ArticleCancer immunology, immunotherapy : CII2011
An engineered superantigen SEC2 exhibits promising antitumor activity and low toxicity.
Article in Cancer immunology, immunotherapy : CII, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- T cell related osteoimmunology in fracture healing: Potential targets for augmenting bone regeneration.Journal of orthopaedic translation · 2025Review
- Staphylococcal enterotoxin B as DNA vaccine against breast cancer in a murine model.International microbiology : the official journal of the Spanish Society for Microbiology · 2023Article
- Low-Dose Staphylococcal Enterotoxin C2 Mutant Maintains Bone Homeostasis via Regulating Crosstalk between Bone Formation and Host T-Cell Effector Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Staphylococcal Enterotoxin C2 Mutant-Induced Antitumor Immune Response Is Controlled by CDC42/MLC2-Mediated Tumor Cell Stiffness.International journal of molecular sciences · 2023Article
- Enhanced interaction between SEC2 mutant and TCR Vβ induces MHC II-independent activation of T cells via PKCθ/NF-κB and IL-2R/STAT5 signaling pathways.The Journal of biological chemistry · 2018Article
- In vitro effects of Staphylococcus aureus enterotoxin C3 on T cell activation, proliferation and cytokine production.Molecular medicine reports · 2017Article
- Article
- In Silico Design and Analysis of TGFαL3-SEB Fusion Protein as "a New Antitumor Agent" Candidate by Ligand-Targeted Superantigens Technique.Iranian journal of cancer prevention · 2014Article
- Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent studies suggested that the histidine residues at 118 and 122 play an important role for the toxicity of staphylococcal enterotoxin C subtype 2 (SEC2), and the substitutions of both histidines with alanine can severely impair the fever activity of SEC2. We hypothesized that promising SEC2 antitumor agent with low toxicity and enhanced superantigen activity can be constructed by introducing related mutations at protein functional sites of SEC2. We showed that the SEC2 mutants H122A and H118A/H122A exhibited improved superantigen activity after introducing the point mutations at Thr20 and Gly22. A resultant mutant, named as SAM-3, has considerable abilities to inhibit the growth of H22 and Hepa1-6 tumor cells in vitro and colon 26 solid tumor in vivo. Furthermore, SAM-3 also exhibits significantly reduced toxicity compared with native SEC2. The study provides a novel strategy for designing promising superantigen immunotherapeutic agent. The constructed SEC2 mutant SAM-3 can be used as a powerful candidate for cancer immunotherapy and could compensate the deficiency caused by toxicity of native SEC2 in clinic.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.