1). Wipperman MF, Sampson NS, Thomas ST. Pathogen roid rage: Cholesterol utilization by Mycobacterium tuberculosis. Crit Rev Biochem Mol Biol. 2014; 49:269–93.
2). Bonah C. The ‘experimental stable' of the BCG vaccine: safety, efficacy, proof, and standards, 1921–1933. Stud Hist Philos Biol Biomed Sci. 2005; 36:696–721.
Article
3). Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998; 393:537–44.
4). Glickman MS, Jacobs WR Jr. Microbial pathogenesis of Mycobacterium tuberculosis: dawn of a discipline. Cell. 2001; 104:477–85.
5). Daffé M, Draper P. The envelope layers of mycobacteria with reference to their pathogenicity. Adv Microb Physiol. 1998; 39:131–203.
Article
6). Wilson R, Kumar P, Parashar V, Vilchèze C, Veyron-Churlet R, Freundlich JS, et al. Anti-tuberculosis thiophenes define a requirement for Pks13 in mycolic acid biosynthesis. Nat Chem Biol. 2013; 9:499–506.
Article
7). Sibley LD, Adams LB, Krahenbuhl JL. Inhibition of interferon-gamma-mediated activation in mouse macrophages treated with lipoarabinomannan. Clin Exp Immunol. 1990; 80:141–8.
Article
8). Chatterjee D, Roberts AD, Lowell K, Brennan PJ, Orme IM. Structural basis of capacity of lipoarabinomannan to induce secretion of tumor necrosis factor. Infect Immun. 1992; 60:1249–53.
Article
9). McEvoy CR, Cloete R, Müller B, Schürch AC, van Helden PD, Gagneux S, et al. Comparative Analysis of Mycobacterium tuberculosis pe and ppe genes reveals high sequence variation and an apparent absence of selective constraints. PLoS One. 2012; 7:e30593.
10). Sampson SL. Mycobacterial PE/PPE Proteins at the Host-Pathogen Interface. Clin Dev Immunol. 2010; 2011:497203.
Article
11). Vordermeier HM, Hewinson RG, Wilkinson RJ, Wilkinson KA, Gideon HP, Young DB, et al. Conserved immune recognition hierarchy of mycobacterial PE/PPE proteins during infection in natural hosts. PLoS One. 2012; 7:e40890.
Article
12). Nair S. Immunomodulatory Role of Mycobacterial PE/PPE Family of Proteins. Proc Indian Natn Sci Acad. 2014; 80:1055–72.
Article
13). Chaitra MG, Hariharaputran S, Chandra NR, Shaila MS, Nayak R. Defining putative T cell epitopes from PE and PPE families of proteins of Mycobacterium tuberculosis with vaccine potential. Vaccine. 2005; 23:1265–72.
14). Gey van Pittius NC, Sampson SL, Lee H, Kim Y, van Helden PD, Warren RM. Evolution and expansion of the Mycobacterium tuberculosis PE and PPE multigene families and their association with the duplication of the ESAT-6 (esx) gene cluster region. BMC Evol Biol. 2006; 6:95.
15). Abdallah AM, Gey van Pittius NC, Champion PA, Cox J, Luirink J, Vandenbroucke-Grauls CM, et al. Type VII secretion mycobacteria show the way. Nat Rev Microbiol. 2007; 5:883–91.
16). Sayes F, Sun L, Di Luca M, Simeone R, Degaiffier N, Fiette L, et al. Strong immunogenicity and cross-reactivity of Mycobacterium tuberculosis ESX-5 type VII secretion: encoded PE-PPE proteins predicts vaccine potential. Cell Host Microb. 2012; 11:352–63.
17). Quesniaux V, Fremond C, Jacobs M, Parida S, Nicolle D, Yeremeev V, et al. Toll-like receptor pathways in the immune responses to mycobacteria. Microbes Infect. 2004; 6:946–59.
Article
18). Bafica A, Scanga CA, Feng CG, Leifer C, Cheever A, Sher A. TLR9 regulates Th1 responses and cooperates with TLR2 in mediating optimal resistance to Mycobacterium tuberculosis. J Exp Med. 2005; 202:1715–24.
19). Brightbill HD, Libraty DH, Krutzik SR, Yang RB, Belisle JT, Bleharski JR, et al. Host defense mechanisms triggered by microbial lipoproteins through toll-like receptors. Science. 1999; 285:732–6.
Article
20). Gehring AJ, Dobos KM, Belisle JT, Harding CV, Boom WH. Mycobacterium tuberculosis LprG (Rv1411c): a novel TLR-2 ligand that inhibits human macrophage class II MHC antigen processing. J Immunol. 2004; 173:2660–8.
21). Fortune SM, Solache A, Jaeger A, Hill PJ, Belisle JT, Bloom BR, et al. Mycobacterium tuberculosis inhibits macrophage responses to IFN-gamma through myeloid differentiation factor 88-dependent and -independent mechanisms. J Immunol. 2004; 172:6272–80.
22). Higgins DM, Sanchez-Campillo J, Rosas-Taraco AG, Lee EJ, Orme IM, Gonzalez-Juarrero M. Lack of IL-10 alters inflammatory and immune responses during pulmonary Mycobacterium tuberculosis infection. Tuberculosis. 2009; 89:149–57.
23). Mukhopadhyay S, Balaji KN. The PE and PPE proteins of Mycobacterium tuberculosis. Tuberculosis. 2011; 91:441–7.
24). Betts JC, Lukey PT, Robb LC, McAdam RA, Duncan K. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Mol Microbiol. 2002; 43:717–31.
25). Nair S, Pandey AD, Mukhopadhyay S. The PPE18 protein of Mycobacterium tuberculosis inhibits NF-kappaB/rel-mediated proinflammatory cytokine production by upregulating and phosphorylating suppressor of cytokine signaling 3 protein. J Immunol. 2011; 186:5413–24.
26). Ahmed A, Das A, Mukhopadhyay S. Immunoregulatory functions and expression patterns of PE/PPE family members: Roles in pathogenicity and impact on anti-tuberculosis vaccine and drug design. IUBMB Life. 2015; 67:414–27.
Article
27). Maglione PJ, Xu J, Chan J. B cells moderate inflammatory progression and enhance bacterial containment upon pulmonary challenge with Mycobacterium tuberculosis. J Immunol. 2007; 178:7222–34.
28). Delogu G, Brennan MJ. Comparative immune response to PE and PE_PGRS antigens of Mycobacterium tuberculosis. Infect Immun. 2001; 69:5606–11.
29). Jang B, Shin SJ. Peptidylarginine Deiminase and Citrullination: Potential Therapeutic Targets for Inflammatory Diseases. J Bacteriol Virol. 2013; 43:159–67.
Article
30). Cha SB, Shin SJ. Mycobacterium bovis Bacillus Calmette-Guerin (BCG) and BCG-based vaccines against Tuberculosis. J Bacteriol Virol. 2014; 44:236–43.