Proteomic analysis of rutin-induced secreted proteins from Aspergillus flavus

Medina, Martha L.; Kiernan, Urban A.; Francisco, Wilson A.

doi:10.1016/j.fgb.2003.11.014

Cited by 90 publications

(99 citation statements)

References 22 publications

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“…Indeed, 28 of the 50 proteins identified in our study have not previously been reported in A. fumigatus. The percentage sequence coverage range (9.4-50.5%) obtained here for MALDI-MS identification of A. fumigatus proteins is consistent with that recently reported by Medina et al for the identification of rutininduced secreted proteins from A. flavus (7-43% sequence coverage) and Grinyer et al who mapped mitochondrial proteins from Trichoderma harizium (8-54% sequence coverage) [3,5].…”

Section: Discussionsupporting

confidence: 91%

“…A number of identified proteins have been shown to be located in the cell wall of other fungi, included HSP90 and HSP70 in C. albicans [25], enolase and glyceraldehyde-3-phosphate dehydrogenase [26]. Others, such as catalase, ATP synthase (subunit b), and phosphoglycerate mutase were recently shown to be secreted by A. flavus [5]. Overall, it is clear that a more systematic and focused approach is required to further elucidate the functional rationale governing the unexpected localisation, and dynamic nature, of these fungal proteins which were previously thought to be predominantly of cytoplasmic origin.…”

Section: Discussionmentioning

confidence: 99%

“…Until recently, however, little information was available with respect to either the technical requirements for protein extraction or the proteome content of most Aspergillus species. However, dissection of the secreted proteome (secretome) of Aspergillus flavus has demonstrated the ability of this organism to adapt to altered conditions such as the presence of various carbon sources (e.g., rutin) [5].…”

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confidence: 99%

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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

Carberry

Neville

Kavanagh

et al. 2006

Biochemical and Biophysical Research Communications

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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 (eEF1Bc), termed ElfA and B have been identified and phylogenetically confirmed to belong to the eEF1Bc class of GST-like proteins. One of these proteins (ElfA) 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 lmol/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.

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Section: Discussionsupporting

confidence: 91%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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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

Carberry

Neville

Kavanagh

et al. 2006

Biochemical and Biophysical Research Communications

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“…In fungi this is often identifying what proteins are secreted, as fungi are important degraders of biomass (Medina et al 2005, Medina et al 2004, Vanden Wymelenberg et al 2005) have symbiotic relationships with roots of agriculturally important plants (Bestel-Corre et al 2004) and protect plants from other soil-borne microbes (Grinyer et al 2005, Grinyer et al 2004). The majority of these studies are again targeting biological niches that are dominated by fungi, and are expected to involve fungal-specific genes.…”

Section: Annotation In Fungi With Experimental Datamentioning

confidence: 99%

Fungal Genomic Annotation

Grigoriev¹,

Martínez²,

Salamov³

2006

Applied Mycology and Biotechnology

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(admar@lanl.gov).Sequencing technology in the last decade has advanced at an incredible pace. Currently there are hundreds of microbial genomes available with more still to come. Automated genome annotation aims to analyze this amount of sequence data in a high-throughput fashion and help researches to understand the biology of these organisms. Manual curation of automatically annotated genomes validates the predictions and set up 'gold' standards for improving the methodologies used. Here we review the methods and tools used for annotation of fungal genomes in different genome sequencing centers.

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“…Descriptive proteomics has also been carried out on Aspergillus fumigatus 21 and Aspergillus flavus. 22 Many enzymes have been identified and functionally classified: fungal proteolytic and peptidolytic enzymes, serine/threonine kinases and further molecules important for carbohydrate transport and metabolism, electron/proton transfer, chitin and chitosan metabolism or melanine synthesis. 23 Some fungal enzymes (proteases, elastases, phospholipases, etc.)…”

Section: Role Of Mass Spectrometry In Fungal Diagnosticsmentioning

confidence: 99%

Nonribosomal cyclic peptides: specific markers of fungal infections

Jegorov¹,

Hajdúch

Šulc

et al. 2006

J. Mass Spectrom.

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Some cyclic peptides and depsipeptides are synthesized in microorganisms by large multienzymes called nonribosomal peptide synthetases. The structures of peptide products originating in this way are complex and diverse and are microorganism-specific. This work proposes the use of fungal cyclic peptides and depsipeptides as extremely specific markers of fungal infections. Since a reliable molecular tool for diagnosing fungal infections at an early stage is still missing, we present mass spectrometry as a new, modern, broadband (with respect to fungal strain) and specific tool for clinical mycologists. More than 40 different fungal species can be rapidly characterized according to specific families of cyclic peptides, and in some cases, a particular fungal strain can be identified on the basis of its cyclopeptide profile. This paper is also aimed at initiating discussion on the biological role of these secondary metabolites, especially of those synthesized by medically important strains. Proven cytotoxic, anti-inflammatory or immunosuppressive activities of some cyclic peptides indicate that these molecules may contribute to the synergistic array of fungal virulence factors and support microbial invasion during fungal infection. In addition to an overview on recent mass spectrometric protocols for cyclic peptide sequencing, the structures of new peptides from Paecilomyces and Pseudallescheria are presented.

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Proteomic analysis of rutin-induced secreted proteins from Aspergillus flavus

Cited by 90 publications

References 22 publications

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

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

Fungal Genomic Annotation

Nonribosomal cyclic peptides: specific markers of fungal infections

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