A method for detecting natural selection at single amino acid substitutions and its applications
| Project/Area Number |
26650134
|
|---|
| Research Category |
Grant-in-Aid for Challenging Exploratory Research
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
Evolutionary biology
|
|---|
| Research Institution | Nagoya City University |
|---|
Principal Investigator |
SUZUKI YOSHIYUKI 名古屋市立大学, 大学院システム自然科学研究科, 教授 (70353430)
|
|---|
| Project Period (FY) |
2014-04-01 – 2016-03-31
|
| Project Status |
Completed (Fiscal Year 2015)
|
| Budget Amount *help |
¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2015: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2014: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
|
|---|
| Keywords | 分子進化 / 自然選択 / 同義置換 / 非同義置換 / インフルエンザウイルス / ヘマグルチニン / 免疫逃避 / 糖鎖 |
|---|
| Outline of Final Research Achievements |
In the present study, a method for detecting natural selection at single amino acid substitutions is developed and applied to infer the evolutionary mechanism operating on the change in the number of N-liked glycosylation sites in the hemagglutinin protein of H3N2 human influenza A virus. Positive selection is detected for the amino acid substitutions generating N-linked glycosylation sites, suggesting that N-linked glycans shield antigenic sites from immune responses. The method developed in the present study is applicable to a wide variety of evolutionary problems and the results obtained from the analysis of influenza A virus are useful for prophylaxis and treatment against influenza A virus.
|
Report
(3 results)
Research Products
(15 results)
-
[Journal Article] Comparison of the primary structures, cytotoxicities, and affinities to phospholipids of five kinds of cytotoxins from the venom of Indian cobra, Naja naja.2016
Author(s)
Suzuki-Matsubara, M., Athauda, S. B. P., Suzuki, Y., Matsubara, K. and Akihiko Moriyama, A.
-
Journal Title
Comparative Biochemistry and Physiology, Part C
Volume: 179
Pages: 158-164
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research / Acknowledgement Compliant
-
-
-
-
-
-
-
-
-
-
-
-
-
-
