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N-glycoproteomic analyses of human intestinal enteroids, varying in histo-blood group geno- and phenotypes, reveal a wide repertoire of fucosylated glycoproteins.
Nilsson, Jonas; Rimkute, Inga; Sihlbom, Carina; Tenge, Victoria R; Lin, Shih-Ching; Atmar, Robert L; Estes, Mary K; Larson, Göran.
Afiliación
  • Nilsson J; Department of Laboratory Medicine, Institute of Biomedicine, University of Gothenburg, Sahlgrenska University Hospital, Bruna Stråket 16, SE 413 45, Gothenburg, Sweden.
  • Rimkute I; Department of Clinical Chemistry, Region Västra Götaland, Sahlgrenska University Hospital, Bruna Stråket 16, SE 413 45, Gothenburg, Sweden.
  • Sihlbom C; Proteomics Core Facilities, Sahlgrenska Academy, University of Gothenburg, Medicinaregatan 9E, SE 413 90, Gothenburg, Sweden.
  • Tenge VR; Department of Laboratory Medicine, Institute of Biomedicine, University of Gothenburg, Sahlgrenska University Hospital, Bruna Stråket 16, SE 413 45, Gothenburg, Sweden.
  • Lin SC; Department of Microbiology and Immunology, Institute of Biomedicine, University of Gothenburg, Medicinaregatan 7A, SE 413 90, Gothenburg, Sweden.
  • Atmar RL; Proteomics Core Facilities, Sahlgrenska Academy, University of Gothenburg, Medicinaregatan 9E, SE 413 90, Gothenburg, Sweden.
  • Estes MK; Department of Molecular Virology, Baylor College School of Medicine, One Baylor Plaza, Houston, TX 770 30, United States.
  • Larson G; Department of Molecular Virology, Baylor College School of Medicine, One Baylor Plaza, Houston, TX 770 30, United States.
Glycobiology ; 34(6)2024 04 24.
Article en En | MEDLINE | ID: mdl-38590172
ABSTRACT
Human noroviruses, globally the main cause of viral gastroenteritis, show strain specific affinity for histo-blood group antigens (HBGA) and can successfully be propagated ex vivo in human intestinal enteroids (HIEs). HIEs established from jejunal stem cells of individuals with different ABO, Lewis and secretor geno- and phenotypes, show varying susceptibility to such infections. Using bottom-up glycoproteomic approaches we have defined and compared the N-linked glycans of glycoproteins of seven jejunal HIEs. Membrane proteins were extracted, trypsin digested, and glycopeptides enriched by hydrophilic interaction liquid chromatography and analyzed by nanoLC-MS/MS. The Byonic software was used for glycopeptide identification followed by hands-on verifications and interpretations. Glycan structures and attachment sites were identified from MS2 spectra obtained by higher-energy collision dissociation through analysis of diagnostic saccharide oxonium ions (B-ions), stepwise glycosidic fragmentation of the glycans (Y-ions), and peptide sequence ions (b- and y-ions). Altogether 694 unique glycopeptides from 93 glycoproteins were identified. The N-glycans encompassed pauci- and oligomannose, hybrid- and complex-type structures. Notably, polyfucosylated HBGA-containing glycopeptides of the four glycoproteins tetraspanin-8, carcinoembryonic antigen-related cell adhesion molecule 5, sucrose-isomaltase and aminopeptidase N were especially prominent and were characterized in detail and related to donor ABO, Lewis and secretor types of each HIE. Virtually no sialylated N-glycans were identified for these glycoproteins suggesting that terminal sialylation was infrequent compared to fucosylation and HBGA biosynthesis. This approach gives unique site-specific information on the structural complexity of N-linked glycans of glycoproteins of human HIEs and provides a platform for future studies on the role of host glycoproteins in gastrointestinal infectious diseases.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Antígenos de Grupos Sanguíneos / Glicoproteínas / Organoides / Infecciones por Caliciviridae / Fucosa / Antígenos de Histocompatibilidad / Yeyuno Límite: Humans Idioma: En Revista: Glycobiology Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Suecia

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Antígenos de Grupos Sanguíneos / Glicoproteínas / Organoides / Infecciones por Caliciviridae / Fucosa / Antígenos de Histocompatibilidad / Yeyuno Límite: Humans Idioma: En Revista: Glycobiology Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Suecia