Ask about this productRelated genes to: BTN2A1 Blocking Peptide
- Gene:
- BTN2A1 NIH gene
- Name:
- butyrophilin subfamily 2 member A1
- Previous symbol:
- -
- Synonyms:
- BT2.1, BTF1, BTN2.1
- Chromosome:
- 6p22.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-08-27
- Date modifiied:
- 2016-10-05
Related products to: BTN2A1 Blocking Peptide
Related articles to: BTN2A1 Blocking Peptide
- Anti-GD2 monoclonal antibody effectively treats high-risk neuroblastoma (HR-NB) by recruiting NK cells for antibody-dependent cellular cytotoxicity (ADCC). We recently developed a cell product containing mature, cytotoxic γδ T and NK cells (GADEKILL), and its potential use as a novel immunotherapy for HR-NB has been investigated. - Source: PubMed
Publication date: 2026/01/30
Morandi FabioDella Lastra MartinaPastorino FabioCiampi EleonoraFaraci MauraBrignole ChiaraGiardino StefanoAiroldi Irma - Phosphoantigens (pAgs) are phosphate-containing small molecules that elicit an immune response. The pAgs bind to the intracellular domain of butyrophilin 3 (BTN3), enabling interactions with other butyrophilins to form complexes that trigger the T cell receptor (TCR) of Vγ9Vδ2 (γ9δ2) T cells. Despite multiple reports on this process, the conditions that regulate pAg levels leading to their detection remain unclear. Here we reveal a novel stress detection pathway, a type of lymphoid stress-surveillance response, in which mild cold stress triggers endogenous pAgs to engage with BTN family proteins, leading to the activation of γ9δ2 T cells. This stress response is dependent upon endogenous pAgs, as inhibition of HMG-CoA reductase abrogates the effect. It is also dependent upon BTN proteins, as depletion of BTN3A1 reduces the response. The ability of BTN2A1/BTN3A1 to respond is enhanced by the presence of BTN3A2 or BTN3A3. Furthermore, the internal domains of BTN2A1, BTN3A1, and BTN3A3 display differing abilities to dimerize, with BTN2A1 a constitutive dimer, BTN3A1 a monomer, and BTN3A3 a concentration dependent dimer. Full length BTN2A1/3A1 hybrid proteins additionally reveal that appropriately spaced multimers of BTN2A1 and BTN3A1 are critical in engaging the γ9δ2 TCR. In summary, our study uncovers a novel γ9δ2 T cell activation pathway mediated by cell stress and mevalonate pathway intermediates and highlights the critical roles of the BTN family members and their spacing in this process. - Source: PubMed
Publication date: 2026/01/22
Jin YimingNguyen KhiemBashir SidraPawge GirijaStrand Reagan MHsiao Chia-Hung ChristineVinogradova OlgaWiemer Andrew J - Schizophrenia (SCZ) has strong genetic underpinnings, yet the functional impact of associated genetic variants remains unclear. We computationally analyzed SCZ-associated missense single-nucleotide polymorphisms (SNPs) from the National Human Genome Research Institute-European Bioinformatics Institute (NHGRI-EBI) Genome-Wide Association Studies (GWAS) Catalog to identify variants with significant functional consequences. From 5083 SCZ-associated SNPs, we prioritized five genes harboring highly deleterious missense SNPs: STX2, BTN2A1, and UGT1A8/9/10. We integrated pathogenicity predictions, protein stability assessments, structural analyses, and protein-protein interaction networks to understand how these SCZ-associated missense variants may contribute to disease pathogenesis. Amino acid changes, or variants, of the five genes were consistently predicted to decrease protein stability. The STX2 variant affects the syntaxin N-terminus domain, crucial for neurotransmitter release and implicated in antipsychotic pharmacology. The BTN2A1 variants disrupt immunoglobulin-like domains involved in T-cell regulation. The UGT1A8/9/10 variant impacts the UDP-glycosyltransferase domain, potentially altering drug metabolism. Protein interaction analyses revealed connections to synaptic signaling, immune regulation, and xenobiotic metabolism pathways implicated in SCZ. Our findings illuminate potential molecular mechanisms by which these genetic variants may contribute to SCZ pathophysiology and highlight promising targets for therapeutic development. - Source: PubMed
Publication date: 2026/01/14
Coppin Fatimah MKwon MichelleBakhteri AriyaAbugaliyeva Aziza - The effectiveness of immunotherapies against glioblastoma (GB) remains limited. A major obstacle in advancing new strategies is the reliance on non-autologous systems, which do not accurately mimic the true extent of inter-patient heterogeneity in both immune responses and tumor susceptibility. This often leads to misleading conclusions about therapeutic efficacy and targetability. - Source: PubMed
Publication date: 2025/12/17
Nicolasen Mara J TGatti Lucrezia CdeGasull-Celades LaiaBrazda PeterBotas MartaZawal Danielvan Vliet Esmee JCleven AstridSebestyén ZsoltRobe Pierre ABeringer Dennis XKuball Jurgen - The activation of human Vδ2 γδ T cells by phosphoantigens (pAg) strictly depends on transmembrane butyrophilin (BTN) molecules, specifically BTN3A isoforms and BTN2A1. Several bacteria, including , produce potent pAg and thus trigger a strong activation of Vδ2 T cells. The antigen-specific activation of CD4 and regulatory (Treg) T cells can be monitored by the rapid upregulation of CD154 and CD137, respectively. We have previously established that CD137 is also rapidly upregulated on Vδ2 T cells upon stimulation with pAg. In the present study, we have used antagonistic anti-BTN3A/2A1 antibodies to dissect the pAg-dependent and pAg-independent activation of Vδ2 T cells by various microbes. While the activation of Vδ2 T cells by pAg and aminobisphosphonate zoledronate was completely blocked by anti-BTN3A/2A1 antibodies, only partial inhibition was observed for activation with and other bacteria as analyzed by CD137/CD154 upregulation and intracellular interferon-γ expression. Similarly, anti-TCR antibody 7A5 and Lck inhibitor emodin had only a minimal inhibitory effect on activation by bacteria but strongly reduced pAg activation of Vδ2 T cells. Further studies revealed a crucial role of IL-18 in the BTN/TCR-independent early activation of Vδ2 T cells by bacteria. Neutralizing anti-IL-18 antibodies and inflammasome inhibition did not affect pAg activation of Vδ2 T cells but strongly reduced their activation by bacteria. Our results identify a BTN/TCR-independent but IL-18 and inflammasome-dependent activation pathway of Vδ2 T cells, which might be relevant for the role of Vδ2 T cells during bacterial infections. - Source: PubMed
Publication date: 2025/11/13
Gombert DanielSimeonov JaraKlein KatharinaAgaugué SophieScheffold AlexanderKabelitz DieterPeters Christian