<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Jia LJ</submitter><funding>Bundesministerium für Bildung und Forschung</funding><funding>Deutsche Forschungsgemeinschaft</funding><pagination>e00535-20</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7426169</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>5(4)</volume><pubmed_abstract>&lt;i>Aspergillus fumigatus&lt;/i> is one of the most common airborne molds capable of causing mycoses and allergies in humans. During infection, fungal surface proteins mediate the first contact with the human immune system to evade immune responses or to induce hypersensitivity. Several methods have been established for surface proteomics (surfomics). Biotinylation coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS) identification of peptides is a particularly efficient method to identify the surface-exposed regions of proteins that potentially mediate interaction with the host. After biotinylation of surface proteins during spore germination, we detected 231 different biotinylated surface proteins (including several well-known proteins such as RodA, CcpA, and DppV; allergen</pubmed_abstract><journal>mSphere</journal><pubmed_title>Biotinylated Surfome Profiling Identifies Potential Biomarkers for Diagnosis and Therapy of Aspergillus fumigatus Infection.</pubmed_title><pmcid>PMC7426169</pmcid><funding_grant_id>CRC/Transregio 124 project Z02 (210879364)</funding_grant_id><funding_grant_id>EXASENS (13N13861)</funding_grant_id><funding_grant_id>AfuInf (316898429)</funding_grant_id><funding_grant_id>CRC/Transregio 124 project A01 (210879364)</funding_grant_id><pubmed_authors>Brakhage AA</pubmed_authors><pubmed_authors>Jia LJ</pubmed_authors><pubmed_authors>Blango MG</pubmed_authors><pubmed_authors>von Eggeling F</pubmed_authors><pubmed_authors>Kruger T</pubmed_authors><pubmed_authors>Kniemeyer O</pubmed_authors></additional><is_claimable>false</is_claimable><name>Biotinylated Surfome Profiling Identifies Potential Biomarkers for Diagnosis and Therapy of Aspergillus fumigatus Infection.</name><description>&lt;i>Aspergillus fumigatus&lt;/i> is one of the most common airborne molds capable of causing mycoses and allergies in humans. During infection, fungal surface proteins mediate the first contact with the human immune system to evade immune responses or to induce hypersensitivity. Several methods have been established for surface proteomics (surfomics). Biotinylation coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS) identification of peptides is a particularly efficient method to identify the surface-exposed regions of proteins that potentially mediate interaction with the host. After biotinylation of surface proteins during spore germination, we detected 231 different biotinylated surface proteins (including several well-known proteins such as RodA, CcpA, and DppV; allergen</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Aug</publication><modification>2026-06-06T23:05:33.072Z</modification><creation>2020-09-14T07:16:37Z</creation></dates><accession>S-EPMC7426169</accession><cross_references><pubmed>32817453</pubmed><doi>10.1128/mSphere.00535-20</doi></cross_references></HashMap>