Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M207959200 on January 6, 2003

J. Biol. Chem., Vol. 278, Issue 18, 16423-16432, May 2, 2003
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
278/18/16423    most recent
M207959200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Michell, S. L.
Right arrow Articles by Hewinson, R. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Michell, S. L.
Right arrow Articles by Hewinson, R. G.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

The MPB83 Antigen from Mycobacterium bovis Contains O-Linked Mannose and (1 right-arrow  3)-Mannobiose Moieties*

Stephen L. MichellDagger §, Adam O. WhelanDagger , Paul R. WheelerDagger , Maria Panico, Richard L. Easton, A. Tony Etienne, Stuart M. Haslam, Anne Dell||, Howard R. Morris**, Andrew J. Reason**, Jean Louis HerrmannDagger Dagger , Douglas B. Young§§, and R. Glyn HewinsonDagger

From the Dagger  TB Research Group, Department of Bacterial Diseases, Veterinary Laboratories Agency (Weybridge), New Haw, Addlestone, Surrey KT15 3NB, United Kingdom, the  Department of Biological Sciences, Imperial College of Science Technology and Medicine, London SW7 2AY, United Kingdom, ** M-Scan Mass Spectrometry Research and Training Centre, Silwood Park, Ascot SL5 7PZ, United Kingdom, the Dagger Dagger  Service de Microbiologie, Hopital Saint Louis, 1 Avenue Claude Vellefaux, 75475 Paris, Cedex 10, France, and the §§ Centre for Molecular Microbiology and Infection, Imperial College of Science Technology and Medicine, London SW7 2AY, United Kingdom

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 right-arrow 3) linkage, in contrast to the (1 right-arrow 2) linkage previously observed in antigen MPT32 from M. tuberculosis and the (1 right-arrow 2) and (1 right-arrow 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.

* This work was supported in part by grants from the Department for the Environment Food and Rural Affairs (DEFRA) UK, the Biotechnology and Biological Sciences Research Council, and the Wellcome Trust (to A. D. and H. R. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§  To whom correspondence should be addressed. Current address: DSTL, Porton Down, Salisbury, Wiltshire SP4 0JQ, United Kingdom. Tel.: 44-1980614950; E-mail: slmichell@dstl.gov.uk.

|| Biotechnology and Biological Sciences Research Council Professorial fellow.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 GlycobiologyHome page
M. Lommel and S. Strahl
Protein O-mannosylation: Conserved from bacteria to humans
Glycobiology, August 1, 2009; 19(8): 816 - 828.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
M. J Sartain and J. T Belisle
N-Terminal clustering of the O-glycosylation sites in the Mycobacterium tuberculosis lipoprotein SodC
Glycobiology, January 1, 2009; 19(1): 38 - 51.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
S. Berg, D. Kaur, M. Jackson, and P. J Brennan
The glycosyltransferases of Mycobacterium tuberculosis--roles in the synthesis of arabinogalactan, lipoarabinomannan, and other glycoconjugates
Glycobiology, June 1, 2007; 17(6): 35R - 56R.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Ragas, L. Roussel, G. Puzo, and M. Riviere
The Mycobacterium tuberculosis Cell-surface Glycoprotein Apa as a Potential Adhesin to Colonize Target Cells via the Innate Immune System Pulmonary C-type Lectin Surfactant Protein A
J. Biol. Chem., February 23, 2007; 282(8): 5133 - 5142.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
B. C. VanderVen, J. D. Harder, D. C. Crick, and J. T. Belisle
Export-Mediated Assembly of Mycobacterial Glycoproteins Parallels Eukaryotic Pathways
Science, August 5, 2005; 309(5736): 941 - 943.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
M. Lara, L. Servin-Gonzalez, M. Singh, C. Moreno, I. Cohen, M. Nimtz, and C. Espitia
Expression, Secretion, and Glycosylation of the 45- and 47-kDa Glycoprotein of Mycobacterium tuberculosis in Streptomyces lividans
Appl. Envir. Microbiol., February 1, 2004; 70(2): 679 - 685.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. D. Carr, M. J. Bloemink, E. Dentten, A. O. Whelan, S. V. Gordon, G. Kelly, T. A. Frenkiel, R. G. Hewinson, and R. A. Williamson
Solution Structure of the Mycobacterium tuberculosis Complex Protein MPB70: FROM TUBERCULOSIS PATHOGENESIS TO INHERITED HUMAN CORNEAL DISEASE
J. Biol. Chem., October 31, 2003; 278(44): 43736 - 43743.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement