Reichard, Utz

[["dc.bibliographiccitation.firstpage","405"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Infection and Immunity"],["dc.bibliographiccitation.lastpage","412"],["dc.bibliographiccitation.volume","69"],["dc.contributor.author","Zaugg, C."],["dc.contributor.author","Borg-von Zepelin, Margarete"],["dc.contributor.author","Reichard, Utz"],["dc.contributor.author","Sanglard, D."],["dc.contributor.author","Monod, Michel"],["dc.date.accessioned","2018-11-07T09:34:03Z"],["dc.date.available","2018-11-07T09:34:03Z"],["dc.date.issued","2001"],["dc.description.abstract","Medically important yeasts of the genus Candida secrete aspartic proteinases (Saps), which are of particular interest as virulence factors. Like Candida albicans, Candida tropicalis secretes in vitro one dominant Sap (Sapt1p) in a medium containing bovine serum albumin (BSA) as the sole source of nitrogen. Using the gene SAPT1 as a probe and under low-stringency hybridization conditions, three new closely related gene sequences, SAPT2 to SAPT4, encoding secreted proteinases were cloned from a C. tropicalis lambda EMBL3 genomic library. All bands identified by Southern blotting of EcoRI-digested C. tropicalis genomic DNA with SAPT1 could be assigned to a specific SAP gene. Therefore, the SAPT gene family of C. tropicalis is likely to contain only four members. Interestingly, the SAPT2 and SAPT3 gene products, Sapt2p and Sapt3p, which have not yet been detected in C. tropicalis cultures in vitro, were produced as active recombinant enzymes with the methylotrophic yeast Pichia pastoris as an expression system. As expected, reverse transcriptase PCR experiments revealed a strong SAPT1 signal with RNA extracted from cells grown in BSA medium. However, a weak signal was obtained with all other SAPT genes under several renditions tested, showing that these SAPT genes could be expressed at a basic level. Together, these experiments suggest that the gene products Sapt2p, Sapt3p, and Sapt4p could be produced under conditions yet to be described in vitro or during infection."],["dc.identifier.doi","10.1128/IAI.69.1.405-412.2001"],["dc.identifier.isi","000165943500050"],["dc.identifier.pmid","11119531"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32096"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0019-9567"],["dc.title","Secreted aspartic proteinase family of Candida tropicalis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","424"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Current protein & peptide science"],["dc.bibliographiccitation.lastpage","429"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Reichard, Utz"],["dc.contributor.author","Herrmann, Sahra"],["dc.contributor.author","Asif, Abdul R."],["dc.date.accessioned","2019-07-09T11:41:29Z"],["dc.date.available","2019-07-09T11:41:29Z"],["dc.date.issued","2014"],["dc.description.abstract","Although innate immunity primarily combats systemic infections of opportunistic fungi such as Aspergillus and Candida spp., acquired and protective immunoreactions were observed long ago in animal trials following sublethal systemic infections caused by viable fungi or after challenging animals with inactivated fungal cells. Based on these observations, fungal antigens should exist which mediate such protective immunoreactions and have in part already been identified. In this context, this review focuses primarily on the various approaches that have been used to identify protection-mediating Aspergillus-antigens and their rationale. Emphasis is placed on screening methods that have exploited genetic or proteomic approaches on the basis of the corresponding fungal genome projects. Thereby, a survey and description is given of the antigens so far known to be capable of inducing immune responses that protect animals against acquiring lethal systemic aspergillosis."],["dc.identifier.doi","10.2174/1389203715666140512122037"],["dc.identifier.fs","611058"],["dc.identifier.pmid","24818757"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12124"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58444"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1875-5550"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.mesh","Animals"],["dc.subject.mesh","Antigens, Fungal"],["dc.subject.mesh","Aspergillosis"],["dc.subject.mesh","Aspergillus fumigatus"],["dc.subject.mesh","Humans"],["dc.subject.mesh","Opportunistic Infections"],["dc.subject.mesh","Vaccination"],["dc.title","Vaccination approaches against opportunistic fungal infections caused by Aspergillus fumigatus."