Effective replication of human influenza viruses in mice lacking a major α2,6 sialyltransferase
| Autor: | Peter Palese, James C. Paulson, Gina M. Conenello, Laurel Glaser |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Cancer Research
Sialyltransferase Sialoglycoproteins Respiratory System Cell Hemagglutinin (influenza) Biology Virus Replication Virus Mice chemistry.chemical_compound Influenza A Virus H1N1 Subtype Orthomyxoviridae Infections Virology medicine Animals Humans Receptor beta-D-Galactoside alpha 2-6-Sialyltransferase Mice Knockout chemistry.chemical_classification Cell Membrane Sialyltransferases Sialic acid Mice Inbred C57BL Infectious Diseases medicine.anatomical_structure chemistry Influenza A virus Sialic Acids biology.protein Receptors Virus Glycoprotein Respiratory tract |
| Zdroj: | Virus Research. 126:9-18 |
| ISSN: | 0168-1702 |
| DOI: | 10.1016/j.virusres.2007.01.011 |
| Popis: | The hemagglutinins of influenza viruses isolated from humans typically prefer binding to sialic acid in an alpha2,6 linkage. Presumably, the virus uses the presence of these receptors on the respiratory tract to gain entrance into the host cell. The ST6Gal I sialyltransferase knock-out mouse lacks the main enzyme necessary for the attachment of alpha2,6 sialic acid to N-linked glycoproteins on the cell surface. Yet even in the absence of detectable alpha2,6 sialic acid in the mouse respiratory tract, human influenza viruses can still infect these mice and grow to similar titers in the lung and trachea as compared to wild-type animals. This work demonstrates that the presence of a major alpha2,6 sialic acid on N-linked glycoproteins is not essential for human influenza virus infection in mice. |
| Databáze: | OpenAIRE |
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