The MPB83 antigen from Mycobacterium bovis contains O-linked mannose and (1 → 3)-mannobiose moieties

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The MPB83 antigen from Mycobacterium bovis contains O-linked mannose and (1 → 3)-mannobiose moieties. / Michell, Stephen L.; Whelan, Adam O.; Wheeler, Paul R. et al.

In: Journal of Biological Chemistry, Vol. 278, No. 18, 02.05.2003, p. 16423-16432.

Research output: Contribution to journal › Article › peer-review

Harvard

Michell, SL, Whelan, AO, Wheeler, PR, Panico, M, Easton, RL, Etienne, AT, Haslam, SM, Dell, A, Morri, HR, Reason, AJ, Herrmann, JL, Young, DB & Hewinson, RG 2003, 'The MPB83 antigen from Mycobacterium bovis contains O-linked mannose and (1 → 3)-mannobiose moieties', Journal of Biological Chemistry, vol. 278, no. 18, pp. 16423-16432. https://doi.org/10.1074/jbc.M207959200

APA

Michell, S. L., Whelan, A. O., Wheeler, P. R., Panico, M., Easton, R. L., Etienne, A. T., Haslam, S. M., Dell, A., Morri, H. R., Reason, A. J., Herrmann, J. L., Young, D. B., & Hewinson, R. G. (2003). The MPB83 antigen from Mycobacterium bovis contains O-linked mannose and (1 → 3)-mannobiose moieties. Journal of Biological Chemistry, 278(18), 16423-16432. https://doi.org/10.1074/jbc.M207959200

Vancouver

Michell SL, Whelan AO, Wheeler PR, Panico M, Easton RL, Etienne AT et al. The MPB83 antigen from Mycobacterium bovis contains O-linked mannose and (1 → 3)-mannobiose moieties. Journal of Biological Chemistry. 2003 May 2;278(18):16423-16432. doi: 10.1074/jbc.M207959200

Author

Michell, Stephen L. ; Whelan, Adam O. ; Wheeler, Paul R. et al. / The MPB83 antigen from Mycobacterium bovis contains O-linked mannose and (1 → 3)-mannobiose moieties. In: Journal of Biological Chemistry. 2003 ; Vol. 278, No. 18. pp. 16423-16432.

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@article{c2b7dc6cfcfe47cfbd5b2e8456dc6553,
title = "The MPB83 antigen from Mycobacterium bovis contains O-linked mannose and (1 → 3)-mannobiose moieties",
abstract = "Mycobacterium tuberculosis and Mycobacterium bovis, the causative agents of human and bovine tuberculosis, have been reported to express a range of surface and secreted glycoproteins, although only one of these has been subjected to detailed structural analysis. We describe the use of a genetic system, in conjunction with lectin binding, to characterize the points of attachment of carbohydrate moieties to the polypeptide backbone of a second mycobacterial glycoprotein, antigen MPB83 from M. bovis. Biochemical and structural analysis of the native MPB83 protein and derived peptides demonstrated the presence of 3 mannose units attached to two threonine residues. Mannose residues were joined by a (1 → 3) linkage, in contrast to the (1 → 2) linkage previously observed in antigen MPT32 from M. tuberculosis and the (1 → 2) and (1 → 6) linkages in other mycobacterial glycolipids and polysaccharides. The identification of glycosylated antigens within the M. tuberculosis complex raises the possibility that the carbohydrate moiety of these glycoproteins might be involved in pathogenesis, either by interaction with mannose receptors on host cells, or as targets or modulators of the cell-mediated immune response. Given such a possibility characterization of mycobacterial glycoproteins is a step toward understanding their functional role and elucidating the mechanisms of mycobacterial glycosylation.",
author = "Michell, {Stephen L.} and Whelan, {Adam O.} and Wheeler, {Paul R.} and Maria Panico and Easton, {Richard L.} and Etienne, {A. Tony} and Haslam, {Stuart M.} and Anne Dell and Morri, {Howard R.} and Reason, {Andrew J.} and Herrmann, {Jean Louis} and Young, {Douglas B.} and Hewinson, {R. Glyn}",
year = "2003",
month = may,
day = "2",
doi = "10.1074/jbc.M207959200",
language = "English",
volume = "278",
pages = "16423--16432",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology",
number = "18",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - The MPB83 antigen from Mycobacterium bovis contains O-linked mannose and (1 → 3)-mannobiose moieties

AU - Michell, Stephen L.

AU - Whelan, Adam O.

AU - Wheeler, Paul R.

AU - Panico, Maria

AU - Easton, Richard L.

AU - Etienne, A. Tony

AU - Haslam, Stuart M.

AU - Dell, Anne

AU - Morri, Howard R.

AU - Reason, Andrew J.

AU - Herrmann, Jean Louis

AU - Young, Douglas B.

AU - Hewinson, R. Glyn

PY - 2003/5/2

Y1 - 2003/5/2

N2 - Mycobacterium tuberculosis and Mycobacterium bovis, the causative agents of human and bovine tuberculosis, have been reported to express a range of surface and secreted glycoproteins, although only one of these has been subjected to detailed structural analysis. We describe the use of a genetic system, in conjunction with lectin binding, to characterize the points of attachment of carbohydrate moieties to the polypeptide backbone of a second mycobacterial glycoprotein, antigen MPB83 from M. bovis. Biochemical and structural analysis of the native MPB83 protein and derived peptides demonstrated the presence of 3 mannose units attached to two threonine residues. Mannose residues were joined by a (1 → 3) linkage, in contrast to the (1 → 2) linkage previously observed in antigen MPT32 from M. tuberculosis and the (1 → 2) and (1 → 6) linkages in other mycobacterial glycolipids and polysaccharides. The identification of glycosylated antigens within the M. tuberculosis complex raises the possibility that the carbohydrate moiety of these glycoproteins might be involved in pathogenesis, either by interaction with mannose receptors on host cells, or as targets or modulators of the cell-mediated immune response. Given such a possibility characterization of mycobacterial glycoproteins is a step toward understanding their functional role and elucidating the mechanisms of mycobacterial glycosylation.

AB - Mycobacterium tuberculosis and Mycobacterium bovis, the causative agents of human and bovine tuberculosis, have been reported to express a range of surface and secreted glycoproteins, although only one of these has been subjected to detailed structural analysis. We describe the use of a genetic system, in conjunction with lectin binding, to characterize the points of attachment of carbohydrate moieties to the polypeptide backbone of a second mycobacterial glycoprotein, antigen MPB83 from M. bovis. Biochemical and structural analysis of the native MPB83 protein and derived peptides demonstrated the presence of 3 mannose units attached to two threonine residues. Mannose residues were joined by a (1 → 3) linkage, in contrast to the (1 → 2) linkage previously observed in antigen MPT32 from M. tuberculosis and the (1 → 2) and (1 → 6) linkages in other mycobacterial glycolipids and polysaccharides. The identification of glycosylated antigens within the M. tuberculosis complex raises the possibility that the carbohydrate moiety of these glycoproteins might be involved in pathogenesis, either by interaction with mannose receptors on host cells, or as targets or modulators of the cell-mediated immune response. Given such a possibility characterization of mycobacterial glycoproteins is a step toward understanding their functional role and elucidating the mechanisms of mycobacterial glycosylation.

UR - http://www.scopus.com/inward/record.url?scp=0037507310&partnerID=8YFLogxK

U2 - 10.1074/jbc.M207959200

DO - 10.1074/jbc.M207959200

M3 - Article

C2 - 12517764

AN - SCOPUS:0037507310

VL - 278

SP - 16423

EP - 16432

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 18

ER -

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