Plasticity of the β-Trefoil Protein Fold in the Recognition and Control of Invertebrate Predators and Parasites by a Fungal Defence System
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{"title"=>"Plasticity of the β-trefoil protein fold in the recognition and control of invertebrate predators and parasites by a fungal defence system", "type"=>"journal", "authors"=>[{"first_name"=>"Mario", "last_name"=>"Schubert", "scopus_author_id"=>"35564909300"}, {"first_name"=>"Silvia", "last_name"=>"Bleuler-Martinez", "scopus_author_id"=>"29067485300"}, {"first_name"=>"Alex", "last_name"=>"Butschi", "scopus_author_id"=>"35502924500"}, {"first_name"=>"Martin A.", "last_name"=>"Wälti", "scopus_author_id"=>"13204927300"}, {"first_name"=>"Pascal", "last_name"=>"Egloff", "scopus_author_id"=>"55307788700"}, {"first_name"=>"Katrin", "last_name"=>"Stutz", "scopus_author_id"=>"38762252800"}, {"first_name"=>"Shi", "last_name"=>"Yan", "scopus_author_id"=>"54382556100"}, {"first_name"=>"Iain B.H.", "last_name"=>"Wilson", "scopus_author_id"=>"55367238900"}, {"first_name"=>"Michael O.", "last_name"=>"Hengartner", "scopus_author_id"=>"7006384526"}, {"first_name"=>"Markus", "last_name"=>"Aebi", "scopus_author_id"=>"7102318072"}, {"first_name"=>"Frédéric H.T.", "last_name"=>"Allain", "scopus_author_id"=>"6603685405"}, {"first_name"=>"Markus", "last_name"=>"Künzler", "scopus_author_id"=>"6701917716"}], "year"=>2012, "source"=>"PLoS Pathogens", "identifiers"=>{"sgr"=>"84863676996", "doi"=>"10.1371/journal.ppat.1002706", "pui"=>"365220890", "pmid"=>"22615566", "scopus"=>"2-s2.0-84863676996", "issn"=>"15537366", "isbn"=>"1553-7374 (Electronic)\\r1553-7366 (Linking)"}, "id"=>"b6b98a3e-dd38-3ef3-ab39-5e38be6633fe", "abstract"=>"Discrimination between self and non-self is a prerequisite for any defence mechanism; in innate defence, this discrimination is often mediated by lectins recognizing non-self carbohydrate structures and so relies on an arsenal of host lectins with different specificities towards target organism carbohydrate structures. Recently, cytoplasmic lectins isolated from fungal fruiting bodies have been shown to play a role in the defence of multicellular fungi against predators and parasites. Here, we present a novel fruiting body lectin, CCL2, from the ink cap mushroom Coprinopsis cinerea. We demonstrate the toxicity of the lectin towards Caenorhabditis elegans and Drosophila melanogaster and present its NMR solution structure in complex with the trisaccharide, GlcNAcβ1,4[Fucα1,3]GlcNAc, to which it binds with high specificity and affinity in vitro. The structure reveals that the monomeric CCL2 adopts a β-trefoil fold and recognizes the trisaccharide by a single, topologically novel carbohydrate-binding site. Site-directed mutagenesis of CCL2 and identification of C. elegans mutants resistant to this lectin show that its nematotoxicity is mediated by binding to α1,3-fucosylated N-glycan core structures of nematode glycoproteins; feeding with fluorescently labeled CCL2 demonstrates that these target glycoproteins localize to the C. elegans intestine. Since the identified glycoepitope is characteristic for invertebrates but absent from fungi, our data show that the defence function of fruiting body lectins is based on the specific recognition of non-self carbohydrate structures. The trisaccharide specifically recognized by CCL2 is a key carbohydrate determinant of pollen and insect venom allergens implying this particular glycoepitope is targeted by both fungal defence and mammalian immune systems. In summary, our results demonstrate how the plasticity of a common protein fold can contribute to the recognition and control of antagonists by an innate defence mechanism, whereby the monovalency of the lectin for its ligand implies a novel mechanism of lectin-mediated toxicity.", "link"=>"http://www.mendeley.com/research/plasticity-%CE%B2trefoil-protein-fold-recognition-control-invertebrate-predators-parasites-fungal-defence", "reader_count"=>44, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>3, "Student > Doctoral Student"=>4, "Researcher"=>13, "Student > Ph. D. Student"=>12, "Student > Master"=>5, "Other"=>1, "Professor"=>4}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>3, "Student > Doctoral Student"=>4, "Researcher"=>13, "Student > Ph. D. Student"=>12, "Student > Master"=>5, "Other"=>1, "Professor"=>4}, "reader_count_by_subject_area"=>{"Unspecified"=>3, "Biochemistry, Genetics and Molecular Biology"=>10, "Agricultural and Biological Sciences"=>23, "Medicine and Dentistry"=>2, "Chemistry"=>5, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Chemistry"=>{"Chemistry"=>5}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>23}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>10}, "Unspecified"=>{"Unspecified"=>3}}, "reader_count_by_country"=>{"Japan"=>1}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/329185", "https://ndownloader.figshare.com/files/329231", "https://ndownloader.figshare.com/files/329302", "https://ndownloader.figshare.com/files/329358", "https://ndownloader.figshare.com/files/329447", "https://ndownloader.figshare.com/files/329553", "https://ndownloader.figshare.com/files/329606", "https://ndownloader.figshare.com/files/329643", "https://ndownloader.figshare.com/files/329677", "https://ndownloader.figshare.com/files/329702", "https://ndownloader.figshare.com/files/329728", "https://ndownloader.figshare.com/files/329759", "https://ndownloader.figshare.com/files/329849", "https://ndownloader.figshare.com/files/329947", "https://ndownloader.figshare.com/files/329990", "https://ndownloader.figshare.com/files/330159", "https://ndownloader.figshare.com/files/330321", "https://ndownloader.figshare.com/files/330363", "https://ndownloader.figshare.com/files/330407", "https://ndownloader.figshare.com/files/330466", "https://ndownloader.figshare.com/files/330528", "https://ndownloader.figshare.com/files/330593"], "description"=>"<div><p>Discrimination between self and non-self is a prerequisite for any defence mechanism; in innate defence, this discrimination is often mediated by lectins recognizing non-self carbohydrate structures and so relies on an arsenal of host lectins with different specificities towards target organism carbohydrate structures. Recently, cytoplasmic lectins isolated from fungal fruiting bodies have been shown to play a role in the defence of multicellular fungi against predators and parasites. Here, we present a novel fruiting body lectin, CCL2, from the ink cap mushroom <em>Coprinopsis cinerea</em>. We demonstrate the toxicity of the lectin towards <em>Caenorhabditis elegans</em> and <em>Drosophila melanogaster</em> and present its NMR solution structure in complex with the trisaccharide, GlcNAcβ1,4[Fucα1,3]GlcNAc, to which it binds with high specificity and affinity <em>in vitro</em>. The structure reveals that the monomeric CCL2 adopts a β-trefoil fold and recognizes the trisaccharide by a single, topologically novel carbohydrate-binding site. Site-directed mutagenesis of CCL2 and identification of <em>C. elegans</em> mutants resistant to this lectin show that its nematotoxicity is mediated by binding to α1,3-fucosylated N-glycan core structures of nematode glycoproteins; feeding with fluorescently labeled CCL2 demonstrates that these target glycoproteins localize to the <em>C. elegans</em> intestine. Since the identified glycoepitope is characteristic for invertebrates but absent from fungi, our data show that the defence function of fruiting body lectins is based on the specific recognition of non-self carbohydrate structures. The trisaccharide specifically recognized by CCL2 is a key carbohydrate determinant of pollen and insect venom allergens implying this particular glycoepitope is targeted by both fungal defence and mammalian immune systems. In summary, our results demonstrate how the plasticity of a common protein fold can contribute to the recognition and control of antagonists by an innate defence mechanism, whereby the monovalency of the lectin for its ligand implies a novel mechanism of lectin-mediated toxicity.