Mycolyltransferase from Mycobacterium leprae Excludes Mycolate-containing Glycolipid Substrates

Journal of Biochemistry

Volumn 146, Issue 5, 2009, Pages 659-665

  Nakao, Hitomi ^a,b   Matsunaga, Isamu ^a,b   Morita, Daisuke ^a,b   Aboshi, Takako ^a   Harada, Toshiyuki ^a   Nakagawa, Yoshiaki ^a   Mori, Naoki ^a   Sugita, Masahiko ^a,b  

^a KYOTO UNIVERSITY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

Glucose monomycolate; Glycolipid; Mycobacterium leprae; Mycolyltransferase; Trehalose dimycolate

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; CORD FACTOR; FBPA PROTEIN; GLUCOSE MONOMYCOLATE; GLYCOLIPID; LEUCINE; MYCOLYLTRANSFERASE; TRANSFERASE; UNCLASSIFIED DRUG;

ARTICLE; DOWN REGULATION; ENZYME ACTIVITY; ENZYME SUBSTRATE; MOLECULAR MODEL; MUTATIONAL ANALYSIS; MYCOBACTERIUM AVIUM; MYCOBACTERIUM LEPRAE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PROTEIN FUNCTION; PROTEIN TRANSPORT;

ACYLTRANSFERASES; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; FATTY ACIDS; GLYCOLIPIDS; KINETICS; LEUCINE; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; MYCOBACTERIUM LEPRAE; MYCOLIC ACIDS; PROTEIN BINDING; SUBSTRATE SPECIFICITY;

CORYNEBACTERINEAE; MYCOBACTERIUM AVIUM; MYCOBACTERIUM LEPRAE; MYCOBACTERIUM TUBERCULOSIS;

EID: 70449686288     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvp113     Document Type: Article

References (19)

1. Brennan, P.J. (2003) Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis. Tuberculosis 83, 91-97
2. Ryll, R., Kumazawa, Y., and Yano, I. (2001) Immunological properties of trehalose dimycolate (cord factor) and other mycolic acid-containing glycolipids-a review. Microbiol. Immunol. 45, 801-811
3. Otsuka, A., Matsunaga, I., Komori, T., Tomita, K., Toda, Y., Manabe, T., Miyachi, Y., and Sugita, M. (2008) Trehalose dimycolate elicits eosinophilic skin hypersensitivity in mycobacteria-infected guinea pigs. J. Immunol. 181, 8528-8533
4. Matsunaga, I., Naka, T., Talekar, R.S., McConnell, M.J., Katoh, K., Nakao, H., Otsuka, A., Behar, S.M., Yano, I., Moody, D.B., and Sugita, M. (2008) Mycolyltransferasemediated glycolipid exchange in Mycobacteria. J. Biol. Chem. 283, 28835-28841
5. Belisle, J.T., Vissa, V.D., Sievert, T., Takayama, K., Brennan, P.J., and Besra, G.S. (1997) Role of the major antigen of Mycobacterium tuberculosis in cell wall biogenesis. Science 276, 1420-1422
6. Dhariwal, K.R., Yang, Y.M., Fales, H.M., and Goren, M.B. (1987) Detection of trehalose monomycolate in Mycobacterium leprae grown in armadillo tissues. J. Gen. Microbiol. 133, 201-209
7. Cole, S.T., Eiglmeier, K., Parkhill, J., James, K.D., Thomson, N.R., Wheeler, P.R., Honore, N., Garnier, T., Churcher, C., Harris, D., Mungall, K., Basham, D., Brown, D., Chillingworth, T., Connor, R., Davies, R.M., Devlin, K., Duthoy, S., Feltwell, T., Fraser, A., Hamlin, N., Holroyd, S., Hornsby, T., Jagels, K., Lacroix, C., Maclean, J., Moule, S., Murphy, L., Oliver, K., Quail, M.A., Rajandream, M.A., Rutherford, K.M., Rutter, S., Seeger, K., Simon, S., Simmonds, M., Skelton, J., Squares, R., Squares, S., Stevens, K., Taylor, K., Whitehead, S., Woodward, J.R., and Barrell, B.G. (2001) Massive gene decay in the leprosy bacillus. Nature 409, 1007-1011
8. Maeda, S., Matsuoka, M., Nakata, N., Kai, M., Maeda, Y., Hashimoto, K., Kimura, H., Kobayashi, K., and Kashiwabara, Y. (2001) Multidrug resistant Mycobacterium leprae from patients with leprosy. Antimicrob. Agents Chemother. 45, 3635-3639
9. Raku, T., Kitagawa, M., Shimakawa, H., and Tokiwa, Y. (2003) Enzymatic synthesis of trehalose esters having lipophilicity. J. Biotechnol. 100, 203-208
10. Kremer, L., Maughan, W.N., Wilson, R.A., Dover, L.G., and Besra, G.S. (2002) The M. tuberculosis antigen 85 complex and mycolyltransferase activity. Lett. Appl. Microbiol. 34, 233-237
11. Matsunaga, I., Komori, T., Ochi, A., Mori, N., and Sugita, M. (2008) Identification of antibody responses to the serotype-nonspecific molecular species of glycopeptidolipids in Mycobacterium avium infection. Biochem. Biophys. Res. Commun. 377, 165-169
12. Ogata, K. and Umeyama, H. (2000) An automatic homology modeling method consisting of database searches and simulated annealing. J. Mol. Graph. Model 18, 258-272 (Pubitemid 30938434)
13. Wheelock, C.E., Nakagawa, Y., Harada, T., Oikawa, N., Akamatsu, M., Smagghe, G., Stefanou, D., Iatrou, K., and Swevers, L. (2006) High-throughput screening of ecdysone agonists using a reporter gene assay followed by 3-D QSAR analysis of the molting hormonal activity. Bioorg. Med. Chem. 14, 1143-1159
14. Anderson, D.H., Harth, G., Horwitz, M.A., and Eisenberg, D. (2001) An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30 kDa major secretory protein (Antigen 85B), a mycolyl transferase. J. Mol. Biol. 307, 671-681
15. Ronning, D.R., Klabunde, T., Besra, G.S., Vissa, V.D., Belisle, J.T., and Sacchettini, J.C. (2000) Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines. Nat. Struct. Biol. 7, 141-146
16. Ronning, D.R., Vissa, V., Besra, G.S., Belisle, J.T., and Sacchettini, J.C. (2004) Mycobacterium tuberculosis antigen 85A and 85C structures confirm binding orientation and conserved substrate specificity. J. Biol. Chem. 279, 36771-36777
17. Moody, D.B., Reinhold, B.B., Guy, M.R., Beckman, E.M., Frederique, D.E., Furlong, S.T., Ye, S., Reinhold, V.N., Sieling, P.A., Modlin, R.L., Besra, G.S., and Porcelli, S.A. (1997) Structural requirements for glycolipid antigen recognition by CD1b- restricted T cells. Science 278, 283-286
18. Stenger, S., Mazzaccaro, R.J., Uyemura, K., Cho, S., Barnes, P.F., Rosat, J.P., Sette, A., Brenner, M.B., Porcelli, S.A., Bloom, B.R., and Modlin, R.L. (1997) Differential effects of cytolytic T cell subsets on intracellular infection. Science 276, 1684-1687
19. Williams, D.L., Torrero, M., Wheeler, P.R., Truman, R.W., Yoder, M., Morrison, N., Bishai, W.R., and Gillis, T.P. (2004) Biological implications of Mycobacterium leprae gene expression during infection. J. Mol. Microbiol. Biotechnol. 8, 58-72