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.
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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)
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Copyright | Copyright © 2011 Elsevier Inc. All rights reserved. |
Chemical References |
- Galactosides
- Neuraminidase
- N-Acetylneuraminic Acid
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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
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