</p> </div>", "links"=>[], "tags"=>["plasticity", "invertebrate", "predators", "parasites", "fungal", "defence"], "article_id"=>125005, "categories"=>["Biological Sciences", "Biochemistry", "Microbiology", "Biophysics"], "users"=>["Mario Schubert", "Silvia Bleuler-Martinez", "Alex Butschi", "Martin A. Wälti", "Pascal Egloff", "Katrin Stutz", "Shi Yan", "Iain B. H. Wilson", "Michael O. Hengartner", "Markus Aebi", "Frédéric H.-T. Allain", "Markus Künzler"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1002706.s001", "https://dx.doi.org/10.1371/journal.ppat.1002706.s002", "https://dx.doi.org/10.1371/journal.ppat.1002706.s003", "https://dx.doi.org/10.1371/journal.ppat.1002706.s004", "https://dx.doi.org/10.1371/journal.ppat.1002706.s005", "https://dx.doi.org/10.1371/journal.ppat.1002706.s006", "https://dx.doi.org/10.1371/journal.ppat.1002706.s007", "https://dx.doi.org/10.1371/journal.ppat.1002706.s008", "https://dx.doi.org/10.1371/journal.ppat.1002706.s009", "https://dx.doi.org/10.1371/journal.ppat.1002706.s010", "https://dx.doi.org/10.1371/journal.ppat.1002706.s011", "https://dx.doi.org/10.1371/journal.ppat.1002706.s012", "https://dx.doi.org/10.1371/journal.ppat.1002706.s013", "https://dx.doi.org/10.1371/journal.ppat.1002706.s014", "https://dx.doi.org/10.1371/journal.ppat.1002706.s015", "https://dx.doi.org/10.1371/journal.ppat.1002706.s016", "https://dx.doi.org/10.1371/journal.ppat.1002706.s017", "https://dx.doi.org/10.1371/journal.ppat.1002706.s018", "https://dx.doi.org/10.1371/journal.ppat.1002706.s019", "https://dx.doi.org/10.1371/journal.ppat.1002706.s020", "https://dx.doi.org/10.1371/journal.ppat.1002706.s021", "https://dx.doi.org/10.1371/journal.ppat.1002706.s022"], "stats"=>{"downloads"=>30, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Plasticity_of_the_Trefoil_Protein_Fold_in_the_Recognition_and_Control_of_Invertebrate_Predators_and_Parasites_by_a_Fungal_Defence_System/125005", "title"=>"Plasticity of the β-Trefoil Protein Fold in the Recognition and Control of Invertebrate Predators and Parasites by a Fungal Defence System", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2012-05-17 01:23:25"}
  • {"files"=>["https://ndownloader.figshare.com/files/637928"], "description"=>"a<p>nd: not determined.</p>b<p>The increased affinity of N91A might be an artifact caused by interaction of the artificial carbohydrate spacer O-(CH<sub>2</sub>)<sub>5</sub>-COOH with residue 91. Whereas the spacer might sterically clash with N91, Ala in this position could form favorable van-der-Waals interactions. In the case of natural N-glycans, where the reducing GlcNAc is linked to Asn of a glycoprotein projecting away from CCL2 (upper right corner of <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1002706#ppat-1002706-g005\" target=\"_blank\">Figure 5D</a>), Asn is likely to be favored at this position of CCL2 due to the potential formation of H-bonds.</p>", "links"=>[], "tags"=>["ccl2", "wild-type", "carbohydrates", "variants", "spacer", "isothermal", "titration", "calorimetry", "nmr", "spectroscopy"], "article_id"=>308396, "categories"=>["Biological Sciences", "Biochemistry", "Microbiology", "Biophysics"], "users"=>["Mario Schubert", "Silvia Bleuler-Martinez", "Alex Butschi", "Martin A. Wälti", "Pascal Egloff", "Katrin Stutz", "Shi Yan", "Iain B. H. Wilson", "Michael O. Hengartner", "Markus Aebi", "Frédéric H.-T. Allain", "Markus Künzler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002706.t001", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Binding_of_CCL2_wild_type_to_different_carbohydrates_and_CCL2_variants_to_GlcNAc_1_4_Fuc_1_3_GlcNAc_1_sp_sp_spacer_O_CH_2_5_COOH_measured_with_isothermal_titration_calorimetry_and_NMR_spectroscopy_at_299K_/308396", "title"=>"Binding of CCL2 wild-type to different carbohydrates and CCL2 variants to GlcNAcβ1,4[Fucα1,3]GlcNAcβ1-sp (sp: spacer O-[CH<sub>2</sub>]<sub>5</sub>COOH) measured with isothermal titration calorimetry and NMR spectroscopy at 299K.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2012-05-17 02:19:56"}
