Backbone and side chain 1H, 13C and 15N resonance assignments of the catalytic domain of diphtheria toxin

被引:0
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作者
Simon Sauvé
Geneviève Gingras
Yves Aubin
机构
[1] Centre for Vaccine Evaluation,Department of Chemistry
[2] Biologics and Genetic Therapies Directorate,Department of Biochemistry, Molecular Biology and Immunology
[3] Health Canada,Department of Biochemistry
[4] Carleton University,undefined
[5] University of Ottawa,undefined
[6] Université de Montréal,undefined
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关键词
Diphtheria toxin; Catalytic domain; Toxoid; Protein structure;
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学科分类号
摘要
Diphtheria is a serious upper respiratory tract disease caused by the diphtheria toxin (DT) secreted from the bacteria Corynebacterium diphtheriae. Vaccination is the best way to protect against this infectious disease. Diphtheria vaccines are prepared by isolating, purifying and chemically deactivating DT. Although toxoids have been used for decades in immunization, there is still little understanding at the molecular level of the process of toxoid preparation, and how chemical treatment enhances their immunogenicity. We have undertaken an NMR study of the catalytic domain as a first step in understanding the molecular details involved in vaccine antigen preparation. Here we report a near complete assignment for the backbone and side chain resonances of the diphtheria toxin catalytic domain.
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页码:189 / 192
页数:3
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