 17.2 and the R13 peptide in the crystal structure<sup>1</sup> and the model<sup>2</sup>.</p>", "links"=>[], "tags"=>["complementarities", "contacts", "observed", "mab", "r13", "peptide"], "article_id"=>389539, "categories"=>["Biological Sciences", "Microbiology", "Immunology"], "users"=>["Juan Carlos Pizarro", "Ginette Boulot", "Graham A. Bentley", "Karina A. Gómez", "Johan Hoebeke", "Mireille Hontebeyrie", "Mariano J. Levin", "Cristian R. Smulski"], "doi"=>"https://dx.doi.org/10.1371/journal.pntd.0001375.t004", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Buried_surface_upon_complex_formation_with_shape_complementarities_Sc_50_and_number_of_contacts_observed_between_the_mAb_17_2_and_the_R13_peptide_in_the_crystal_structure_1_and_the_model_2_/389539", "title"=>"Buried surface upon complex formation, with shape complementarities (Sc) [50] and number of contacts observed between the mAb 17.2 and the R13 peptide in the crystal structure<sup>1</sup> and the model<sup>2</sup>.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-20 12:16:10"}
  • {"files"=>["https://ndownloader.figshare.com/files/719065"], "description"=>"<p>MC: Main Chain; SC: Side Chain.</p>", "links"=>[], "tags"=>["contacts", "fab", "r13"], "article_id"=>389422, "categories"=>["Biological Sciences", "Microbiology", "Immunology"], "users"=>["Juan Carlos Pizarro", "Ginette Boulot", "Graham A. Bentley", "Karina A. Gómez", "Johan Hoebeke", "Mireille Hontebeyrie", "Mariano J. Levin", "Cristian R. Smulski"], "doi"=>"https://dx.doi.org/10.1371/journal.pntd.0001375.t002", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Polar_contacts_between_Fab_17_2_and_R13_peptide_/389422", "title"=>"Polar contacts between Fab 17.2 and R13 peptide.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-20 12:15:34"}
  • {"files"=>["https://ndownloader.figshare.com/files/719099"], "description"=>"<p>MC: Main Chain; SC: Side Chain.</p>", "links"=>[], "tags"=>["contacts"], "article_id"=>389455, "categories"=>["Biological Sciences", "Microbiology", "Immunology"], "users"=>["Juan Carlos Pizarro", "Ginette Boulot", "Graham A. Bentley", "Karina A. Gómez", "Johan Hoebeke", "Mireille Hontebeyrie", "Mariano J. Levin", "Cristian R. Smulski"], "doi"=>"https://dx.doi.org/10.1371/journal.pntd.0001375.t003", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Polar_contacts_in_the_model_between_17_2_and_946_1_AR_/389455", "title"=>"Polar contacts in the model between 17.2 and β1-AR.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-20 12:15:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/718726"], "description"=>"<p>A. Representative histogram showing the HEK and HEK-β1 cells labelled with mAb 17.2 followed by a Cy3-conjugated goat anti-mouse IgG. B. Results are expressed as means ± SD (n = 3). Inset: Binding of mAb 17.2 to HEK-β1 cells in the presence of R13 peptide. ** <i>p</i><0.01; *** <i>p</i><0.001. C. Passive transfer of mAb 17.2 to naïve mice. Repolarisation abnormalities (a) and first degree AV conduction block (b) are indicated by arrows. bpm: beats per minute.</p>", "links"=>[], "tags"=>["mab"], "article_id"=>389081, "categories"=>["Biological Sciences", "Microbiology", "Immunology"], "users"=>["Juan Carlos Pizarro", "Ginette Boulot", "Graham A. Bentley", "Karina A. Gómez", "Johan Hoebeke", "Mireille Hontebeyrie", "Mariano J. Levin", "Cristian R. Smulski"], "doi"=>"https://dx.doi.org/10.1371/journal.pntd.0001375.g003", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Functional_activity_of_the_mAb_17_2_/389081", "title"=>"Functional activity of the mAb 17.2.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 12:13:53"}
  • {"files"=>["https://ndownloader.figshare.com/files/719144"], "description"=>"<p>Crystallographic data and refinement statistics.</p>", "links"=>[], "tags"=>["refinement"], "article_id"=>389499, "categories"=>["Biological Sciences", "Microbiology", "Immunology"], "users"=>["Juan Carlos Pizarro", "Ginette Boulot", "Graham A. Bentley", "Karina A. Gómez", "Johan Hoebeke", "Mireille Hontebeyrie", "Mariano J. Levin", "Cristian R. Smulski"], "doi"=>"https://dx.doi.org/10.1371/journal.pntd.0001375.t001", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Crystallographic_data_and_refinement_statistics_/389499", "title"=>"Crystallographic data and refinement statistics.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-20 12:15:59"}