  • {"files"=>["https://ndownloader.figshare.com/files/637119"], "description"=>"<p>The side (A) and top (B) view of the most representative structure out of 20 structures is shown. The three pseudo symmetric sections of the β-trefoil fold corresponding to residues S9–N60, S61–S100 and G101–V142 are colored green, yellow and orange, respectively. Characteristic regions are labeled according to Renko et al. for better orientation <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1002706#ppat.1002706-Renko1\" target=\"_blank\">[26]</a>. (C) Chemical shift deviations mapped on the structure of CCL2 in the same orientation as in A. Chemical shifts of residues in red experience a combined NH chemical shift deviation >0.4 ppm, for residues in pink >0.15 ppm. (D) Secondary structure and subdomain borders displayed on the protein sequence. The same color code as in A and B is used. Bold residues are forming the hydrophobic core of the protein.</p>", "links"=>[], "tags"=>["ccl2", "lectin", "ligand", "nmr"], "article_id"=>307597, "categories"=>["Biological Sciences", "Biochemistry", "Microbiology", "Biophysics"], "users"=>["Mario Schubert", "Silvia Bleuler-Martinez", "Alex Butschi", "Martin A. Wälti", "Pascal Egloff", "Katrin Stutz", "Shi Yan", "Iain B. H. Wilson", "Michael O. Hengartner", "Markus Aebi", "Frédéric H.-T. Allain", "Markus Künzler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002706.g004", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Solution_structure_of_the_CCL2_lectin_in_the_absence_of_a_ligand_determined_by_NMR_spectroscopy_/307597", "title"=>"Solution structure of the CCL2 lectin in the absence of a ligand determined by NMR spectroscopy.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-17 02:06:37"}
  • {"files"=>["https://ndownloader.figshare.com/files/637556"], "description"=>"<p>(A) ITC experiment of wild type CCL2 binding to GlcNAcβ1,4[Fucα1,3]GlcNAc-spacer. The raw calorimetric output is shown on top, the fitted binding isotherm at the bottom. The protein concentration in the cell was 70 µM, carbohydrate concentration in the syringe was 2.4 mM. (B) Thermodynamic binding parameters of CCL2 (in red) in comparison to other lectins with a focus on high affinity binding. Anti Le<sup>X</sup> Fab: Fab fragment of the monoclonal antibody 291-2G3-4; ConA: concavalin A from jack bean seeds (<i>Canavalia ensiformis</i>); CTB: cholera-toxin B subdomain; GS4: <i>Griffonia simplicifolia</i> lectin 4; MOA: <i>Marasmius oreades</i> agglutinin; RSL: <i>Ralstonia solanacearum</i> fucose-binding lectin; TeNT: tetanus neurotoxin; WBA II: winged bean (<i>Psophocarpus tetragonolobus</i>) acidic agglutinin. For simplicity, lectins that use Ca<sup>2+</sup> for carbohydrate recognition are not displayed. Details for each correlation are found in <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1002706#ppat.1002706.s019\" target=\"_blank\">Table S6</a>. Data points in blue are discussed in the text.</p>", "links"=>[], "tags"=>["binding"], "article_id"=>308039, "categories"=>["Biological Sciences", "Biochemistry", "Microbiology", "Biophysics"], "users"=>["Mario Schubert", "Silvia Bleuler-Martinez", "Alex Butschi", "Martin A. Wälti", "Pascal Egloff", "Katrin Stutz", "Shi Yan", "Iain B. H. Wilson", "Michael O. Hengartner", "Markus Aebi", "Frédéric H.-T. Allain", "Markus Künzler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002706.g007", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Thermodynamic_binding_parameters_/308039", "title"=>"Thermodynamic binding parameters.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-17 02:13:59"}
