The article – T cell activation-associated epitopes of CD147 in regulation of the T cell response, and their definition by antibody affinity and antigen density., International Immunology, 1999 (DOI: 10.3410/f.1000986.793520162) –
has been recommended as being of special significance in the field of Immunology and rated "very good".
„What affinity does an antibody need to be to give effective binding and/or cross-linking? This older paper is still highly relevant, as it describes the systematic analysis of binding of antibodies of varying affinities to T cells expressing CD147 and of activated T cells, which have increased levels of expression. The important findings are that low-affinity antibodies may not give detectable binding in typical labelling experiments unless there is sufficient antigen density, as found on activated T cells. This is a simpler interpretation rather than suggesting neoantigens appear due to activation, as have been proposed in other systems (e.g. CD2). In addition, the functional effects of high-affinity antibodies can be lower at higher concentrations where there may be a greater proportion of antibodies binding bivalently.“
„The appearance of cell surface molecule "activation epitopes" is often assumed to involve protein conformational changes - this paper reminds us there may be a different, and simpler explanation for the appearance of new epitopes, in that low affinity protein clustering could easily be mistaken for protein "activation".
Using the cell surface CD147 protein as a model, it is demonstrated that protein clustering enables increased bivalent monoclonal antibody binding among relatively low affinity monoclonal antibodies.“
Heads of Faculty: Frederick Alt, Douglas Fearon and Philippa Marrack.
01.07.2016back to: Institute for Hygiene and Applied Immunology