Lymphocyte function-associated antigen 1, also known as LFA-1 is found on all T-cells and also on B-cells, macrophages and neutrophils and is involved in recruitment to the site of infection. It binds to ICAM-1 on antigen-presenting cells and functions as an adhesion molecule. LFA-1 is the first to bind T-cells to antigen-presenting cells and initially binds weakly. A signal from the T-cell receptor and/or the cytokine receptor changes the conformation and prolongs the cell contact, allowing the T-cell to proliferate. LFA-1/ICAM-1 interaction has recently been shown to be important for T cell-T cell interactions, leading to further T cell differentiation.
LFA-1 is part of the family of leukocyte integrins that are recognised by their common β-chains (β2, CD18). LFA-1 also has a distinct α-chain (αL, CD11a).
^Gjelstrup, L. C.; Boesen, T.; Kragstrup, T. W.; Jorgensen, A.; Klein, N. J.; Thiel, S.; Deleuran, B. W.; Vorup-Jensen, T. (8 September 2010). "Shedding of Large Functionally Active CD11/CD18 Integrin Complexes from Leukocyte Membranes during Synovial Inflammation Distinguishes Three Types of Arthritis through Differential Epitope Exposure". The Journal of Immunology185 (7): 4154–4168. doi:10.4049/jimmunol.1000952.
Audrey Gérard, Omar Khan, Peter Beemiller, Erin Oswald, Joyce Hu, Mehrdad Matloubian, Matthew F Krummel (2013). "Secondary T cell–T cell synaptic interactions drive the differentiation of protective CD8+ T cells". Nature Immunology14: 356–363. doi:10.1038/ni.2547.