  • {"files"=>["https://ndownloader.figshare.com/files/637414"], "description"=>"<p>Sequence alignment of several fungal and plant R-type lectins. CCL2_A: CCL2 of <i>C. cinerea</i> strain AmutBmut; CCL2_O: CCL2 of <i>C. cinerea</i> strain Okayama7; CCL1_A: CCL1 of <i>C. cinerea</i> strain AmutBmut; CCL1_O: CCL1 of <i>C. cinerea</i> strain Okayama7; PP_L1: <i>Postia placenta</i> lectin 1 (Pospl1_130016); PP_L2: <i>Postia placenta</i> lectin 2 (Pospl1_121916); SL_L1: <i>Serpula lacrymans</i> lectin 1 (SerlaS7_144703); CP_L1: <i>Coniophora puteana</i> lectin 1 (Conpu1_119225); PO_L1: <i>Pleurotus ostreatus</i> lectin 1 (PleosPC9_89828); PO_L2: <i>Pleurotus ostreatus</i> lectin 2 (PleosPC15_1043947); PO_L3: <i>Pleurotus ostreatus</i> lectin 3 (PleosPC9_64199); PO_L4: <i>Pleurotus ostreatus</i> lectin 4 (PleosPC15_1065820); DS_L1: <i>Dicomitus squalis</i> lectin 1 (Dicsq1); AO_L1: <i>Arthrobotrys oligospora</i> lectin 1 (s00075g2); LB_L1: <i>Laccaria bicolor</i> lectin 1 (Lbic_330799); LB_L2: <i>Laccaria bicolor</i> lectin 2 (Lbic_327918); MOA: <i>Marasmius oreades</i> agglutinin; SNA-II: <i>Sambucus nigra</i> agglutinin/ribosome inactivating protein type II. The distantly related canonical R-type lectins MOA (fungal, 14% sequence identity) and SNA-II (plant, 13% sequence identity) were included in the alignment based on comparison of their 3D structures <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1002706#ppat.1002706-Grahn2\" target=\"_blank\">[70]</a>, <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1002706#ppat.1002706-Maveyraud1\" target=\"_blank\">[71]</a>. The Clustal X color scheme was used. Residues involved in the carbohydrate recognition are indicated at the bottom for CCL2, MOA and SNA-II. The secondary structure of CCL2 and the conservation is indicated as well. The alignment was generated with Jalview <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1002706#ppat.1002706-Waterhouse1\" target=\"_blank\">[72]</a>.</p>", "links"=>[], "tags"=>["ccl2-like", "proteins", "representatives", "fungi"], "article_id"=>307893, "categories"=>["Biological Sciences", "Biochemistry", "Microbiology", "Biophysics"], "users"=>["Mario Schubert", "Silvia Bleuler-Martinez", "Alex Butschi", "Martin A. Wälti", "Pascal Egloff", "Katrin Stutz", "Shi Yan", "Iain B. H. Wilson", "Michael O. Hengartner", "Markus Aebi", "Frédéric H.-T. Allain", "Markus Künzler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002706.g006", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Sequence_conservation_among_CCL2_like_proteins_and_comparison_to_two_typical_representatives_of_fungi_and_plants_/307893", "title"=>"Sequence conservation among CCL2-like proteins and comparison to two typical representatives of fungi and plants.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-17 02:11:33"}
  • {"files"=>["https://ndownloader.figshare.com/files/636880"], "description"=>"<p>Fluorescently labeled CCL2 was analyzed for binding to the mammalian glycan array (V3.1) of the Consortium for Functional Glycomics (CFG). Results shown are averages of triplicate measurements of fluorescence intensity at a lectin concentration of 200 µg/ml. Error bars indicate the standard deviations of the mean. Glycan structures are depicted for those epitopes with highest relative fluorescence. The raw data and the entire list of glycans with the respective spacers can be found on the CFG homepage [<a href=\"http://functionalglycomics.org/\" target=\"_blank\">http://functionalglycomics.org/</a>] or in <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1002706#ppat.1002706.s015\" target=\"_blank\">Tables S2</a> and <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1002706#ppat.1002706.s016\" target=\"_blank\">S3</a>. Binding of 6'sulfo-sialyllactose (glycan #45) is likely to be an artifact since it is also bound by fucose-binding lectin AAL [<a href=\"http://functionalglycomics.org/\" target=\"_blank\">http://functionalglycomics.org/</a>].