<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Clo E</submitter><funding>European Commission FP7</funding><pagination>6268-78</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3372205</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>86(11)</volume><pubmed_abstract>Viral envelope proteins mediate interactions with host cells, leading to internalization and intracellular propagation. Envelope proteins are glycosylated and are known to serve important functions in masking host immunity to viral glycoproteins. However, the viral infectious cycle in cells may also lead to aberrant glycosylation that may elicit immunity. Our knowledge of immunity to aberrant viral glycans and glycoproteins is limited, potentially due to technical limitations in identifying immunogenic glycans and glycopeptide epitopes. This work describes three different complementary methods for high-throughput screening and identification of potential immunodominant O-glycopeptide epitopes on viral envelope glycoproteins: (i) on-chip enzymatic glycosylation of scan peptides, (ii) chemic</pubmed_abstract><journal>Journal of virology</journal><pubmed_title>Characterization of the viral O-glycopeptidome: a novel tool of relevance for vaccine design and serodiagnosis.</pubmed_title><pmcid>PMC3372205</pmcid><funding_grant_id>FP7_215536</funding_grant_id><pubmed_authors>Bergstrom T</pubmed_authors><pubmed_authors>Kracun SK</pubmed_authors><pubmed_authors>Nudelman AS</pubmed_authors><pubmed_authors>Clo E</pubmed_authors><pubmed_authors>Olofsson S</pubmed_authors><pubmed_authors>Blixt O</pubmed_authors><pubmed_authors>Jensen KJ</pubmed_authors><pubmed_authors>Liljeqvist JA</pubmed_authors></additional><is_claimable>false</is_claimable><name>Characterization of the viral O-glycopeptidome: a novel tool of relevance for vaccine design and serodiagnosis.</name><description>Viral envelope proteins mediate interactions with host cells, leading to internalization and intracellular propagation. Envelope proteins are glycosylated and are known to serve important functions in masking host immunity to viral glycoproteins. However, the viral infectious cycle in cells may also lead to aberrant glycosylation that may elicit immunity. Our knowledge of immunity to aberrant viral glycans and glycoproteins is limited, potentially due to technical limitations in identifying immunogenic glycans and glycopeptide epitopes. This work describes three different complementary methods for high-throughput screening and identification of potential immunodominant O-glycopeptide epitopes on viral envelope glycoproteins: (i) on-chip enzymatic glycosylation of scan peptides, (ii) chemic</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 Jun</publication><modification>2026-05-02T00:03:24.448Z</modification><creation>2019-03-27T00:54:24Z</creation></dates><accession>S-EPMC3372205</accession><cross_references><pubmed>22491453</pubmed><doi>10.1128/JVI.00392-12</doi><doi>10.1128/jvi.00392-12</doi></cross_references></HashMap>