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","submitted_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","954"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Proteome Research"],["dc.bibliographiccitation.lastpage","962"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Asif, Abdul Rahman"],["dc.contributor.author","Oellerich, M."],["dc.contributor.author","Amstrong, V. W."],["dc.contributor.author","Riemenschneider, B."],["dc.contributor.author","Monod, Michel"],["dc.contributor.author","Reichard, Utz"],["dc.date.accessioned","2018-11-07T10:02:59Z"],["dc.date.available","2018-11-07T10:02:59Z"],["dc.date.issued","2006"],["dc.description.abstract","Aspergillus fumigatus is a mold causing most of the invasive fungal lung infections in the immunocompromised host. In addition, the species is the causative agent of certain allergic diseases. Both in invasive and in allergic diseases, the conidial surface mediates the first contact with the human immune system. Thus, conidial surface proteins may be reasonable vaccine candidates as well as important allergens. To broaden the list of those antigens, intact viable Aspergillus conidia were extracted with mild alkaline buffer at pH 8.5 in the presence of a 1,3-beta-glucanase. The proteome of this fraction was separated by two- dimensional gel electrophoresis (2-DE) and analyzed by liquid chromatography coupled with tandem mass spectrometry. Altogether 26 different A. fumigatus proteins were identified, twelve of which contain a signal for secretion. Among these were the known major conidial surface protein rodlet A, one acid protease PEP2, one lipase, a putative disulfide isomerase and a putative fructose-1,6-biphosphatase. The known allergen Aspf 3 was identified among the proteins without a signal for secretion. On the basis of the recently annotated A. fumigatus genome (Nature 2005, 438, 1151-1156), proteome analysis is now a powerful tool to confirm expression of hypothetical proteins and, thereby to identify additional vaccine candidates and possible new allergens of this important fungal pathogen."],["dc.description.sponsorship","NIAID NIH HHS [U01 AI 48830]; Wellcome Trust"],["dc.identifier.doi","10.1021/pr0504586"],["dc.identifier.isi","000236816100025"],["dc.identifier.pmid","16602703"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38345"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","1535-3893"],["dc.title","Proteome of conidial surface associated proteins of Aspergillus fumigatus reflecting potential vaccine candidates and allergens"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["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","5517"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Journal of Proteome Research"],["dc.bibliographiccitation.lastpage","5529"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Singh, Bharat"],["dc.contributor.author","Oellerich, Michael"],["dc.contributor.author","Kumar, Ram"],["dc.contributor.author","Kumar, Manish"],["dc.contributor.author","Bhadoria, Dharam P."],["dc.contributor.author","Reichard, Utz"],["dc.contributor.author","Gupta, Vijay K."],["dc.contributor.author","Sharma, Gainda L."],["dc.contributor.author","Asif, Abdul R."],["dc.date.accessioned","2018-11-07T08:37:39Z"],["dc.date.available","2018-11-07T08:37:39Z"],["dc.date.issued","2010"],["dc.description.abstract","The secreted proteomes of a three week old culture of an Indian (190/96) and a German (DAYA) Aspergillus fumigatus isolate were investigated for reactivity with IgG and/or IgE antibodies derived from pooled allergic broncho-pulmonary aspergillosis (ABPA) patients' sera. Two dimensional Western blotting followed by mass spectrometric analysis of the reactive protein spots revealed 35 proteins from the two A. fumigatus strains. There were seven known A. fumigatus allergens among them (Asp f1-4, Asp 19, Asp f10, and Asp f13/15), whereas three proteins displaying significant sequence similarity to known fungal allergens have been assigned as predicted allergens (Dipeptidyl-peptidase-V precursor, Nuclear transport factor 2, and Malate dehydrogenase, NAD-dependent). Eight IgG and IgE reactive proteins were common in both strains; however, 12 proteins specifically reacted in 190/96 and 15 in DAYA. Further testing with sera of 5 individual ABPA patients demonstrated that 12 out of 20 immunoreactive proteins of 190/96 strain of A. fumigatus had consistent reactivity with IgE. Seven of these proteins reacted with IgG also. The 25 of 35 identified proteins are novel with respect to immunoreactivity with ABPA patients' sera and could form a panel of molecules to improve the currently existing less-sensitive diagnostic methods. Through expressing recombinantly, these proteins may also serve as a tool in desensibilization strategies."],["dc.identifier.doi","10.1021/pr100604x"],["dc.identifier.isi","000283810500002"],["dc.identifier.pmid","20828163"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6075"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18588"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","1535-3893"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Immuno-Reactive Molecules Identified from the Secreted Proteome of 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","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","785"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","799"],["dc.bibliographiccitation.volume","52"],["dc.contributor.author","Krappmann, Sven"],["dc.contributor.author","Bignell, Elaine M."],["dc.contributor.author","Reichard, Utz"],["dc.contributor.author","Rogers, T."],["dc.contributor.author","Haynes, K."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T10:49:24Z"],["dc.date.available","2018-11-07T10:49:24Z"],["dc.date.issued","2004"],["dc.description.abstract","We have cloned and characterized the Aspergillus fumigatus cpcA gene encoding the transcriptional activator of the cross-pathway control system of amino acid biosynthesis. cpcA encodes a functional orthologue of Saccharomyces cerevisiae Gcn4p. The coding sequence of the 2.2 kb transcript is preceded by two short upstream open reading frames, the larger one being well conserved among Aspergilli. Deletion strains in which either the coding sequence or the entire locus are replaced by a bifunctional dominant marker are impaired in their cross-pathway control response upon amino acid starvation, as demonstrated by analyses of selected reporter genes and specific enzymatic activities. In a murine model of pulmonary aspergillosis, cpcADelta strains display attenuated virulence. Pathogenicity is restored to wild-type levels in strains with reconstitution of the genomic locus. Competitive mixed infection experiments additionally demonstrate that cpcADelta strains are less able to survive in vivo than their wild-type progenitor. Our data suggest that specific stress conditions are encountered by A. fumigatus within the mammalian host and that the fungal cross-pathway control system plays a significant role in pulmonary aspergillosis."],["dc.identifier.doi","10.1111/j.1365-2958.2004.04015.x"],["dc.identifier.isi","000220941400016"],["dc.identifier.pmid","15101984"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48419"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1365-2958"],["dc.relation.issn","0950-382X"],["dc.title","The Aspergillus fumigatus transcriptional activator CpcA contributes significantly to the virulence of this fungal pathogen"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Mycoses"],["dc.bibliographiccitation.volume","54"],["dc.contributor.author","Bader, Oliver"],["dc.contributor.author","Lugert, Raimond"],["dc.contributor.author","Kuhns, Martin"],["dc.contributor.author","Reichard, Utz"],["dc.contributor.author","Weig, Michael S."],["dc.contributor.author","Gross, U."],["dc.date.accessioned","2018-11-07T08:52:29Z"],["dc.date.available","2018-11-07T08:52:29Z"],["dc.date.issued","2011"],["dc.format.extent","403"],["dc.identifier.isi","000294878900056"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22171"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Malden"],["dc.relation.issn","0933-7407"],["dc.title","Azole antifungal drug resistance in clinical Aspergillus fumigatus isolates as a consequence of azole use in agriculture in Germany?"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","723"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Medical Mycology"],["dc.bibliographiccitation.lastpage","731"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Spreer, Annette"],["dc.contributor.author","Ruechel, Reinhard"],["dc.contributor.author","Reichard, Utz"],["dc.date.accessioned","2018-11-07T08:54:56Z"],["dc.date.available","2018-11-07T08:54:56Z"],["dc.date.issued","2006"],["dc.description.abstract","An endoprotease Arp (alkaline Rhizopus protease) was identified and purified to virtual homogeneity from the culture supernatant of an isolate of Rhizopus microsporus var. rhizopodiformis recovered from a non-fatal case of rhinoorbital mucormycosis. N-terminal sequencing of the mature native enzyme was obtained for the first 20 amino acids and revealed high homology to serine proteases of the subtilisin subfamily. Arp migrated in SDS-PAGE with an estimated molecular mass of 33 kDa and had a pI determined to be at pH 8.8. Arp is proteolytically active against various substrates, including elastin, over a broad pH range between 6 and 12 with an optimum at pH 10.5. After invasive mucormycosis, specific antibodies against Arp were detected in stored serum samples taken from the patient from whom the R. microsporus strain of this study had been isolated. Furthermore, in search of factors involved in thrombosis as a typical complication of mucormycosis, a procoagulatory effect of the enzyme has recently been shown. Altogether, these data substantiate the expression of Arp during human rhinoorbital mucormycosis and suggest a role of the enzyme in pathogenesis."],["dc.identifier.doi","10.1080/13693780600936399"],["dc.identifier.isi","000244151400005"],["dc.identifier.pmid","17127629"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22790"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Taylor & Francis Ltd"],["dc.relation.issn","1369-3786"],["dc.title","Characterization of an extracellular subtilisin protease of Rhizopus microsporus and evidence for its expression during invasive rhinoorbital mycosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Mycoses"],["dc.bibliographiccitation.volume","55"],["dc.contributor.author","Herrmann, S."],["dc.contributor.author","Iben, I."],["dc.contributor.author","Gross, U."],["dc.contributor.author","Reichard, Utz"],["dc.date.accessioned","2018-11-07T09:09:42Z"],["dc.date.available","2018-11-07T09:09:42Z"],["dc.date.issued","2012"],["dc.format.extent","59"],["dc.identifier.isi","000305069800189"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26322"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.issn","0933-7407"],["dc.title","Reduced virulence of Aspergillus fumigatus mutants after knock-out of conidial surface proteins"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]