</p>", "links"=>[], "tags"=>["specificity"], "article_id"=>307363, "categories"=>["Biological Sciences", "Biochemistry", "Microbiology", "Biophysics"], "users"=>["Mario Schubert", "Silvia Bleuler-Martinez", "Alex Butschi", "Martin A. Wälti", "Pascal Egloff", "Katrin Stutz", "Shi Yan", "Iain B. H. Wilson", "Michael O. Hengartner", "Markus Aebi", "Frédéric H.-T. Allain", "Markus Künzler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002706.g002", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Carbohydrate_binding_specificity_of_CCL2_/307363", "title"=>"Carbohydrate-binding specificity of CCL2.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-17 02:02:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/637266"], "description"=>"<p>(A) Intermolecular NOEs observed in a 3D <sup>13</sup>C F1-edited F3-filtered HSQC-NOESY spectrum in a schematic presentation. (B) Structural ensemble of 20 structures of the protein backbone and the carbohydrate in cyan. The subunits α, β and γ are colored green, yellow and orange, respectively. The orientation is identical to <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1002706#ppat-1002706-g004\" target=\"_blank\">Figure 4</a>. (C) Ribbon presentation of the most representative structure. (D) Stereo view of the carbohydrate recognition site. Potential intermolecular hydrogen bonds are shown with dashed magenta lines. (E) Details of the interaction site illustrating how the trisaccharide is recognized by hydrogen bonds. (F) Summary of the interactions between the trisaccharide and CCL2. Potential H-bonds are indicated as dotted lines in magenta and hydrophobic interactions by green lines. (G) Crystal structure of the β-trefoil domain of the fungal lectin MOA in complex with the trisaccharide Galα1,3[Fucα1,2]Gal <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1002706#ppat.1002706-Grahn1\" target=\"_blank\">[19]</a> showing all three occupied canonical binding sites (pdb∶3EF2). For better comparison, the same orientation and colors as in panel B and C were used.</p>", "links"=>[], "tags"=>["ccl2", "lectin", "fucosylated", "chitobiose"], "article_id"=>307741, "categories"=>["Biological Sciences", "Biochemistry", "Microbiology", "Biophysics"], "users"=>["Mario Schubert", "Silvia Bleuler-Martinez", "Alex Butschi", "Martin A. Wälti", "Pascal Egloff", "Katrin Stutz", "Shi Yan", "Iain B. H. Wilson", "Michael O. Hengartner", "Markus Aebi", "Frédéric H.-T. Allain", "Markus Künzler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002706.g005", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_NMR_solution_structure_of_the_CCL2_lectin_in_complex_with_fucosylated_chitobiose_GlcNAc_946_1_4_Fuc_945_1_3_GlcNAc_/307741", "title"=>"NMR solution structure of the CCL2 lectin in complex with fucosylated chitobiose (GlcNAcβ1,4[Fucα1,3]GlcNAc).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-17 02:09:01"}
  • {"files"=>["https://ndownloader.figshare.com/files/637673"], "description"=>"<p>(A) Schematic representation of N-glycan structures in plants, insects and nematodes. Upper panel, left: Typical paucimannosidic plant N-glycan, highly abundant in HRP. Upper panel right: Fucosylated paucimannosidic N-glycan present in <i>D. melanogaster</i>. Lower panel: Fucose biosynthesis and N-glycan structure in <i>C. elegans</i>. Genes coding for enzymes involved in the fucose biosynthesis (lower panel, left) and fucose transfer to the core of N-glycans in <i>C. elegans</i> (lower panel, right) are indicated in dashed boxes. (B) Toxicity of recombinant <i>E. coli</i> expressing CCL2 (black bars) towards <i>C. elegans</i> wildtype (N2) and various fucosylation mutants. Error bars indicate standard errors of the mean. Asterisks (*) show cases where all data were 0. Significant differences were observed between the vector control and CCL2 for N2 (n = 10, p = 0.013), <i>fut-1(ok892)</i> (n = 10, p = 0.013) and <i>fut-6(ok475)</i> (n = 10, p = 0.013) worms, but not for <i>bre-1(ye4)</i> (n = 10, p = 0.329) or <i>fut-6(ok475)fut-1(ok892)</i> (n = 10, p = 