2013 Fiscal Year Annual Research Report
新規インフルエンザワクチン開発のための付着抗原の糖鎖修飾の基礎的研究
| Project/Area Number |
24792010
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| Research Institution | Nihon University |
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Principal Investigator |
CUENO Marni 日本大学, 歯学部, ポスト・ドクトラル・フェロー (20569967)
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| Keywords | H1N1 / 2013 H7N9 / Hemagglutinin / Influenza / OGS / salt bridge |
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| Research Abstract |
Influenza A virus HA glycoprotein which is a type I integral membrane with an ectodomain composed of a globular head and a stem region where both of these regions carry N-linked oligosaccharide chains. Moreover, HA proteins have several N-glycosylation sites, however, not all sites are conserved in the influenza HA protein since some of these sites can also be found in other eukaryotic N-glycosylated proteins. Among these N-glycosylation sites, overlapping glycosylation sequons (OGS) can be detected in a majority of the influenza HA subtypes where it is found to be highly conserved through several generations of the influenza virus. In one aspect of our study, we established the significance of certain salt bridges found within HA that may have resulted in cross species infection of the H1N1 strain and the assembly of the novel 2013 H7N9 strain. In the second aspect of our study, we designed a potential tomato-produced influenza subunit vaccine that utilizes the oral mucosa and targets the influenza OGS. We were able to show that an OGS-containing chimeric protein can be produced from a tomato callus. The chimeric protein amount collected was dependent on how long the bombarded tomato calli was incubated in sterile water. We were able to vaccinate mice with the chimeric protein with the ideal protein vaccination concentration, however, we only detected low antibody amounts. We suspect that either the protein vaccination concentration is too low to induce high antibody response or the ELISA assay we developed was not so sensitive. We are currently optimizing both conditions.
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