Secreted glutamic protease rescues aspartic protease Pep deficiency in Aspergillus fumigatus during growth in acidic protein medium

Sriranganadane, Dev; Reichard, Utz; Salamin, Karine; Fratti, Marina; Jousson, Olivier; Waridel, Patrice; Quadroni, Manfredo; Neuhaus, Jean‐Marc; Monod, Michel

doi:10.1099/mic.0.048603-0

Cited by 14 publications

(10 citation statements)

References 77 publications

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“…5′- ccpA and 3′- ccpA were digested with NotI/XmaI and EcoRI/PacI, respectively, and were ligated end to end into pBluescript II S.K. (+)_ Pac I ( 53 ). The hygromycin-resistance cassette was excised with SfiI from pSK397 and cloned into pBluescript to yield pΔ ccpA .…”

Section: Methodsmentioning

confidence: 99%

Proteome Analysis Reveals the Conidial Surface Protein CcpA Essential for Virulence of the Pathogenic FungusAspergillus fumigatus

Voltersen

Blango

Herrmann

et al. 2018

mBio

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The mammalian immune system relies on recognition of pathogen surface antigens for targeting and clearance. In the absence of immune evasion strategies, pathogen clearance is rapid. In the case of Aspergillus fumigatus, the successful fungus must avoid phagocytosis in the lung to establish invasive infection. In healthy individuals, fungal spores are cleared by immune cells; however, in immunocompromised patients, clearance mechanisms are impaired. Here, using proteome analyses, we identified CcpA as an important fungal spore protein involved in pathogenesis. A. fumigatus lacking CcpA was more susceptible to immune recognition and prompt eradication and, consequently, exhibited drastically attenuated virulence. In infection studies, CcpA was required for virulence in infected immunocompromised mice, suggesting that it could be used as a possible immunotherapeutic or diagnostic target in the future. In summary, our report adds a protein to the list of those known to be critical to the complex fungal spore surface environment and, more importantly, identifies a protein important for conidial immunogenicity during infection.

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Section: Methodsmentioning

confidence: 99%

Proteome Analysis Reveals the Conidial Surface Protein CcpA Essential for Virulence of the Pathogenic FungusAspergillus fumigatus

Voltersen

Blango

Herrmann

et al. 2018

mBio

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“…It is also called the Eqolisin, a name derived from the active-site residues, glutamic acid (E) and glutamine (Q), which activate the nucleophilic water and stabilize the tetrahedral intermediate on the hydrolytic pathway, respectively 30 . Glutamic proteases are quite distinct from previously characterized proteases due to the fact that their distribution is limited to filamentous fungi 30 , because they are essential for fungal growth in protein medium at low pH 31 .…”

Section: Total Aspartic Glutamic Threonine Cysteine Serine Metallomentioning

confidence: 96%

Bioinformatic mapping of a more precise Aspergillus niger degradome

Dong

Yang

Lee

2021

Sci Rep

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Aspergillus niger has the ability to produce a large variety of proteases, which are of particular importance for protein digestion, intracellular protein turnover, cell signaling, flavour development, extracellular matrix remodeling and microbial defense. However, the A. niger degradome (the full repertoire of peptidases encoded by the A. niger genome) available is not accurate and comprehensive. Herein, we have utilized annotations of A. niger proteases in AspGD, JGI, and version 12.2 MEROPS database to compile an index of at least 232 putative proteases that are distributed into the 71 families/subfamilies and 26 clans of the 6 known catalytic classes, which represents ~ 1.64% of the 14,165 putative A. niger protein content. The composition of the A. niger degradome comprises ~ 7.3% aspartic, ~ 2.2% glutamic, ~ 6.0% threonine, ~ 17.7% cysteine, ~ 31.0% serine, and ~ 35.8% metallopeptidases. One hundred and two proteases have been reassigned into the above six classes, while the active sites and/or metal-binding residues of 110 proteases were recharacterized. The probable physiological functions and active site architectures of these peptidases were also investigated. This work provides a more precise overview of the complete degradome of A. niger, which will no doubt constitute a valuable resource and starting point for further experimental studies on the biochemical characterization and physiological roles of these proteases.

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“…Actually, genetic modification has been applied to generate strains with reduced protease activity for increasing the protein production by Aspergillus sp. (Punt et al, 2008; Yoon et al, 2009; Sriranganadane et al, 2011). Recently, several studies with the genetic modification method have been carried out to generate the low-protease-level strains in T. reesei (Zhang et al, 2014; Landowski et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Enhancement of Cellulase Production in Trichoderma reesei via Disruption of Multiple Protease Genes Identified by Comparative Secretomics

et al. 2019

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The filamentous fungus Trichoderma reesei is one of the most studied cellulolytic organisms and the major producer of cellulases for industrial applications. However, undesired degradation of cellulases often happens in culture filtrates and commercial enzyme preparations. Even studies have been reported about describing proteolytic degradation of heterologous proteins in T. reesei, there are few systematic explorations concerning the extracellular proteases responsible for degradation of cellulases. In this study, the cellulase activity was observed to rapidly decrease at late cultivation stages using corn steep liquor (CSL) as the nitrogen source in T. reesei. It was discovered that this decrease may be caused by proteases. To identify the proteases, comparative secretomics was performed to analyze the concomitant proteases during the cellulase production. 12 candidate proteases from the secretome of T. reesei were identified and their encoding genes were individually deleted via homologous recombination. Furthermore, three target proteases (tre81070, tre120998, and tre123234) were simultaneously deleted by one-step genetic transformation. The triple deletion strain ΔP70 showed a 78% decrease in protease activity and a six-fold increase in cellulase activity at late fermentation stages. These results demonstrated the feasibility of improvement of cellulase production by genetically disrupting the potential protease genes to construct the T. reesei strains with low extracellular protease secretion. This dataset also provides an efficient approach for strain improvement by precise genetic engineering combined with “omics” strategy for high-production of industrial enzymes to reduce the cost of lignocellulose bioconversion.

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Secreted glutamic protease rescues aspartic protease Pep deficiency in Aspergillus fumigatus during growth in acidic protein medium

Cited by 14 publications

References 77 publications

Proteome Analysis Reveals the Conidial Surface Protein CcpA Essential for Virulence of the Pathogenic FungusAspergillus fumigatus

Proteome Analysis Reveals the Conidial Surface Protein CcpA Essential for Virulence of the Pathogenic FungusAspergillus fumigatus

Bioinformatic mapping of a more precise Aspergillus niger degradome

Enhancement of Cellulase Production in Trichoderma reesei via Disruption of Multiple Protease Genes Identified by Comparative Secretomics

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