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TitleHydrophobic interactions dominate the recognition of a KRAS G12V neoantigen.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 5063, Year 2023
Publish dateAug 21, 2023
AuthorsKatharine M Wright / Sarah R DiNapoli / Michelle S Miller / P Aitana Azurmendi / Xiaowei Zhao / Zhiheng Yu / Mayukh Chakrabarti / WuXian Shi / Jacqueline Douglass / Michael S Hwang / Emily Han-Chung Hsiue / Brian J Mog / Alexander H Pearlman / Suman Paul / Maximilian F Konig / Drew M Pardoll / Chetan Bettegowda / Nickolas Papadopoulos / Kenneth W Kinzler / Bert Vogelstein / Shibin Zhou / Sandra B Gabelli /
PubMed AbstractSpecificity remains a major challenge to current therapeutic strategies for cancer. Mutation associated neoantigens (MANAs) are products of genetic alterations, making them highly specific ...Specificity remains a major challenge to current therapeutic strategies for cancer. Mutation associated neoantigens (MANAs) are products of genetic alterations, making them highly specific therapeutic targets. MANAs are HLA-presented (pHLA) peptides derived from intracellular mutant proteins that are otherwise inaccessible to antibody-based therapeutics. Here, we describe the cryo-EM structure of an antibody-MANA pHLA complex. Specifically, we determine a TCR mimic (TCRm) antibody bound to its MANA target, the KRAS peptide presented by HLA-A*03:01. Hydrophobic residues appear to account for the specificity of the mutant G12V residue. We also determine the structure of the wild-type G12 peptide bound to HLA-A*03:01, using X-ray crystallography. Based on these structures, we perform screens to validate the key residues required for peptide specificity. These experiments led us to a model for discrimination between the mutant and the wild-type peptides presented on HLA-A*03:01 based exclusively on hydrophobic interactions.
External linksNat Commun / PubMed:37604828 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.594 - 3.14 Å
Structure data

25427

7stf

EMDB-25427, PDB-7stf:
Structure of KRAS G12V/HLA-A*03:01 in complex with antibody fragment V2
Method: EM (single particle) / Resolution: 3.14 Å

PDB-8dvg:
Structure of KRAS WT(7-16)-HLA-A*03:01
Method: X-RAY DIFFRACTION / Resolution: 2.594 Å

Chemicals

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER / Diethylene glycol

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsIMMUNE SYSTEM / Complex / MHC-I / KRAS / HLA-A3 / immunotherapy

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