High-throughput neuraminidase substrate specificity study of human and avian influenza A viruses.

Abstract

Despite the importance of neuraminidase (NA) activity in effective infection by influenza A viruses, limited information exists about the differences of substrate preferences of viral neuraminidases from different hosts or from different strains. Using a high-throughput screening format and a library of twenty α2-3- or α2-6-linked para-nitrophenol-tagged sialylgalactosides, substrate specificity of NAs on thirty-seven strains of human and avian influenza A viruses was studied using intact viral particles. Neuraminidases of all viruses tested cleaved both α2-3- and α2-6-linked sialosides but preferred α2-3-linked ones and the activity was dependent on the terminal sialic acid structure. In contrast to NAs of other subtypes of influenza A viruses which did not cleave 2-keto-3-deoxy-d-glycero-d-galacto-nonulosonic acid (Kdn) or 5-deoxy Kdn (5d-Kdn), NAs of all N7 subtype viruses tested had noticeable hydrolytic activities on α2-3-linked sialosides containing Kdn or 5d-Kdn. Additionally, group 1 NAs showed efficient activity in cleaving N-azidoacetylneuraminic acid from α2-3-linked sialoside.

• Authors: Yanhong Li, Hongzhi Cao, Nguyet Dao, Zheng Luo, Hai Yu, Yi Chen, Zheng Xing, Nicole Baumgarth, Carol Cardona, Xi Chen
• Journal: Virology (Virology) Vol. 415 Issue 1 Pg. 12-9 (Jun 20 2011) ISSN: 1096-0341 [Electronic] United States
• PMID: 21501853 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2011 Elsevier Inc. All rights reserved.

Chemical References

• Galactosides
• Neuraminidase
• N-Acetylneuraminic Acid

Topics

• Animals
• Birds (virology)
• Carbohydrate Conformation
• Galactosides (chemistry, metabolism)
• High-Throughput Screening Assays
• Humans
• Influenza A Virus, H9N2 Subtype (enzymology)
• Influenza A virus (enzymology)
• Influenza in Birds (virology)
• Influenza, Human (virology)
• N-Acetylneuraminic Acid (chemistry, metabolism)
• Neuraminidase (antagonists & inhibitors, chemistry, metabolism)
• Substrate Specificity