Structure and interaction analysis of GPI-related glycans

2014 Fiscal Year Final Research Report

• Project/Area Number: 24710257
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Living organism molecular science
• Research Institution: Osaka University (2013-2014); The Institute of Physical and Chemical Research (2012)
• Principal Investigator: HANASHIMA Shinya 大阪大学, 理学(系)研究科(研究院), 講師 (50373353)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: 糖鎖 / NMR / タンパク質

Outline of Final Research Achievements

We studied structures and a glycan-protein complex of functionally unknown GPI- related glycans and proteins through a combination of chemical and structural biological techniques. We chemically synthesized a series of truncated GPI-glycan structures. Enzymatic assay using the synthetic glycan units, human PGAP5, relates to GPI biological synthesis and ER-Golgi transport, requires full 5 sugar sequences for the substrate recognition. Our NMR study revealed that Mycobacterium phosphatidyl inositol glycan PIM is recognized by human lectin ZG16p which abundantly present around mucosa at intestine. Our finding suggests a new defense mechanism through mucosal immune responses.

Free Research Field

生物有機化学