Molecular Virulence Mechanisms of Mycobacterium bovis 121
at: https://www.daera-ni.gov.uk/sites/default/files/publications/dard/afbi-literature-review-tb-review-
cattle-to-cattle-transmission.pdf (accessed 21 February 2018).
Smith, T. (1898) A comparative study of bovine tubercle bacilli and of human bacilli from sputum. The Jour-
nal of Experimental Medicine 3, 451–511.
Smith, N.H., Kremer, K., Inwald, J., Dale, J., Driscoll, J.R., et al. (2006) Ecotypes of the Mycobacterium
tuberculosis complex. Journal of Theoretical Biology 239, 220–225.
Sreevatsan, S., Pan, X., Stockbauer, K.E., Connell, N.D., Kreiswirth, B.N., et al. (1997) Restricted structural
gene polymorphism in the Mycobacterium tuberculosis complex indicates evolutionarily recent global
dissemination. Proceedings of the National Academy of Sciences of the United States of America 94,
9869–9874.
Srivastava, V., Rouanet, C., Srivastava, R., Ramalingam, B., Locht, C., et al. (2007) Macrophage-specific
Mycobacterium tuberculosis genes: identification by green fluorescent protein and kanamycin resis-
tance selection. Microbiology 153, 659–666.
Stewart, G.R., Patel, J., Robertson, B.D., Rae, A. and Young, D.B. (2005) Mycobacterial mutants with defec-
tive control of phagosomal acidification. PLoS Pathogens 1, 269–278.
Swanson, S., Ioerger, T.R., Rigel, N.W., Miller, B.K., Braunstein, M., et al. (2015) Structural similarities and
differences between two functionally distinct seca proteins, Mycobacterium tuberculosis SecA1 and
SecA2. Journal of Bacteriology 198, 720–730.
Triccas, J.A., Berthet, F.X., Pelicic, V. and Gicquel, B. (1999) Use of fluorescence induction and sucrose
counterselection to identify Mycobacterium tuberculosis genes expressed within host cells. Microbiol-
ogy 145(10), 2923–2930.
Trivedi, O.A., Arora, P., Vats, A., Ansari, M.Z., Tickoo, R., et al. (2005) Dissecting the mechanism and
assembly of a complex virulence mycobacterial lipid. Molecular Cell 17, 631–643.
Tufariello, J.M., Chapman, J.R., Kerantzas, C.A., Wong, K.W., Vilcheze, C., et al. (2016) Separable roles
for Mycobacterium tuberculosis ESX-3 effectors in iron acquisition and virulence. Proceedings of the
National Academy of Sciences of the United States of America 113, E348–E357.
Tundup, S., Akhter, Y., Thiagarajan, D. and Hasnain, S.E. (2006) Clusters of PE and PPE genes of Myco-
bacterium tuberculosis are organized in operons: evidence that PE Rv2431c is co-transcribed with
PPE Rv2430c and their gene products interact with each other. FEBS Letters 580, 1285–1293.
Van Der Wel, N., Hava, D., Houben, D., Fluitsma, D., Van Zon, M., et al. (2007) M. tuberculosis and M. lep-
rae translocate from the phagolysosome to the cytosol in myeloid cells. Cell 129, 1287–1298.
Van Ingen, J., Rahim, Z., Mulder, A., Boeree, M.J., Simeone, R., et al. (2012) Characterization of Myco-
bacterium orygis as M. tuberculosis complex subspecies. Emerging Infectious Diseases 18, 653–655.
Vordermeier, H.M., Cockle, P.C., Whelan, A., Rhodes, S., Palmer, N., et al. (1999) Development of diagnos-
tic reagents to differentiate between Mycobacterium bovis BCG vaccination and M. bovis infection in
cattle. Clinical and Diagnostic Laboratory Immunology 6, 675–682.
Wells, A.Q. (1937) Tuberculosis in wild voles. The Lancet 229, 1221.
Wells, A.Q. (1946) The murine type of tubercle bacilli (the vole acid-fast bacillus). MRC Special Report
Series. Medical Research Council, London, UK.
Wiker, H.G., Lyashchenko, K.P., Aksoy, A.M., Lightbody, K.A., Pollock, J.M., et al. (1998) Immunochemical
characterization of the MPB70/80 and MPB83 proteins of Mycobacterium bovis. Infection and Immu-
nity 66, 1445–1452.
Zinn, K., Mcallister, L. and Goodman, C.S. (1988) Sequence analysis and neuronal expression of fasciclin
I in grasshopper and Drosophila. Cell 53, 577–587.
Zumarraga, M., Bigi, F., Alito, A., Romano, M.I. and Cataldi, A. (1999) A 12.7 kb fragment of the Mycobac-
terium tuberculosis genome is not present in Mycobacterium bovis. Microbiology 145(4), 893–897.