Molecular characterization of a cell wall-associated ß(1-3)endoglucanase of<i>Aspergillus fumigatus</i>

Mouyna, Isabelle; Sarfati, J.; Recco, P.; Fontaine, Thierry; Henrissat, Bernard; Latgé, Jean‐Paul

doi:10.1080/mmy.40.5.455.464

Cited by 39 publications

(7 citation statements)

References 42 publications

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“…The enzyme recognized at least five glucose units linked by a β-1,3-bond. The gene encoding this activity has been cloned and named ENGL1 (AFUA_1G04260) (Mouyna et al, 2002). AfEngl1p has an N -terminal signal peptide and a large GH81 domain responsible for the endo-1,3-glucanase activity (Figure 3C).…”

Section: Are β–Glucanase Involved In the Cell Wall Modification?mentioning

confidence: 99%

β-1,3-glucan modifying enzymes in Aspergillus fumigatus

Mouyna¹,

Hartl²,

Latgé³

2013

Front. Microbiol.

114

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In Aspergillus fumigatus like in other filamentous ascomycetes, β-1,3-glucan constitutes a prominent cell wall component being responsible for rigidity of the cell wall structure. In filamentous fungi, softening of the cell wall is absolutely required during conidial germination and hyphal branching. Because of the central structure of β-1,3-glucans, it is expected that β-1,3-glucanases play a major role in cell wall softening. Based on in silico and experimental data, this review gives an overview of β-1,3-glucan modifying enzymes in A. fumigatus genome and their putative role during morphogenesis.

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Section: Are β–Glucanase Involved In the Cell Wall Modification?mentioning

confidence: 99%

β-1,3-glucan modifying enzymes in Aspergillus fumigatus

Mouyna¹,

Hartl²,

Latgé³

2013

Front. Microbiol.

114

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“…2). Two glutamic acid residues have been proposed as putative nucleophiles of the catalytically active site of the endoglucanase of A. fumigatus (43). Substituting these conserved residues for glutamine in the soybean GBP resulted in the GBP-Gln 494 -Gln 498 variant.…”

Section: Table I Comparison Of Specific Binding and Biological Activimentioning

confidence: 99%

An Ancient Enzyme Domain Hidden in the Putative β-Glucan Elicitor Receptor of Soybean May Play an Active Part in the Perception of Pathogen-associated Molecular Patterns during Broad Host Resistance

Fliegmann

Mithöfer

Wanner

et al. 2004

Journal of Biological Chemistry

148

115

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A successful defense against potential pathogens requires that a host organism is able to discriminate between self and nonself structures. Soybean (Glycine max L.) exploits a specific molecular pattern, a 1,6-␤-linked and 1,3-␤-branched heptaglucoside (HG), present in cell walls of the oomycetal pathogen Phytophthora sojae, as a signal compound eliciting the onset of defense reactions. The specific and high affinity HG-binding site is contained in the ␤-glucan-binding protein (GBP), which in turn is part of a proposed receptor complex. The ability to perceive and respond to Phytophthora cell wall-derived ␤-glucan elicitors is exclusive to plants that belong to the Fabaceae. However, we propose that the presence of the GBP is essential, but not sufficient for ␤-glucan elicitor-dependent disease resistance because genes encoding GBP-related proteins can be retrieved from many plant species. Furthermore, we show that the GBP is composed of two different carbohydrateactive protein domains, one containing the ␤-glucanbinding site, and the other related to glucan endoglucosidases of fungal origin. The glucan hydrolase displays most likely an endo-specific mode of action, cleaving only 1,3-␤-D-glucosidic linkages of oligoglucosides consisting of at least four moieties. Thus, the intrinsic endo-1,3-␤-glucanase activity of the GBP is perfectly suited during initial contact with Phytophthora to release oligoglucoside fragments enriched in motifs that constitute ligands for the high affinity binding site present in the same protein. The concept of innate immunity in plants receives substantial support by this highly sophisticated system using ancient enzyme modules as an active part of the recognition mechanism.

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“…BLAST analysis identified 10 potential endo β-1,3-glucanases in the A. fumigatus genome based on homologies with different fungal and bacterial glucanases (Gastebois et al, 2009), and one of them has already been characterized (Mouyna et al, 2002). Two of the remaining proteins feature a GPI modification site predicted by the big-PI Fungal Predictor (Eisenhaber et al, 2004): AFUA_3g03080 and AFUA_2g14360 ( ENG2 ).…”

Section: Resultsmentioning

confidence: 99%

“…A. fumigatus features only one ortholog belonging to the family GH81 (Eng1) which has been described previously. The Afeng1 mutant like the Afeng2 strain did not exhibit a growth phenotype (Mouyna et al, 2002). The endo β-1,3-glucanase of the family GH16 which is found in S. pombe on the contrary has not been characterized so far.…”

Section: Discussionmentioning

confidence: 99%

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Characterization of the GPI-anchored endo β-1,3-glucanase Eng2 of Aspergillus fumigatus

Hartl

Gastebois

Aimanianda

et al. 2011

Fungal Genetics and Biology

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A GPI-anchored endo β-1,3-glucanase of Aspergillusfumigatus was characterized. The enzyme encoded by ENG2 (AFUA_2g14360) belongs to the glycoside hydrolase family 16 (GH16). The activity was characterized using a recombinant protein produced by Pichiapastoris. The recombinant enzyme preferentially acts on soluble β-1,3-glucans. Enzymatic analysis of the endoglucanase activity using Carboxymethyl-Curdlan-Remazol Brilliant Blue (CM-Curdlan-RBB) as a substrate revealed a wide temperature optimum of 24–40 °C, a pH optimum of 5.0–6.5 and a Km of 0.8 mg ml−1. HPAEC analysis of the products formed by Eng2 when acting on different oligo-β-1,3-glucans confirmed the predicted endoglucanase activity and also revealed a transferase activity for oligosaccharides of a low degree of polymerization. The growth phenotype of the Afeng2 mutant was identical to that of the wt strain.

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Molecular characterization of a cell wall-associated ß(1-3)endoglucanase ofAspergillus fumigatus

Cited by 39 publications

References 42 publications

β-1,3-glucan modifying enzymes in Aspergillus fumigatus

β-1,3-glucan modifying enzymes in Aspergillus fumigatus

An Ancient Enzyme Domain Hidden in the Putative β-Glucan Elicitor Receptor of Soybean May Play an Active Part in the Perception of Pathogen-associated Molecular Patterns during Broad Host Resistance

Characterization of the GPI-anchored endo β-1,3-glucanase Eng2 of Aspergillus fumigatus

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