0.329). (C) Fluorescence microscopy of <i>C. elegans</i> feeding on <i>E. coli</i> expressing a dTomato-CCL2 fusion protein, showing the grinder and anterior part of the intestine. (D) Toxicity of purified CCL2 towards <i>D. melanogaster</i> quantified as number of developed pupae (gray bars) or flies (black bars). BSA was included as control. Error bars indicate standard errors of the mean. Development of pupae and flies treated with CCL2 were significantly different from the control (pupae: n = 10, p = 0.013; flies: n = 10, p = 0.013). (E) Toxicity of <i>E. coli</i> expressing different CCL2 variants with mutations in residues involved in carbohydrate binding towards <i>C. elegans</i> wildtype (N2). Vector control and CCL2 wildtype (WT) were included as controls. Asterisks (*) show cases where all data were 0. Error bars indicate standard error of the mean. W78A, Y92A and W94A were significantly different from WT control (n = 10, p = 0.013), whereas L87A, N91A, V93A were not (n = 10, p = 1.0).</p>", "links"=>[], "tags"=>["biotoxicity"], "article_id"=>308156, "categories"=>["Biological Sciences", "Biochemistry", "Microbiology", "Biophysics"], "users"=>["Mario Schubert", "Silvia Bleuler-Martinez", "Alex Butschi", "Martin A. Wälti", "Pascal Egloff", "Katrin Stutz", "Shi Yan", "Iain B. H. Wilson", "Michael O. Hengartner", "Markus Aebi", "Frédéric H.-T. Allain", "Markus Künzler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002706.g008", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Carbohydrate_binding_dependent_biotoxicity_of_CCL2_/308156", "title"=>"Carbohydrate-binding dependent biotoxicity of CCL2.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-17 02:15:56"}
  • {"files"=>["https://ndownloader.figshare.com/files/637869"], "description"=>"*<p>Phi values for prolines were omitted.</p>**<p>Pairwise r.m.s. deviation was calculated among 20 refined structures.</p>", "links"=>[], "tags"=>["ccl2", "fucosylated", "chitobiose", "spacer", "was", "truncated", "calculations", "methyl"], "article_id"=>308341, "categories"=>["Biological Sciences", "Biochemistry", "Microbiology", "Biophysics"], "users"=>["Mario Schubert", "Silvia Bleuler-Martinez", "Alex Butschi", "Martin A. Wälti", "Pascal Egloff", "Katrin Stutz", "Shi Yan", "Iain B. H. Wilson", "Michael O. Hengartner", "Markus Aebi", "Frédéric H.-T. Allain", "Markus Künzler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002706.t002", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_NMR_structure_determination_statistics_of_CCL2_in_the_free_form_and_in_complex_with_the_fucosylated_chitobiose_GlcNAc_1_4_Fuc_1_3_GlcNAc_spacer_the_spacer_CH_2_5_COOH_was_truncated_in_the_structure_calculations_to_a_methyl_group_/308341", "title"=>"NMR structure determination statistics of CCL2 in the free form and in complex with the fucosylated chitobiose (GlcNAcβ1,4[Fucα1,3]GlcNAc-spacer, the spacer [CH<sub>2</sub>]<sub>5</sub>COOH was truncated in the structure calculations to a methyl group.).", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2012-05-17 02:19:01"}
  • {"files"=>["https://ndownloader.figshare.com/files/636982"], "description"=>"<p>(A) The chemical and schematic structure of the fucosylated chitobiose (GlcNAcβ1,4[Fucα1,3]GlcNAc-spacer) that was used as ligand for binding studies and structure determination. Indicated is also the B face that is defined as the face on which the carbons are numbered in an anticlockwise order <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1002706#ppat.1002706-Taylor1\" target=\"_blank\">[69]</a>. (B) Chemical shift deviations upon complex formation at a protein concentration of 0.4 mM at pH 5.7. Overlay of <sup>15</sup>N-HSQC spectra of free CCL2 (blue) and CCL2 bound to one equivalent of fucosylated chitobiose (red). (C) Titration of the amide signal of T111 in CCL2 with fucosylated chitobiose using <sup>15</sup>N-HSQC spectra. The protein∶ligand ratio is displayed on the left. (D) Plot of the chemical shift differences between free and bound CCL2 ( δ = [ δ<sub>HN</sub><sup>2</sup>+(δ<sub>N</sub>/R<sub>scale</sub>)<sup>2</sup> ]<sup>1/2</sup>, R<sub>scale</sub> = 5).