Aeromonas salmonicida binds α2-6 linked sialic acid, which is absent among the glycosphingolipid repertoires from skin, gill, stomach, pyloric caecum, and intestine ...

• Main Authors: Benktander, John, Sundh, Henrik, Sharba, Sinan, Teneberg, Susann, Lindén, Sara K.
• Format: Dataset
• Language: unknown
• Published: Taylor & Francis 2022
• Subjects: Biochemistry; Medicine; Microbiology; FOS Biological sciences; Cell Biology; Environmental Sciences not elsewhere classified; Ecology; Immunology; FOS Clinical medicine; Cancer; Atlantic salmon
• Online Access: https://dx.doi.org/10.6084/m9.figshare.21295520.v1; https://tandf.figshare.com/articles/dataset/_i_Aeromonas_salmonicida_i_binds_2-6_linked_sialic_acid_which_is_absent_among_the_glycosphingolipid_repertoires_from_skin_gill_stomach_pyloric_caecum_and_intestine/21295520/1

Carbohydrates can both protect against infection and act as targets promoting infection. Mucins are major components of the slimy mucus layer covering the fish epithelia. Mucins can act as decoys for intimate pathogen interaction with the host afforded by binding to glycosphingolipids in the host cell membrane. We isolated and characterized glycosphingolipids from Atlantic salmon skin, gill, stomach, pyloric caeca, and intestine. We characterized the glycosphingolipids using liquid chromatography – mass spectrometry and tandem mass spectrometry and the glycan repertoire was compared with the glycan repertoire of mucins from the same epithelia. We also investigated Aeromonas salmonicida binding using chromatogram and microtiter well based binding assays. We identified 29 glycosphingolipids. All detected acid glycans were of the ganglio-series (unless shorter) and showed a high degree of polysialylation. The non-acid glycans were mostly composed of the neolacto, globo, and ganglio core structures. The ...