O-linked glycosylation sites profiling in Mycobacterium tuberculosis culture filtrate proteins
Abstract
Mycobacterium tuberculosis (Mtb) causes tuberculosis, one of the leading causes of fatal infectious diseases worldwide. Cell–cell recognition between the pathogen Mtb and its host is mediated in part by glycosylated proteins. So far, glycoproteins in Mtb are understudied and for only very few glycoproteins glycosylation sites have been described, e.g., alanine and proline rich secreted protein apa, superoxide dismutase SODC, lipoprotein lpqH and MPB83/MPT83. In this study, glycosylated proteins in Mtb culture filtrate were investigated using liquid chromatography–mass spectrometry approaches and bioinformatic analyses. To validate the presence of glycoproteins, several strategies were pursued including collision induced dissociation, high energy collision dissociation and electron transfer dissociation techniques, and bioinformatics analyses involving a neutral loss search for glycosylated moieties. After extensive data curation, we report glycosylation sites for thirteen Mtb glycoproteins using a combination of mass spectrometry techniques on a dataset collected from culture filtrate proteins. This is the first glycoproteomics study identifying glycosylation sites on mycobacterial culture filtrate proteins (CFP) on a global scale. Biological significance In this study, glycosylation sites in Mtb were characterized by collision-induced dissociation, electron-transfer dissociation and high energy collision dissociation techniques. The identification of glycosylation sites is important for our understanding of the physiology and pathophysiology of Mtb. Glycoproteins are often responsible for protein–protein interactions between host and pathogen and thus represent interesting targets for vaccine development. In addition, our strategy is not limited to Mtb, but could be extended to other organisms.
Additional Information
© 2013 Elsevier B.V. Available online 20 May 2013. The Proteome Exploration Laboratory is funded by the Gordon and Betty Moore Foundation through Grant GBMF775, the Beckman Institute and the NIH award SRR029594A.Attached Files
Accepted Version - nihms483027.pdf
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Additional details
- PMCID
- PMC3806883
- Eprint ID
- 79270
- Resolver ID
- CaltechAUTHORS:20170721-125354271
- GBMF775
- Gordon and Betty Moore Foundation
- Caltech Beckman Institute
- SRR029594A
- NIH
- Created
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2017-07-21Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field