Structural insights into antigen recognition of an anti-β-(1,6)-β-(1,3)-D-glucan antibody
Abstract Schizophyllan (SCH) is a high molecular weight homopolysaccharide composed of a β-(1,3)-D-glucan main chain with branching β-(1,6)-bound D-glucose residues. It forms triple helices that are highly stable towards heat and extreme pH, which provides SCH with interesting properties for industr...
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Nature Portfolio
2018
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oai:doaj.org-article:13444bf569474815989dfcbb5d4f17802021-12-02T15:08:16ZStructural insights into antigen recognition of an anti-β-(1,6)-β-(1,3)-D-glucan antibody10.1038/s41598-018-31961-x2045-2322https://doaj.org/article/13444bf569474815989dfcbb5d4f17802018-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-31961-xhttps://doaj.org/toc/2045-2322Abstract Schizophyllan (SCH) is a high molecular weight homopolysaccharide composed of a β-(1,3)-D-glucan main chain with branching β-(1,6)-bound D-glucose residues. It forms triple helices that are highly stable towards heat and extreme pH, which provides SCH with interesting properties for industrial and medical applications. The recombinant anti-SCH antibody JoJ48C11 recognizes SCH and related β-(1,6)-branched β-(1,3)-D-glucans, but details governing its specificity are not known. Here, we fill this gap by determining crystal structures of the antigen binding fragment (Fab) of JoJ48C11 in the apo form and in complex with the unbranched β-(1,3)-D-glucose hexamer laminarihexaose 3.0 and 2.4 Å resolution, respectively. Together with docking studies, this allowed construction of a JoJ48C11/triple-helical SCH complex, leading to the identification of eight amino acid residues of JoJ48C11 (Tyr27H, His35H, Trp47H, Trp100H, Asp105H; Asp49L, Lys52L, Trp90L) that contribute to the recognition of glucose units from all three chains of the SCH triple helix. The importance of these amino acids was confirmed by mutagenesis and ELISA-based analysis. Our work provides an explanation for the specific recognition of triple-helical β-(1,6)-branched β-(1,3)-D-glucans by JoJ48C11 and provides another structure example for anti-carbohydrate antibodies.Kwang Hoon SungJörn JosewskiStefan DübelWulf BlankenfeldtUdo RauNature PortfolioarticleOJ CJSchizophyllan (SCH)Titration ELISALithium SulfateDocking PoseMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-10 (2018) |
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OJ CJ Schizophyllan (SCH) Titration ELISA Lithium Sulfate Docking Pose Medicine R Science Q |
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OJ CJ Schizophyllan (SCH) Titration ELISA Lithium Sulfate Docking Pose Medicine R Science Q Kwang Hoon Sung Jörn Josewski Stefan Dübel Wulf Blankenfeldt Udo Rau Structural insights into antigen recognition of an anti-β-(1,6)-β-(1,3)-D-glucan antibody |
| description |
Abstract Schizophyllan (SCH) is a high molecular weight homopolysaccharide composed of a β-(1,3)-D-glucan main chain with branching β-(1,6)-bound D-glucose residues. It forms triple helices that are highly stable towards heat and extreme pH, which provides SCH with interesting properties for industrial and medical applications. The recombinant anti-SCH antibody JoJ48C11 recognizes SCH and related β-(1,6)-branched β-(1,3)-D-glucans, but details governing its specificity are not known. Here, we fill this gap by determining crystal structures of the antigen binding fragment (Fab) of JoJ48C11 in the apo form and in complex with the unbranched β-(1,3)-D-glucose hexamer laminarihexaose 3.0 and 2.4 Å resolution, respectively. Together with docking studies, this allowed construction of a JoJ48C11/triple-helical SCH complex, leading to the identification of eight amino acid residues of JoJ48C11 (Tyr27H, His35H, Trp47H, Trp100H, Asp105H; Asp49L, Lys52L, Trp90L) that contribute to the recognition of glucose units from all three chains of the SCH triple helix. The importance of these amino acids was confirmed by mutagenesis and ELISA-based analysis. Our work provides an explanation for the specific recognition of triple-helical β-(1,6)-branched β-(1,3)-D-glucans by JoJ48C11 and provides another structure example for anti-carbohydrate antibodies. |
| format |
article |
| author |
Kwang Hoon Sung Jörn Josewski Stefan Dübel Wulf Blankenfeldt Udo Rau |
| author_facet |
Kwang Hoon Sung Jörn Josewski Stefan Dübel Wulf Blankenfeldt Udo Rau |
| author_sort |
Kwang Hoon Sung |
| title |
Structural insights into antigen recognition of an anti-β-(1,6)-β-(1,3)-D-glucan antibody |
| title_short |
Structural insights into antigen recognition of an anti-β-(1,6)-β-(1,3)-D-glucan antibody |
| title_full |
Structural insights into antigen recognition of an anti-β-(1,6)-β-(1,3)-D-glucan antibody |
| title_fullStr |
Structural insights into antigen recognition of an anti-β-(1,6)-β-(1,3)-D-glucan antibody |
| title_full_unstemmed |
Structural insights into antigen recognition of an anti-β-(1,6)-β-(1,3)-D-glucan antibody |
| title_sort |
structural insights into antigen recognition of an anti-β-(1,6)-β-(1,3)-d-glucan antibody |
| publisher |
Nature Portfolio |
| publishDate |
2018 |
| url |
https://doaj.org/article/13444bf569474815989dfcbb5d4f1780 |
| work_keys_str_mv |
AT kwanghoonsung structuralinsightsintoantigenrecognitionofanantib16b13dglucanantibody AT jornjosewski structuralinsightsintoantigenrecognitionofanantib16b13dglucanantibody AT stefandubel structuralinsightsintoantigenrecognitionofanantib16b13dglucanantibody AT wulfblankenfeldt structuralinsightsintoantigenrecognitionofanantib16b13dglucanantibody AT udorau structuralinsightsintoantigenrecognitionofanantib16b13dglucanantibody |
| _version_ |
1718388170730504192 |