{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["MacDonald A"],"funding":["NIDCR NIH HHS","NCI NIH HHS","National Institutes of Health"],"pagination":["755995"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8599986"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12"],"pubmed_abstract":["The phospholipid phosphatidylserine (PS) is naturally maintained on the cytoplasmic side of the plasma membrane. Independent of apoptosis, PS is redistributed to the surface of CD8 T cells in response to TCR-mediated activation. Annexin V (AnnV) is a protein known to bind PS with high affinity and has been effectively utilized to anchor antigen to the surface of CD8 T cells. To expand these studies, we aimed to exploit TCR activation driven PS exposure as a target to deliver cytokine, namely interleukin-2 (IL-2), to the surface of CD8 T cells. This was accomplished using a novel chimeric fusion protein of annexin V and interleukin 2 (AnnV-IL2). <i>In vitro</i> analysis revealed that AnnV-IL2 is able to specifically bind PS on the T cell surface following TCR stimulation. Consequently, AnnV"],"journal":["Frontiers in immunology"],"pubmed_title":["Delivery of IL-2 to the T Cell Surface Through Phosphatidylserine Permits Robust Expansion of CD8 T Cells."],"pmcid":["PMC8599986"],"funding_grant_id":["R21 DE029910","NIH/NCI P50CA098252, NIH/NCI R01CA233486 , R21CA234516, R21DE029910, 5F31CA236051","R01 CA233486","P50 CA098252","F31 CA236051","R21 CA234516"],"pubmed_authors":["MacDonald A","Lam B","Hung CF","Kung YJ","Lin J","Ferrall L","Tsai YC","Wu TC"],"additional_accession":[]},"is_claimable":false,"name":"Delivery of IL-2 to the T Cell Surface Through Phosphatidylserine Permits Robust Expansion of CD8 T Cells.","description":"The phospholipid phosphatidylserine (PS) is naturally maintained on the cytoplasmic side of the plasma membrane. Independent of apoptosis, PS is redistributed to the surface of CD8 T cells in response to TCR-mediated activation. Annexin V (AnnV) is a protein known to bind PS with high affinity and has been effectively utilized to anchor antigen to the surface of CD8 T cells. To expand these studies, we aimed to exploit TCR activation driven PS exposure as a target to deliver cytokine, namely interleukin-2 (IL-2), to the surface of CD8 T cells. This was accomplished using a novel chimeric fusion protein of annexin V and interleukin 2 (AnnV-IL2). <i>In vitro</i> analysis revealed that AnnV-IL2 is able to specifically bind PS on the T cell surface following TCR stimulation. Consequently, AnnV","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021","modification":"2025-06-01T00:03:13.477Z","creation":"2025-06-01T00:03:13.477Z"},"accession":"S-EPMC8599986","cross_references":{"pubmed":["34804041"],"doi":["10.3389/fimmu.2021.755995"]}}