Mycobacterium tuberculosis glycoproteomics based on ConA-lectin affinity capture of mannosylated proteins

Margarita González-Zamorano; Guillermo Mendoza-Hernández; Wendy Xolalpa; Cristina Parada; Antonio J Vallecillo; Fabiana Bigi; Clara Espitia

doi:10.1021/pr800756a

Mycobacterium tuberculosis glycoproteomics based on ConA-lectin affinity capture of mannosylated proteins

J Proteome Res. 2009 Feb;8(2):721-33. doi: 10.1021/pr800756a.

Authors

Margarita González-Zamorano¹, Guillermo Mendoza-Hernández, Wendy Xolalpa, Cristina Parada, Antonio J Vallecillo, Fabiana Bigi, Clara Espitia

Affiliation

¹ Departamento de Inmunologia, Instituto de Investigaciones Biomedicas, Universidad Nacional Autonoma de Mexico, Mexico.

PMID: 19196185
DOI: 10.1021/pr800756a

Abstract

A Mycobacterium tuberculosis culture filtrate enriched with mannose-containing proteins was resolved by 2-DE gel. After ConA ligand blotting, 41 proteins were identified by mass spectrometry as putative glycoproteins with 34 of them new probably mannosylated proteins. These results contribute to the construction of the ConA affinity glycoprotein database of M. tuberculosis, and provide useful information for understanding the biological role of glycoproteins in mycobacteria.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins* / chemistry
Bacterial Proteins* / metabolism
Computational Biology
Concanavalin A / metabolism*
Glycoproteins* / chemistry
Glycoproteins* / metabolism
Humans
Mannose / chemistry*
Mass Spectrometry
Molecular Sequence Data
Mycobacterium tuberculosis* / chemistry
Mycobacterium tuberculosis* / metabolism
Proteomics / methods*

Substances

Bacterial Proteins
Glycoproteins
Concanavalin A
Mannose