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  Immunoproteomic analysis of antibody responses to extracellular proteins of Candida albicans revealed the importance of glycosylation for antigen recognition

Luo, T., Krüger, T., Knüpfer, U., Kasper, L., Wielsch, N., Hube, B., et al. (2016). Immunoproteomic analysis of antibody responses to extracellular proteins of Candida albicans revealed the importance of glycosylation for antigen recognition. Journal of Proteome Research, 15(8), 2394-2406. doi:10.1021/acs.jproteome.5b01065.

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 Urheber:
Luo, Ting, Autor
Krüger, Thomas, Autor
Knüpfer, Uwe, Autor
Kasper, Lydia, Autor
Wielsch, Natalie1, Autor           
Hube, Bernhard, Autor
Kortgen, Andreas, Autor
Bauer, Michael, Autor
Giamarellos-Bourboulis, Evangelos J., Autor
Dimopoulos, George, Autor
Brakhage, Axel A., Autor
Kniemeyer, Olaf, Autor
Affiliations:
1Research Group Mass Spectrometry, MPI for Chemical Ecology, Max Planck Society, ou_421899              

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 Zusammenfassung: During infection, the human pathogenic fungus Candida albicans undergoes a yeast-to-hypha transition, secretes numerous proteins for invasion of host tissues, and modulates the host’s immune response. Little is known about the interplay of C. albicans secreted proteins and the host adaptive immune system. Here, we applied a combined 2D gel- and LC−MS/MSbased approach for the characterization of C. albicans extracellular proteins during the yeast-to-hypha transition, which led to a comprehensive C. albicans secretome map. The serological responses to C. albicans extracellular proteins were investigated by a 2D-immunoblotting approach combined with MS for protein identification. On the basis of the screening of sera from candidemia and three groups of noncandidemia patients, a core set of 19 immunodominant antibodies against secreted proteins of C. albicans was identified, seven of which represent potential diagnostic markers for candidemia (Xog1, Lip4, Asc1, Met6, Tsa1, Tpi1, and Prx1). Intriguingly, some secreted, strongly glycosylated protein antigens showed high cross-reactivity with sera from noncandidemia control groups. Enzymatic deglycosylation of proteins secreted from hyphae significantly impaired sera antibody recognition. Furthermore, deglycosylation of the recombinantly produced, secreted aspartyl protease Sap6 confirmed a significant contribution of glycan epitopes to the recognition of Sap6 by antibodies in patient’s sera.

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 Datum: 2016-07-082016-08-05
 Publikationsstatus: Erschienen
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 Art der Begutachtung: -
 Identifikatoren: Anderer: MS184
DOI: 10.1021/acs.jproteome.5b01065
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Titel: Journal of Proteome Research
  Andere : J. Proteome Res.
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Washington, D.C. : American Chemical Society
Seiten: - Band / Heft: 15 (8) Artikelnummer: - Start- / Endseite: 2394 - 2406 Identifikator: ISSN: 1535-3893
CoNE: https://pure.mpg.de/cone/journals/resource/111019664290000