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dc.contributor.authorSung, Kwang Hoon
dc.contributor.authorJosewski, Jörn
dc.contributor.authorDübel, Stefan
dc.contributor.authorBlankenfeldt, Wulf
dc.contributor.authorRau, Udo
dc.date.accessioned2018-11-13T12:50:41Z
dc.date.available2018-11-13T12:50:41Z
dc.date.issued2018-09-12
dc.identifier.issn2045-2322
dc.identifier.pmid30209318
dc.identifier.doi10.1038/s41598-018-31961-x
dc.identifier.urihttp://hdl.handle.net/10033/621557
dc.description.abstractSchizophyllan (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 (Tyr27en_US
dc.rightsAttribution-NonCommercial-ShareAlike 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/us/*
dc.titleStructural insights into antigen recognition of an anti-β-(1,6)-β-(1,3)-D-glucan antibody.en_US
dc.typeArticleen_US
dc.contributor.departmentHZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.en_US
refterms.dateFOA2018-11-13T12:50:42Z
dc.source.journaltitleScientific reports


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