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Cited by 53Immunotherapy and Immune ResponsesT-cell and B-cell ImmunologyCancer Immunotherapy and Biomarkers

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Post-translational modifications such as citrullination are excellent targets for cancer therapy

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Brentville, V.A., Vankemmelbeke, M., Metheringham, R.L., Durrant, L.G.·2020·Seminars in Immunology
DOI 10.1016/j.smim.2020.101393
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Abstract

Under conditions of cellular stress, proteins can be post-translationally modified causing them to be recognized by the immune system. One such stress-induced post-translational modification (siPTM) is citrullination, the conversion of arginine residues to citrulline by peptidylarginine deiminase (PAD) enzymes. PAD enzymes are activated by millimolar concentrations of calcium which can occur during apoptosis, leading to precipitation of proteins, their subsequent uptake by B cells and stimulation of antibody responses. Detection of anti-citrullinated protein antibodies (ACPAs) is a diagnostic of rheumatoid arthritis (RA), where immune complexes stimulate inflammation around the joints. More recently, autophagy has been shown to play a role in the presentation of citrullinated peptides on MHC class II molecules to CD4 + helper T cells, suggesting that citrullination may be a way of alerting immune cells to cellular stress. Additionally, inflammation-induced IFNγ and concomitant MHC class II expression on target cells contributes to immune activation. Stressful conditions in the tumor microenvironment induce autophagy in cancer cells as a pro-survival mechanism. Cancer cells also over express PAD enzymes and in light of this the hypothesis that citrullinated peptides stimulate CD4 + T cell responses that would recognize these siPTM’s produced during autophagy has been investigated. The induction of potent citrullinated peptide-specific CD4 responses has been shown in both humans and HLA transgenic mouse models. Responses in mouse models resulted in potent anti-tumour responses against tumours expressing either constitutive or IFNγ-inducible MHC class II. The anti-tumour effect relied upon direct recognition of tumours by specific CD4 T cells suggesting that citrullinated peptides are attractive targets for cancer vaccines.

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Metadata

Authors
Brentville, V. A., Vankemmelbeke, M., Metheringham, R. L., & Durrant, L. G.
Affiliations
University of Nottingham (GB)
Corresponding author
Durrant, L.G.
ORCID
Venue
Seminars in Immunology
Publisher
Elsevier BV
Published
2020-02
Volume
47
Pages
101393
ISSN
1044-5323 (ISSN-L)
DOI
10.1016/j.smim.2020.101393
OpenAlex
W3000264784
Cited by
53
References
4
Citations by year
2026: 3 · 2025: 6 · 2024: 4 · 2023: 4 · 2022: 17 · 2021: 12 · 2020: 7
FWCI
1.00
Type
journal article
Language
en
Open access
Licence
Locations
  • Seminars in Immunology (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
Funders
Scancell Ltd, UK
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
  • Health Sciences › Medicine › Oncology › Cancer Immunotherapy and Biomarkers
Keywords
citrullination, post-translational modification, peptidylarginine deiminase, cancer immunotherapy, cancer vaccines, citrullinated peptides, autophagy, MHC class II, CD4+ T cells, anti-citrullinated protein antibodies, rheumatoid arthritis, tumor microenvironment, interferon-gamma, cellular stress
MeSH terms
Citrullination, Protein-Arginine Deiminases, Animals, Histocompatibility Antigens Class II, Disease Models, Animal, Disease Susceptibility, Humans, Immunotherapy, Neoplasms, Peptides, Protein Processing, Post-Translational, Biomarkers, Tumor, CD4-Positive T-Lymphocytes, Autoimmunity, Molecular Targeted Therapy

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