Mycobacterial porins and other beta-barrel outer-membrane proteins are 
represented by the structure of Mycobacterium smegmatis porin MspA. On the basis 
of existing knowledge of beta-barrel outer-membrane proteins, several state of 
the art prediction methods, as well as a new in-house program (PROB) were 
employed for the systematic exploration of Mycobacterium tuberculosis predicted 
proteomes for potential beta-barrel structures. PROB allowed parameter 
optimization while functioning with an adaptive algorithm for the detection of 
outer-membrane beta-barrel proteins in highly divergent proteomes. As a result 
of the predictions, 114 proteins in total were predicted to be beta-barrel 
structures; of these, 40 were PE-PPE proteins, 8 Mce proteins, 24 hypothetical, 
11 probable membrane proteins, 10 transporters, 4 lipoproteins, and 14 
classified as other. The congruence among three of the predictors, PROB, 
TMB-Hunt, and BOMP, was low with only three proteins (MT0318, MT0356, and 
MT2423) predicted by the three. Overall, 79 new proteins for which no previous 
experimental work has been performed are reported. At least 10 of these have 
high potential of being not only surface-exposed but also served as putative 
vaccine candidates as determined by in silico predictions of CD4T cell MHC-II 
restricted epitopes.