Microbiology
Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics , by S. Sinha, K. Kosalai, S. Arora, A. Namane, P. Sharma, A. N. Gaikwad, P. Brodin and S. T. Cole
Microbiology vol. 151, part 7, pp. 2411 - 2419
Supplementary Table
Protein identification data. Peptide-mass mapping of 116 samples [47 originating from detergent-phase (DP) and 69 from the aqueous-phase (AP) protein pools] led to the identification of 105 proteins. Typically, many proteins were present in >1 sample (mostly from 2-D gel electrophoresis) and many samples (especially from 1-D gel electrophoresis) contained >1 protein. Out of the identified proteins, 73 belonged to DP and 19 to AP protein pools. The remaining 13 proteins were common to both (DP/AP). A total of 9 proteins had no previous references in databases or publications pertaining to the Mycobacterium tuberculosis proteome; hence they were considered as ‘new’ to the proteome. Bioinformatic analyses indicated that 77 (73 %) proteins (57 from DP, 12 from AP and 8 from DP/AP) could be considered as ‘membrane-associated’ since their GRAVY scores predicted a hydrophobic character. Similarly, 45 (43 %) proteins (34 from DP, 8 from AP and 3 from DP/AP) were considered as ‘membrane-bound’ as they were predicted to have one or more transmembrane regions with or without a lipid attachment site or signal sequence. Among the 9 newly described proteins, 8 (89 %) possessed transmembrane regions. According to the TubercuList database, the majority of the identified proteins belonged to the following five functional categories: category 2 (information pathways, 32 proteins), category 3 (cell wall and cell processes, 20 proteins), category 7 (intermediary metabolism and respiration, 22 proteins) and category [8+10] (unknowns+conserved hypotheticals, 20 proteins). Most (73 out of 105) proteins had a functional orthologue in Mycobacterium leprae.[ PDF file ] (486kb)
Copyright © 2008 Society for General Microbiology.
