Genetically detoxified pertussis toxin displays near identical structure to its wild-type and exhibits robust immunogenicity View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2020-08-05

AUTHORS

Salvador F. Ausar, Shaolong Zhu, Jessica Duprez, Michael Cohen, Thomas Bertrand, Valérie Steier, Derek J. Wilson, Stephen Li, Anthony Sheung, Roger H. Brookes, Artur Pedyczak, Alexey Rak, D. Andrew James

ABSTRACT

The mutant gdPT R9K/E129G is a genetically detoxified variant of the pertussis toxin (PTx) and represents an attractive candidate for the development of improved pertussis vaccines. The impact of the mutations on the overall protein structure and its immunogenicity has remained elusive. Here we present the crystal structure of gdPT and show that it is nearly identical to that of PTx. Hydrogen-deuterium exchange mass spectrometry revealed dynamic changes in the catalytic domain that directly impacted NAD+ binding which was confirmed by biolayer interferometry. Distal changes in dynamics were also detected in S2-S5 subunit interactions resulting in tighter packing of B-oligomer corresponding to increased thermal stability. Finally, antigen stimulation of human whole blood, analyzed by a previously unreported mass cytometry assay, indicated broader immunogenicity of gdPT compared to pertussis toxoid. These findings establish a direct link between the conserved structure of gdPT and its ability to generate a robust immune response. More... »

PAGES

427

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s42003-020-01153-3

DOI

http://dx.doi.org/10.1038/s42003-020-01153-3

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1129872421

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/32759959


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62 exchange mass spectrometry
63 findings
64 gdPT R9K/E129G
65 human whole blood
66 hydrogen-deuterium exchange mass spectrometry
67 identical structure
68 immune response
69 immunogenicity
70 impact
71 interaction
72 interferometry
73 link
74 mass cytometry assays
75 mass spectrometry
76 mutant gdPT R9K/E129G
77 mutations
78 oligomer corresponding
79 overall protein structure
80 packing
81 pertussis toxin
82 pertussis toxin displays
83 pertussis toxoid
84 pertussis vaccine
85 protein structure
86 response
87 robust immune response
88 robust immunogenicity
89 spectrometry
90 stability
91 stimulation
92 structure
93 subunit interactions
94 thermal stability
95 tight packing
96 toxin
97 toxin displays
98 toxoid
99 unreported mass cytometry assay
100 vaccine
101 variants
102 whole blood
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