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dc.contributor.authorCook, Mary E
dc.contributor.authorVarney, Kristen M
dc.contributor.authorGodoy-Ruiz, Raquel
dc.contributor.authorWeber, David J
dc.date.accessioned2020-10-20T13:51:42Z
dc.date.available2020-10-20T13:51:42Z
dc.date.issued2020-10-09
dc.identifier.urihttp://hdl.handle.net/10713/13904
dc.description.abstractClostridioides difficile is a bacterial pathogen responsible for the majority of nosocomial infections in the developed world. C. difficile infection (CDI) is difficult to treat in many cases because hypervirulent strains have evolved that contain a third toxin, termed the C. difficile toxin (CDT), in addition to the two enterotoxins TcdA and TcdB. CDT is a binary toxin comprised of an enzymatic, ADP-ribosyltransferase (ART) toxin component, CDTa, and a pore-forming or delivery subunit, CDTb. In the absence of CDTa, CDTb assembles into two distinct di-heptameric states, a symmetric and an asymmetric form with both states having two surface-accessible host cell receptor-binding domains, termed RBD1 and RBD2. RBD1 has a unique amino acid sequence, when aligned to other well-studied binary toxins (i.e., anthrax), and it contains a novel Ca2+-binding site important for CDTb stability. The other receptor binding domain, RBD2, is critically important for CDT toxicity, and a domain such as this is missing altogether in other binary toxins and shows further that CDT is unique when compared to other binary toxins. In this study, the 1H, 13C, and 15N backbone and sidechain resonances of the 120 amino acid RBD2 domain of CDTb (residues 757-876) were assigned sequence-specifically and provide a framework for future NMR-based drug discovery studies directed towards targeting the most virulent strains of CDI.en_US
dc.description.urihttps://doi.org/10.1007/s12104-020-09979-yen_US
dc.language.isoenen_US
dc.publisherSpringer Science and Business Media B.V.en_US
dc.relation.ispartofBiomolecular NMR assignmentsen_US
dc.subjectBinary toxinen_US
dc.subjectCDIen_US
dc.subjectCDTben_US
dc.subjectClostridioides difficileen_US
dc.title1HN, 13C, and 15N resonance assignments of the Clostridioides difficile receptor binding domain 2 (CDTb, residues 757-876).en_US
dc.typeArticleen_US
dc.identifier.doi10.1007/s12104-020-09979-y
dc.identifier.pmid33034833
dc.source.countryNetherlands


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