Reichard, Utz

[["dc.bibliographiccitation.firstpage","79"],["dc.bibliographiccitation.journal","Gene"],["dc.bibliographiccitation.lastpage","88"],["dc.bibliographiccitation.volume","339"],["dc.contributor.author","Jousson, Olivier"],["dc.contributor.author","Lechenne, B."],["dc.contributor.author","Bontems, O."],["dc.contributor.author","Mignon, B."],["dc.contributor.author","Reichard, Utz"],["dc.contributor.author","Barblan, J."],["dc.contributor.author","Quadroni, Manfredo"],["dc.contributor.author","Monod, Michel"],["dc.date.accessioned","2018-11-07T10:45:34Z"],["dc.date.available","2018-11-07T10:45:34Z"],["dc.date.issued","2004"],["dc.description.abstract","Secreted proteases constitute potential virulence factors of dermatophytes. A total of seven genes encoding putative serine proteases of the subtilisin family (SUB) were isolated in Trichophyton rubrum. Based on sequence data and intron-exon structure, a phylogenetic analysis of subtilisins from T rubrum and other fungi revealed a presumed ancestral lineage comprising T rubrum SUB2 and Aspergillus SUBs. All other SUBs (SUB1, SUB3-7) are dermatophyte-specific and have apparently emerged more recently, through successive gene duplication events. We showed that two subtilisins, Sub3 and Sub4, were detected in culture supernatants of T rubrum grown in a medium containing soy protein as a sole nitrogen source. Both recombinant enzymes produced in Pichia pastoris are highly active on keratin azure suggesting that these proteases play an important role in invasion of keratinised tissues by the fungus. The set of deduced amino acid sequences of T rubrum SUB ORFs allowed the identification of orthologous Subs secreted by other dermatophyte species using proteolysis and mass spectrometry. (C) 2004 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.gene.2004.06.024"],["dc.identifier.isi","000224173200009"],["dc.identifier.pmid","15363848"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/47530"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0378-1119"],["dc.title","Secreted subtilisin gene family in Trichophyton rubrum"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","87"],["dc.bibliographiccitation.lastpage","106"],["dc.contributor.author","Monod, Michel"],["dc.contributor.author","Jousson, Olivier"],["dc.contributor.author","Reichard, Utz"],["dc.contributor.editor","Latgé, Jean-Paul"],["dc.contributor.editor","Steinbach, William J."],["dc.date.accessioned","2021-12-08T12:28:05Z"],["dc.date.available","2021-12-08T12:28:05Z"],["dc.date.issued","2008"],["dc.identifier.doi","10.1128/9781555815523.ch8"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/95549"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-476"],["dc.publisher","ASM Press"],["dc.publisher.place","Washington, DC, USA"],["dc.relation.eisbn","9781683671381"],["dc.relation.eisbn","9781555815523"],["dc.relation.isbn","9781555814380"],["dc.relation.ispartof","Aspergillus fumigatus\n and Aspergillosis"],["dc.title","Aspergillus fumigatus Secreted Proteases"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1541"],["dc.bibliographiccitation.journal","Microbiology"],["dc.bibliographiccitation.lastpage","1550"],["dc.bibliographiccitation.volume","157"],["dc.contributor.author","Sriranganadane, Dev"],["dc.contributor.author","Reichard, Utz"],["dc.contributor.author","Salamin, Karine"],["dc.contributor.author","Fratti, Marina"],["dc.contributor.author","Jousson, Olivier"],["dc.contributor.author","Waridel, Patrice"],["dc.contributor.author","Quadroni, Manfredo"],["dc.contributor.author","Neuhaus, Jean-Marc"],["dc.contributor.author","Monod, Michel"],["dc.date.accessioned","2018-11-07T08:56:19Z"],["dc.date.available","2018-11-07T08:56:19Z"],["dc.date.issued","2011"],["dc.description.abstract","In an acidic protein medium Aspergillus fumigatus secretes an aspartic endoprotease (Pep) as well as tripeptidyl-peptidases, a prolyl-peptidase and carboxypeptidases. In addition, LC-MS/MS revealed a novel glutamic protease, AfuGprA, homologous to Aspergillus niger aspergillopepsin II. The importance of AfuGprA in protein digestion was evaluated by deletion of its encoding gene in A. fumigatus wild-type D141 and in a pepA mutant. Either A. fumigatus Pep or AfuGprA was shown to be necessary for fungal growth in protein medium at low pH. Exoproteolytic activity is therefore not sufficient for complete protein hydrolysis and fungal growth in a medium containing proteins as the sole nitrogen source. Pep and AfuGprA constitute a pair of endoproteases active at low pH, in analogy to A. fumigatus alkaline protease (Alp) and metalloprotease I (Mep), where at least one of these enzymes is necessary for fungal growth in protein medium at neutral pH. Heterologous expression of AfuGprA in Pichia pastoris showed that the enzyme is synthesized as a preproprotein and that the propeptide is removed through an autoproteolytic reaction at low pH to generate the mature protease. In contrast to A. niger aspergillopepsin II, AfuGprA is a single-chain protein and is structurally more similar to G1 proteases characterized in other non-Aspergillus fungi."],["dc.description.sponsorship","Swiss National Foundation for Scientific Research [320030-1179641]"],["dc.identifier.doi","10.1099/mic.0.048603-0"],["dc.identifier.isi","000291179900029"],["dc.identifier.pmid","21349972"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23119"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Soc General Microbiology"],["dc.relation.issn","1350-0872"],["dc.title","Secreted glutamic protease rescues aspartic protease Pep deficiency in Aspergillus fumigatus during growth in acidic protein medium"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","573"],["dc.bibliographiccitation.lastpage","606"],["dc.contributor.author","Monod, Michel"],["dc.contributor.author","Staib, Peter"],["dc.contributor.author","Reichard, Utz"],["dc.contributor.author","Jousson, Olivier"],["dc.contributor.editor","Ghosh, Arun K."],["dc.date.accessioned","2021-12-08T12:28:58Z"],["dc.date.available","2021-12-08T12:28:58Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1002/9783527630943.ch20"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/95910"],["dc.notes.intern","DOI-Import GROB-476"],["dc.publisher","Wiley-VCH Verlag GmbH & Co. KGaA"],["dc.publisher.place","Weinheim, Germany"],["dc.relation.eisbn","978-3-527-63094-3"],["dc.relation.isbn","978-3-527-31811-7"],["dc.relation.ispartof","Methods and Principles in Medicinal Chemistry"],["dc.relation.ispartof","Aspartic Acid Proteases as Therapeutic Targets : GHOSH:PROTEASES DRUG TARG O-BK"],["dc.title","Fungal Aspartic Proteases as Possible Therapeutic Targets"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1739"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Applied and Environmental Microbiology"],["dc.bibliographiccitation.lastpage","1748"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Reichard, Utz"],["dc.contributor.author","Lechenne, B."],["dc.contributor.author","Asif, Abdul Rahman"],["dc.contributor.author","Streit, Frank"],["dc.contributor.author","Grouzmann, E."],["dc.contributor.author","Jousson, Olivier"],["dc.contributor.author","Monod, Michel"],["dc.date.accessioned","2018-11-07T10:09:26Z"],["dc.date.available","2018-11-07T10:09:26Z"],["dc.date.issued","2006"],["dc.description.abstract","The secreted proteolytic activity of Aspergillus fumigatus is of potential importance as a virulence factor and in the industrial hydrolysis of protein sources. The A. fumigatus genome contains sequences that could encode a five-member gene family that produces proteases in the sedolisin family (MEROPS S53). Four putative secreted sedolisms with a predicted 17- to 20-amino-acid signal sequence were identified and termed SedA to SedD. SedA produced heterologously in Pichia pastoris was an acidic endoprotease. Heterologously produced SedB, SedC, and SedD were tripeptidyl-peptidases (TPP) with a common specificity for tripeptide-p-nitroanilide substrates at acidic pHs. Purified SedB hydrolyzed the peptide Ala-Pro-Gly-Asp-Arg-Ile-Tyr-Val-HisPro-Phe to Arg-Pro-Gly, Asp-Arg-Ile, and Tyr-Val-His-Pro-Phe, thereby confirming TPP activity of the enzyme. SedB, SedC, and SedD were detected by Western blotting in culture supernatants of A. fumigatus grown in a medium containing hemoglobin as the sole nitrogen source. A degradation product of SedA also was observed. A search for genes encoding sedolisin homologues in other fungal genomes indicates that sedolisin gene families are widespread among filamentous ascomycetes."],["dc.identifier.doi","10.1128/AEM.72.3.1739-1748.2006"],["dc.identifier.isi","000236069200003"],["dc.identifier.pmid","16517617"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39647"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0099-2240"],["dc.title","Sedolisins, a new class of secreted proteases from aspergillus fumigatus with endoprotease or tripeptidyl-peptidase activity at acidic pHs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","30"],["dc.bibliographiccitation.journal","Mycoses"],["dc.bibliographiccitation.lastpage","32"],["dc.bibliographiccitation.volume","51"],["dc.contributor.author","Reichard, Utz"],["dc.contributor.author","Jousson, Olivier"],["dc.contributor.author","Monod, Michel"],["dc.date.accessioned","2018-11-07T11:11:48Z"],["dc.date.available","2018-11-07T11:11:48Z"],["dc.date.issued","2008"],["dc.identifier.doi","10.1111/j.1439-0507.2008.01584.x"],["dc.identifier.isi","000258078900010"],["dc.identifier.pmid","18782242"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53519"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0933-7407"],["dc.title","Secreted protease of the mould fungus Aspergillus fumigatus"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","395"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Mycoses"],["dc.bibliographiccitation.lastpage","396"],["dc.bibliographiccitation.volume","51"],["dc.contributor.author","Reichard, Utz"],["dc.contributor.author","Jousson, Olivier"],["dc.contributor.author","Monod, Michel"],["dc.date.accessioned","2018-11-07T11:20:25Z"],["dc.date.available","2018-11-07T11:20:25Z"],["dc.date.issued","2008"],["dc.identifier.isi","000258408900057"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55532"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Malden"],["dc.relation.issn","0933-7407"],["dc.title","Novel secreted proteases of Aspergillus fumigatus"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]