Journal
VIROLOGY
Volume 527, Issue -, Pages 132-140Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2018.11.010
Keywords
Influenza A virus; Lectin microarray; Hemagglutinin; Glycosylation; alpha-Gal
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Funding
- Japan Society for the Promotion of Science (JSPS) KAKENHI [16H06597, 18K15176]
- Grants-in-Aid for Scientific Research [16H06597, 18K15176] Funding Source: KAKEN
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Glycan structures on hemagglutinin (HA) of influenza A viruses have been analyzed previously to understand their significance. However, the formerly established methods using mass spectrometry present disadvantages such as procedure complexity, sensitivity, and throughput. Our study has established a novel method for analyzing glycan profiles of HA using lectin microarray techniques. We successfully obtained glycan profiles of HA starting from 1 ml of the 10(6) TCID50 samples through simple antigen enrichment using optimized immunoprecipitation. The profiles were reasonably consistent with known glycan structures of HA. Next, we compared glycan profiles of the HAs prepared from chicken embryos, MDCK, Vero, and A549 cells, and demonstrated the host cell-specific HA glycan profiles. Notably, the HA from MDCK cells was alpha 1-3 galactosylated. Our method provides a highly sensitive and simple procedure for glycan profiling of the viral glycoproteins, thereby paving way for direct glycan analyses of human- and animal-derived virions.
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