ABSTRACT
In mycobacteria secreted proteins represent a distinct group, probably of particular importance for development of immune responses following infection. Quantification of individual proteins in Mycobacterium tuberculosis culture fluid and corresponding disrupted bacilli permits determination of a localization index for identification of secreted proteins. This procedure cannot be applied for Mycobacterium leprae since secreted proteins are lost during isolation of bacilli from tissues. The DNA sequences of secreted proteins of M. tuberculosis were compared with sequences of M. leprae. Genes for homologues of the 85a, 85b, 85c, mpt32 (apa), mpt51, erp, mtc28, mtb12, Rv3354 and Rv0526 genes were identified. All of these and six genes of the mcel operon contain signal sequences for secretion in M. leprae as well. In several instances the local distance between marker genes and occurrence on the same or the complementary DNA strand was similar in these two species. The genomic organization of genes for secreted proteins is thus very similar in M. leprae and M. tuberculosis, the homology being higher for the mature polypeptide chains than for the corresponding signal peptides.