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- W2949771937 endingPage "3294.e6" @default.
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- W2949771937 abstract "A species barrier for the influenza A virus is the differential expression of sialic acid, which can either be α2,3-linked for avians or α2,6-linked for human viruses. The influenza A virus hosts also express other species-specific sialic acid derivatives. One major modification at C-5 is N-glycolyl (NeuGc), instead of N-acetyl (NeuAc). N-glycolyl is mammalian specific and expressed in pigs and horses, but not in humans, ferrets, seals, or dogs. Hemagglutinin (HA) adaptation to either N-acetyl or N-glycolyl is analyzed on a sialoside microarray containing both α2,3- and α2,6-linkage modifications on biologically relevant N-glycans. Binding studies reveal that avian, human, and equine HAs bind either N-glycolyl or N-acetyl. Structural data on N-glycolyl binding HA proteins of both H5 and H7 origin describe this specificity. Neuraminidases can cleave N-glycolyl efficiently, and tissue-binding studies reveal strict species specificity. The exclusive manner in which influenza A viruses differentiate between N-glycolyl and N-acetyl is indicative of selection." @default.
- W2949771937 created "2019-06-27" @default.
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- W2949771937 date "2019-06-01" @default.
- W2949771937 modified "2023-10-18" @default.
- W2949771937 title "N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses" @default.
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- W2949771937 doi "https://doi.org/10.1016/j.celrep.2019.05.048" @default.
- W2949771937 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6750725" @default.
- W2949771937 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31189111" @default.
- W2949771937 hasPublicationYear "2019" @default.