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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Li, Changgui Li, Xuguang Brown, Earl G. Jaentschke, Bozena Farnsworth, Aaron Wang, Junzhi Forbes, Nicole E. He, Runtao Van Domselaar, Gary Doyle, Tracey M. Hashem, Anwar M. |
| Description | Author Affiliation: Doyle TM ( Centre for Vaccine Evaluation, Biologics and Genetic Therapies Directorate, Health Products and Food Branch, Health Canada, Ottawa, Ontario K1A 0K9, Canada.) |
| Abstract | The only universally conserved sequence among all influenza A viral neuraminidases is located between amino acids 222 and 230. However, the potential roles of these amino acids remain largely unknown. Through an array of experimental approaches including mutagenesis, reverse genetics, and growth kinetics, we found that this sequence could markedly affect viral replication. Additional experiments revealed that enzymes with mutations in this region demonstrated substantially decreased catalytic activity, substrate binding, and thermostability. Consistent with viral replication analyses and enzymatic studies, protein modeling suggests that these amino acids could either directly bind to the substrate or contribute to the formation of the active site in the enzyme. Collectively, these findings reveal the essential role of this unique region in enzyme function and viral growth, which provides the basis for evaluating the validity of this sequence as a potential target for antiviral intervention and vaccine development. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 25 |
| Volume Number | 288 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2013-06-21 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Epitopes Metabolism Influenza A Virus Enzymology Neuraminidase Viral Proteins Virus Replication Amino Acid Substitution Animals Binding Sites Genetics Biocatalysis Catalytic Domain Cell Line Chick Embryo Enzyme Stability Chemistry HEK293 Cells Kinetics Models, Molecular Mutation Protein Structure, Tertiary Substrate Specificity Temperature Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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