Peer-Reviewed Journal Details
Mandatory Fields
Carberry, S;Neville, CM;Kavanagh, KA;Doyle, S
2006
March
Biochemical and Biophysical Research Communications
Analysis of major intracellular proteins of Aspergillus fumigatus by MALDI mass spectrometry: Identification and characterisation of an elongation factor 1B protein with glutathione transferase activity
Published
52 ()
Optional Fields
ALLERGIC BRONCHOPULMONARY ASPERGILLOSIS TRYPANOTHIONE S-TRANSFERASE CELL-WALL SACCHAROMYCES-CEREVISIAE INVASIVE ASPERGILLOSIS SECRETED PROTEINS ESCHERICHIA-COLI CANDIDA-ALBICANS EXPRESSION ELECTROPHORESIS
341
1096
1104
Aspergillus fumigatus is a recognised human pathogen, especially in immunocompromised individuals. The availability of the annotated A. fumigatus genome sequence will significantly accelerate our understanding of this organism. However, limited information is available with respect to the A. fumigatus proteome. Here, both a direct proteomic approach (2D-PAGE and MALDI-MS) and a sub-proteomic strategy involving initial glutathione affinity chromatography have been deployed to identify 54 proteins from A. fumigatus primarily involved in energy metabolism and protein biosynthesis. Furthermore, two novel eukaryotic elongation factor proteins (eEF1B gamma), termed E1fA and B have been identified and phylogenetically confirmed to belong to the eEF1B gamma class of GST-like proteins. One of these proteins (E1fA) has been purified to homogeneity, identified as a monomeric enzyme (molecular mass = 20 kDa; pI = 5.9 and 6.5), and found to exhibit glutathione transferase activity specific activities (mean standard deviation, n = 3) of 3.13 +/- 0.27 and 3.43 +/- 1.0 mu mol/min/mg, using CDNB and ethacrynic acid, respectively. Overall, these data highlight the importance of new approaches to dissect the proteome of, and elucidate novel functions within, A. fumigatus. (c) 2006 Elsevier Inc. All rights reserved.
SAN DIEGO
0006-291X
10.1016/j.bbrc.2006.01.078
Grant Details