Bispecific antibodies targeting mutant RAS neoantigens
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Bispecific T cell–engaging antibodies capable of specifically killing cancer cells expressing mutant RAS neoantigens were generated.
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Peptides derived from KRASG12 variants and from KRASQ61H/L/R are presented on the surface of malignant cells by various MHC I (HLA-A) molecules.
“As noted above, peptides derived from KRASG12 variants193,194, and also from KRASQ61H/L/R (ref.198), have been demonstrated to be presented on the surface of malignant cells by various MHC I (HLA-A) molecules.”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [198]
Diabodies engineered to recognize MHC I-peptide complexes on KRAS-mutant cells and to bind CD3 induced T cell-mediated cytotoxicity in vitro, with some anticancer activity in mouse models that did not reach statistical significance.
“Bispecific dimeric single-chain antibody fragment constructs, so-called ‘diabodies’, have been engineered to recognize such MHC I–peptide complexes on KRAS-mutant cells and recruit T cells by simultaneously binding to CD3; these agents induced T cell-mediated cytotoxicity in vitro, with some anticancer activity observed in mouse models (although the effect did not reach statistical significance)”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [198]
Preclinical studies have identified bi-specific T cell engager molecules that bind mutant RAS peptide neoepitopes (G12V, Q61H/L/R) complexed with HLA and induce T cell-mediated killing of cancer cells expressing endogenous mutant RAS and cognate HLA alleles.
“Recent preclinical studies have identified bi-specific T cell engager protein molecules that specifically bind to mutant RAS peptide neoepitopes (G12V, Q61H/L/R) complexed with human leukocyte antigen inducing T cell-mediated killing of target cancer cells expressing endogenous levels of the mutant RAS proteins and cognate HLA alleles (85).”
From Expanding the Reach of Precision Oncology by Drugging All <i>KRAS</i> Mutants (2022) · cites this paper as [85]
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The current state of the art and future trends in RAS-targeted cancer therapies
Punekar, S. R., Velcheti, V., Neel, B. G., & Wong, K.-K. (2022) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-022-00671-9 · Cited by 549 · see citing works
Targeting a neoantigen derived from a common <i>TP53</i> mutation
Hsiue, E. H.-C., Wright, K. M., Douglass, J., Hwang, M. S., Mog, B. J., Pearlman, A. H., Paul, S., DiNapoli, S. R., Konig, M. F., Wang, Q., et al. (2021) · Science · doi:10.1126/science.abc8697 · Cited by 367 · see citing works
Self-citationExpanding the Reach of Precision Oncology by Drugging All <i>KRAS</i> Mutants
Hofmann, M. H., Gerlach, D., Misale, S., Petronczki, M., & Kraut, N. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-1331 · Cited by 336 · see citing works
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- Authors
- Douglass, J., Hsiue, E. H.-C., Mog, B. J., Hwang, M. S., DiNapoli, S. R., Pearlman, A. H., Miller, M. S., Wright, K. M., Azurmendi, P. A., Wang, Q., Paul, S., Schaefer, A., Skora, A. D., Molin, M. D., Konig, M. F., Liu, Q., Watson, E., Li, Y., Murphy, M. B., Pardoll, D. M., Bettegowda, C., Papadopoulos, N., Gabelli, S. B., Kinzler, K. W., Vogelstein, B., & Zhou, S.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of Maryland Medical Center (US)
- Johns Hopkins University (US)
- Cytiva, Marlborough, MA 01752, USA.
- Corresponding author
- Douglass, Jacqueline
- Hsiue, Emily Han-Chung
- Mog, Brian J.
- Hwang, Michael S.
- DiNapoli, Sarah R.
- Pearlman, Alexander H.
- Wang, Qing
- Vogelstein, Bert
- Zhou, Shibin
- ORCID
- Douglass, Jacqueline
- Hsiue, Emily Han-Chung
- Mog, Brian J.
- Hwang, Michael S.
- DiNapoli, Sarah R.
- Pearlman, Alexander H.
- Miller, Michelle S.
- Wright, Katharine M.
- Azurmendi, P. Aitana
- Wang, Qing
- Paul, Suman
- Schaefer, Annika
- Skora, Andrew D.
- Molin, Marco Dal
- Konig, Maximilian F.
- Liu, Qiang
- Li, Yana
- Murphy, Michael B.
- Pardoll, Drew M.
- Bettegowda, Chetan
- Papadopoulos, Nickolas
- Gabelli, Sandra B.
- Kinzler, Kenneth W.
- Vogelstein, Bert
- Zhou, Shibin
- Venue
- Science Immunology
- Published
- 2021-03-04
- Volume
- 6
- Issue
- 57
- ISSN
- 2470-9468 (ISSN-L)
- PMC
- PMC8141259
- OpenAlex
- W3134794297
- Cited by
- 171
- References
- 67
- Citations by year
- 2026: 18 · 2025: 29 · 2024: 22 · 2023: 34 · 2022: 37 · 2021: 31
- FWCI
- 16.38
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science Immunology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- NIH Office of the Director (5T32CA009071-38, T32 GM73009)
- National Cancer Institute (R37 CA230400)
- Commonwealth Fund
- Lustgarten Foundation
- Bloomberg~Kimmel Institute for Cancer Immunotherapy, Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University
- Bloomberg Philanthropies
- The Virginia and D.K. Ludwig Fund for Cancer Research
- The Mark Foundation for Cancer Research
- NIH Cancer Center Support (P30 CA006973)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases of the National Institutes of Health (T32AR048522)
- SITC-Amgen Cancer Immunotherapy in Hematologic Malignancies Fellowship
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Health Sciences › Medicine › Oncology › Cancer Immunotherapy and Biomarkers
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- bispecific antibodies, RAS mutations, neoantigens, oncogenic mutations, cancer immunotherapy
- MeSH terms
- Amino Acid Sequence, Animals, Antigens, Neoplasm, Cell Line, Cross Reactions, HLA Antigens, Humans, Lymphocyte Activation, Mutation, Peptide Fragments, Protein Binding, Biomarkers, Tumor, T-Lymphocyte Subsets, Antibodies, Bispecific, ras Proteins, Mutant Proteins
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