</p>", "links"=>[], "tags"=>["specificity", "ccl2"], "article_id"=>307461, "categories"=>["Biological Sciences", "Biochemistry", "Microbiology", "Biophysics"], "users"=>["Mario Schubert", "Silvia Bleuler-Martinez", "Alex Butschi", "Martin A. Wälti", "Pascal Egloff", "Katrin Stutz", "Shi Yan", "Iain B. H. Wilson", "Michael O. Hengartner", "Markus Aebi", "Frédéric H.-T. Allain", "Markus Künzler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002706.g003", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Refining_the_specificity_of_the_CCL2_lectin_/307461", "title"=>"Refining the specificity of the CCL2 lectin.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-17 02:04:21"}
  • {"files"=>["https://ndownloader.figshare.com/files/636774"], "description"=>"<p>(A) Specific binding of CCL2 to horseradish peroxidase (HRP). Coomassie-stained SDS-PAGE showing Input, Flow through and Bound (Beads) fractions of a soluble protein extract from <i>C. cinerea</i> fruiting bodies upon affinity-chromatography using immobilized HRP. The Bound fraction was released by boiling the HRP-sepharose beads in Lämmli sample buffer. The loaded protein amount of the Bound fraction (Beads) corresponds to two equivalents of Input and Flow through fractions. Sizes of the marker proteins are indicated. (B) Immunoblot comparing expression levels of CCL2 between vegetative mycelium and fruiting bodies of <i>C. cinerea</i>. Equal amounts of total protein were loaded in each lane. A polyclonal antiserum raised in rabbits against purified CCL2 was used for detection. (C) Comparisons of relative expression ratio (or fold up-regulation) of the genes encoding CCL1 and CCL2 by qRT-PCR in fruiting bodies relative to vegetative mycelium. Error bars represent standard deviation of the mean.</p>", "links"=>[], "tags"=>["differential", "ccl1"], "article_id"=>307251, "categories"=>["Biological Sciences", "Biochemistry", "Microbiology", "Biophysics"], "users"=>["Mario Schubert", "Silvia Bleuler-Martinez", "Alex Butschi", "Martin A. Wälti", "Pascal Egloff", "Katrin Stutz", "Shi Yan", "Iain B. H. Wilson", "Michael O. Hengartner", "Markus Aebi", "Frédéric H.-T. Allain", "Markus Künzler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002706.g001", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Isolation_and_differential_expression_of_C_cinerea_CCL1_and_CCL2_/307251", "title"=>"Isolation and differential expression of <i>C. cinerea</i> CCL1 and CCL2.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-17 02:00:51"}
  • {"files"=>["https://ndownloader.figshare.com/files/637817"], "description"=>"<p>Note that no intermolecular hydrogen bond constraints were used during the calculations.</p>", "links"=>[], "tags"=>["intermolecular", "hydrogen", "bonds", "orientations", "positions"], "article_id"=>308292, "categories"=>["Biological Sciences", "Biochemistry", "Microbiology", "Biophysics"], "users"=>["Mario Schubert", "Silvia Bleuler-Martinez", "Alex Butschi", "Martin A. Wälti", "Pascal Egloff", "Katrin Stutz", "Shi Yan", "Iain B. H. Wilson", "Michael O. Hengartner", "Markus Aebi", "Frédéric H.-T. Allain", "Markus Künzler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1002706.t003", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Potential_intermolecular_protein_8211_carbohydrate_hydrogen_bonds_based_on_the_orientations_and_positions_of_the_carbohydrate_in_the_complex_structure_/308292", "title"=>"Potential intermolecular protein–carbohydrate hydrogen bonds based on the orientations and positions of the carbohydrate in the complex structure.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2012-05-17 02:18:12"}

PMC Usage Stats | Further Information

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Relative Metric

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