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. 2022 Aug 11;9:889667. doi: 10.3389/fmolb.2022.889667

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Copyright © 2022 Paliwal, Thom, Hussein, Ravishankar, Wilkes, Charleston and Jones.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Example histidine-tagged M. bovis proteins purified by immobilised metal affinity chromatography pull down with magnetic beads from E.coli (A) and insect cells (B). The lane identity and predicted molecular masses are: Panel A, 1-Mb0704 (44 kDa), 2-Mb3070 (37 kDa), 3-Mb2054 (36 kDa), 4-Mb2002_Mb0062 (35 kDa), 5-Mb0671 (17 kDa), 6-Mb0854 (31 kDa), 7- Mb3157c_Mb3743c (37 kDa), 8-Mb0337 (26 kDa). Panel B, 1-PE5_PE32 (19.5 kDa), 2-LpqN (25 kDa), 3-LpqX (22 kDa), 4-EsxAB (21.2 kDa), 5-EsxFDE (27.3 kDa), 6-EsxNOQ (30 kDa), 7- EsxRST (32 kDa), 8-EsxU (24 kDa), 9- Mb0485 (21 kDa), 10-PPE41_PE25 (34 kDa), 11-Mb1228 (39 kDa), 12-PPE69_PE36 (46.6 kDa), 13- PPE68_PE35 (47.5 kDa), 14-PPE14_PE7 (51 kDa), 15-PPE4_PE5 (67 kDa), 16- PPE15_PE8 (66 kDa), 17- PPE20_PE15 (67 kDa), 18-PPE31_PE20 (51 kDa). Asterisk (*) indicates all Esx related proteins, most as concatenates. Diamonds (♦) indicate concatenated PPE-PE pairs. M indicates the marker track, the molecular masses of which are given on the left of panel (A) in kilodaltons.