The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan, and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. FbpA mediates triacylglycerol (TAG) formation with long-chain acyl-CoA as the acyl donor and 1,2-dipalmitoyl-sn-glycerol (1,2-dipalmitin) as the acyl acceptor. It has a preference for C26:0-CoA over C18:1-CoA.
