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Resistance to the isocitrate dehydrogenase 1 mutant inhibitor ivosidenib can be overcome by alternative dimer-interface binding inhibitors

Abstract:
Ivosidenib, an inhibitor of isocitrate dehydrogenase 1 (IDH1) R132C and R132H variants, is approved for the treatment of acute myeloid leukaemia (AML). Resistance to ivosidenib due to a second site mutation of IDH1 R132C, leading to IDH1 R132C/S280F, has emerged. We describe biochemical, crystallographic, and cellular studies on the IDH1 R132C/S280F and R132H/S280F variants that inform on the mechanism of second-site resistance, which involves both modulation of inhibitor binding at the IDH1 dimer-interface and alteration of kinetic properties, which enable more efficient 2-HG production relative to IDH1 R132C and IDH1 R132H. Importantly, the biochemical and cellular results demonstrate that it should be possible to overcome S280F mediated resistance in AML patients by using alternative inhibitors, including some presently in phase 2 clinical trials.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-022-32436-4

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Role:
Author
ORCID:
0000-0002-7181-6790
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Role:
Author
ORCID:
0000-0002-3205-9969
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ORCID:
0000-0002-3448-9559
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ORCID:
0000-0001-7935-6269
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Author
ORCID:
0000-0002-5021-2111


Publisher:
Springer Nature
Journal:
Nature Communications More from this journal
Volume:
13
Article number:
4785
Publication date:
2022-08-15
Acceptance date:
2022-07-25
DOI:
EISSN:
2041-1723
Pmid:
35970853


Language:
English
Keywords:
Pubs id:
1274389
Local pid:
pubs:1274389
Deposit date:
2022-11-22

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