The effect of the N-glycosylation on the biological activities of influenza A/H3N2 hemagglutinin
| Autor: | Emi Takashita, Seiji Hongo, Kanetsu Sugawara, Yoko Matsuzaki, Yasuhiro Abe, Yasushi Muraki |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
chemistry.chemical_classification
Cell fusion Glycosylation biology viruses Hemagglutinin (influenza) General Medicine Oligosaccharide medicine.disease_cause Virology Molecular biology Virus chemistry.chemical_compound chemistry N-linked glycosylation biology.protein Influenza A virus medicine Antibody |
| Zdroj: | International Congress Series. 1263:214-217 |
| ISSN: | 0531-5131 |
| Popis: | Influenza A/H3N2 viruses have increased the number of glycosylation sites on the head of the hemagglutinin (HA) protein since their appearance in 1968. Here, the effect of the addition of oligosaccharide chains to the HA of the H3N2 virus on its biological activities was investigated. We constructed wild-type HA and six mutant HAs of A/Aichi/2/68 virus with two or one to six glycosylation sites on the head, respectively. The glycosylation sites of mutated HAs correspond to representative H3N2 isolates (A/Victoria/3/75, A/Memphis/6/86 and A/Sydney/5/97). We analyzed their intracellular transport, receptor-binding and cell fusion activities. The results showed that all the mutated HAs were transported to the cell surface, as well as wild-type HA, but some of them decreased in the receptor-binding activity. By contrast, the cell-fusion activity was not affected. Reactivity of mutated HAs, having four or five oligosaccharides with human serum collected in 1976, was much lower than that of the wild-type HA. These observations raised the possibility that the addition of new oligosaccharides to the head of the HA of the H3N2 virus may have provided the virus with an ability to evade antibody pressures. |
| Databáze: | OpenAIRE |
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