  • {"files"=>["https://ndownloader.figshare.com/files/718948"], "description"=>"<p>A. Superposition of the second extracellular loop (2ECL) of the human β1-AR model (violet) and the region 2–5 of the epitope (light green). B. Complex of the Fab 17.2 (light green) with the human β1-AR (violet) inserted in a membrane model (grey). C. Zoom of the paratope region of 17.2 interacting with the second extracellular loop. The main contact points are illustrated as dotted yellow lines. Heavy chain CDRs are coloured in red and light chain CDRs in blue.</p>", "links"=>[], "tags"=>["fab"], "article_id"=>389308, "categories"=>["Biological Sciences", "Microbiology", "Immunology"], "users"=>["Juan Carlos Pizarro", "Ginette Boulot", "Graham A. Bentley", "Karina A. Gómez", "Johan Hoebeke", "Mireille Hontebeyrie", "Mariano J. Levin", "Cristian R. Smulski"], "doi"=>"https://dx.doi.org/10.1371/journal.pntd.0001375.g004", "stats"=>{"downloads"=>1, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Model_of_the_interaction_of_Fab_17_2_with_the_human_946_1_AR_/389308", "title"=>"Model of the interaction of Fab 17.2 with the human β1-AR.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 12:15:00"}
  • {"files"=>["https://ndownloader.figshare.com/files/718539"], "description"=>"<p>A. Apo Fab 17.2 structure (molecule 1). Heavy chain CDRs are coloured in red and light chain CDRs in blue. B. Superposition of molecules 1, VH-VL region of the two crystals asymmetric units. C. Superposition of molecules 2, VH-VL region of the two crystals asymmetric units. Apo Fab 17.2 (grey), Fab 17.2-R13 molecule 1 (green) and molecule 2 (magenta).</p>", "links"=>[], "tags"=>["fab"], "article_id"=>388893, "categories"=>["Biological Sciences", "Microbiology", "Immunology"], "users"=>["Juan Carlos Pizarro", "Ginette Boulot", "Graham A. Bentley", "Karina A. Gómez", "Johan Hoebeke", "Mireille Hontebeyrie", "Mariano J. Levin", "Cristian R. Smulski"], "doi"=>"https://dx.doi.org/10.1371/journal.pntd.0001375.g001", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structure_of_the_Fab_17_2_/388893", "title"=>"Structure of the Fab 17.2.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 12:12:55"}
  • {"files"=>["https://ndownloader.figshare.com/files/718630"], "description"=>"<p>A. Superposition of the apo Fab 17.2 and R13 complex structures (grey and green respectively). VH and VL contact residues are indicated. B. Main water molecules present on the antigen binding site of Fab 17.2 apo. C. Superposition of water molecules present in the apo Fab 17.2 that are replaced by the peptide in the Fab 17.2 R13 complex. D. Superposition of R13 peptides from molecules 1 (green) and 2 (magenta). E. Structure of the Fab 17.2-R13 complex (molecule 1). All hydrogen bonds between mAb 17.2 and peptide R13 are illustrated as dotted yellow lines. The π-stacking interaction between VL Tyr101 and the epitope Phe9 is also indicated. Heavy chain CDRs are coloured in red and light chain CDRs in blue the peptide is coloured in light green.</p>", "links"=>[], "tags"=>["r13"], "article_id"=>388991, "categories"=>["Biological Sciences", "Microbiology", "Immunology"], "users"=>["Juan Carlos Pizarro", "Ginette Boulot", "Graham A. Bentley", "Karina A. Gómez", "Johan Hoebeke", "Mireille Hontebeyrie", "Mariano J. Levin", "Cristian R. Smulski"], "doi"=>"https://dx.doi.org/10.1371/journal.pntd.0001375.g002", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structure_of_the_Fab17_2_8211_R13_complex_/388991", "title"=>"Structure of the Fab17.2 – R13 complex.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 12:13:25"}

PMC Usage Stats | Further Information

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Relative Metric

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