2011 Fiscal Year Final Research Report
New strategy for inhibition of HIV replication by targeting to NMT1 without appearance of drug resistant virus
| Project/Area Number |
22790130
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Environmental pharmacy
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| Research Institution | Kumamoto University |
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Principal Investigator |
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| Project Period (FY) |
2010 – 2011
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| Keywords | HIV-1 / NMT / 薬剤耐性 |
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| Research Abstract |
N-Myristoyltransferase(NMT) isozymes, i. e., NMT1 and NMT2, are essential host factors for the AIDS-causing human immunodeficiency virus type-1(HIV-1), by which the viral proteins Pr55(gag) and Nef are N-myristoylated. N-Myristoylation is important for the membrane targeting of modified proteins. Since it is predicted that approximately 0. 5% of all proteins in the human genome are N-myristoylated, selective inhibition of closely HIV-1-associated NMT isozymes is thought to be important for the improvement of specificity in the anti-HIV-1 strategy with the inhibition of NMT function. NMT isozymes contain two characteristic structures, the N-terminal region and the catalytic region. Here, it was shown that the N-terminal region of each NMT isozyme is required for isozyme-specific binding to the ribosome. The specific binding of each isozyme to the ribosome was associated with HIV-1 production, in which NMT1 and NMT2 in the ribosome were suggested to be mainly related to Pr55(gag) and Nef, respectively. These results indicate that the N-terminal region that mediates binding to the ribosome can become a target for NMT-isozyme-specific inhibition, which could block HIV-1 production.
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[Journal Article] Fluorescence imaging of potassium ions in living cells using a fluorescent probe based on a thrombin binding aptamer-peptide conjugate2012
Author(s)
Ohtsuka K, Sato S, Sato Y, Sota K, Ohzawa S, Matsuda T, Takemoto K, Takamune N, Juskowiak B, Nagai T, Takenaka S
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Journal Title
Chem. Commun
Volume: (in press)
Peer Reviewed
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