2020 Fiscal Year Annual Research Report
Direct visualization of conformational dynamics of hemagglutinin and interaction between hemagglutinin and exosomes using high-speed atomic force microscopy.
| Project/Area Number |
19K23841
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| Research Institution | Kanazawa University |
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Principal Investigator |
LIM KEE・SIANG 金沢大学, ナノ生命科学研究所, 特任助教 (60842987)
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| Project Period (FY) |
2019-08-30 – 2021-03-31
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| Keywords | Hemagglutinin / Influenza A / viral fusion protein / HS-AFM |
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| Outline of Annual Research Achievements |
In summary, study aims have been achieved. The native conformation of human influenza A hemagglutinin (HA) observed using HS-AFM is ellipsoidal, and it undergoes fusogenic transition in acidic condition to become Y-shape. Direct real-time observation of fusogenic transition suggests that the transition mechanism is likely to fit to the Uncaging Model. HA-exosome interaction is weak in neutral condition but firm in acidic condition. The weak interaction could be mediated by HA-receptor (sialic acid) interaction. In contrast, the firm interaction implies that HA fusion peptide could be released after fusogenic transition, and then inserted into exosomal layer, resulted deformation or rupture of exosomes.
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