Exoproteome Analysis of Human Pathogenic Dermatophyte Species and Identification of Immunoreactive Proteins
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Exoproteome Analysis of Human Pathogenic Dermatophyte Species and Identification of Immunoreactive Proteins. / Eymann, Christine; Wachlin, Gerhild; Albrecht, Dirk; Tiede, Stephan; Krummrei, Ulrike; Jünger, Michael; Hecker, Michael; Daeschlein, Georg.
In: PROTEOM CLIN APPL, Vol. 12, No. 6, 11.2018, p. e1800007.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Exoproteome Analysis of Human Pathogenic Dermatophyte Species and Identification of Immunoreactive Proteins
AU - Eymann, Christine
AU - Wachlin, Gerhild
AU - Albrecht, Dirk
AU - Tiede, Stephan
AU - Krummrei, Ulrike
AU - Jünger, Michael
AU - Hecker, Michael
AU - Daeschlein, Georg
N1 - © 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
PY - 2018/11
Y1 - 2018/11
N2 - PURPOSE: Increasing incidence of onychomycosis and tinea pedis in humans of industrialized countries together with deep tissue infections are a therapeutic challenge in clinical mycology. For a better understanding of the pathology and immunology of infection, the authors analyze the exoproteomes of three reference strains of the most common clinical dermatophyte species (Trichophyton rubrum, Trichophyton interdigitale, Arthroderma benhamiae) and of Trichophyton strains isolated from affected patients.EXPERIMENTAL DESIGN: Extracellular proteins of those in vitro grown strains are separated via 2D High Performance Electrophoresis and identified by mass spectrometry to find proteins with provoked host immune reactivity.RESULTS: More than 80 secreted proteins including virulence factors such as peptidases and other hydrolases are identified. By Western blotting with respective patient sera, up to 31 proteins with significant antigen-antibody reactions are detected in comparison with control sera, for example, peptidases as well as several oxidoreductases. One protein, beta-glucosidase F2SZI9 seems to be a commonly processed antigen in all Trichophyton infections.CONCLUSIONS AND CLINICAL RELEVANCE: These first global exoproteome data of three dermatophyte species can be a stepping stone on the way to further study the molecular mechanisms of Trichophyton pathogenicity-associated traits. Possible candidates for potential new diagnostic methods or vaccination have to be validated in further investigations.
AB - PURPOSE: Increasing incidence of onychomycosis and tinea pedis in humans of industrialized countries together with deep tissue infections are a therapeutic challenge in clinical mycology. For a better understanding of the pathology and immunology of infection, the authors analyze the exoproteomes of three reference strains of the most common clinical dermatophyte species (Trichophyton rubrum, Trichophyton interdigitale, Arthroderma benhamiae) and of Trichophyton strains isolated from affected patients.EXPERIMENTAL DESIGN: Extracellular proteins of those in vitro grown strains are separated via 2D High Performance Electrophoresis and identified by mass spectrometry to find proteins with provoked host immune reactivity.RESULTS: More than 80 secreted proteins including virulence factors such as peptidases and other hydrolases are identified. By Western blotting with respective patient sera, up to 31 proteins with significant antigen-antibody reactions are detected in comparison with control sera, for example, peptidases as well as several oxidoreductases. One protein, beta-glucosidase F2SZI9 seems to be a commonly processed antigen in all Trichophyton infections.CONCLUSIONS AND CLINICAL RELEVANCE: These first global exoproteome data of three dermatophyte species can be a stepping stone on the way to further study the molecular mechanisms of Trichophyton pathogenicity-associated traits. Possible candidates for potential new diagnostic methods or vaccination have to be validated in further investigations.
KW - Journal Article
U2 - 10.1002/prca.201800007
DO - 10.1002/prca.201800007
M3 - SCORING: Journal article
C2 - 29952123
VL - 12
SP - e1800007
JO - PROTEOM CLIN APPL
JF - PROTEOM CLIN APPL
SN - 1862-8346
IS - 6
ER -