The immunodominant 38-kDa lipoprotein antigen of Mycobacterium tuberculosis is a phosphate-binding protein.

Several antigens of Mycobacterium tuberculosis have been identified by monoclonal antibodies and are being exploited in the development of improved vaccines and diagnostic reagents, but none has been linked to a specific function. Herein we report that the 38-kDa extracellular lipoprotein antigen, the most potent immunogen of the mycobacteria, is a phosphate-binding protein with features very similar to those of the well characterized periplasmic phosphate-binding protein of Escherichia coli which serves as an initial receptor for active transport. This is also the first report definitively linking a function of a binding protein anchored to a membrane and found in other than Gram-negative bacteria.