2001 Fiscal Year Final Research Report Summary
Analysis of virus-receptor interaction and its application in veterinary science
| Project/Area Number |
11460148
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied veterinary science
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| Research Institution | National Institute of Neutoscience, NCNP |
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Principal Investigator |
TAGUCHI Fumihiro National Institute of Neuroscience, NCNP Section chief, 神経研究所, 室長 (30107429)
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| Co-Investigator(Kenkyū-buntansha) |
ITO Toshihiro Department of Veterinary Public Health, Faculty of Agriculture Tottori University, Professor, 農学部, 教授 (00176348)
OKAZAKI Katsunori Department of Disease Control, Faculty of Veterinary Medicine Hokkaido University, Accociate professor, 獣医学研究科, 助教授 (90160663)
MATSUYAMA Shutoku National Institute of Neuroscience, NCNP Postdoctral fellow, 神経研究所, 流動研究員
IKEDA Hidetoshi Laboratory of Virological Pproducts, National Institute of Animal Health Section chief, 動物衛生研究所, 室長
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| Project Period (FY) |
1999 – 2001
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| Keywords | virus-receptor interation / mouse hepatitis virus (MHV) / murine leukemia virus / influenza virus / ウシヘルペスウイルス |
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| Research Abstract |
We have investigated the interaction of mouse hepatitis virus (MHV) and its receptor CEACAM1 (MHVR) by using soluble form of MHVR (soMHVR). soMHVR1 derived from MHV-susceptible BALB/c mouse showed high affinity and neutralizing activity to MHV, while soMHVR2 isolated from MHV-resistant SJL mouse was low in affinity and neutralization activity. We have isolated mutant virus resistant to neutralization (srr7) by soMHVR1 from MHV-JHMV. Srr7 infected as efficiently as wild type JHMV to cells expressing MHVR1, but did more than 2 logs less efficiently than wt virus to cells expressing MHVR2.This inefficient infection of srr7 was revealed to be due to its low fusogenicity, namely low capability to enter into these cells. These results suggested that the binding ofMHVR2 to wild type S protein triggered its conformational change, while it failed to do so for srr7 S proteins. We have also found that soMHVR1 activated or potentiated MHV infection to MHVR-deficient cells. This implied that binding of soMHVR converted fusion-negative S protein to fusion-positive phenotype. Using this system, we can further investigate in cell-free system the interaction of MHV and receptor as well as dynamics MHV particles following its interaction with receptor. Env protein ofmurine leukemia virus Fv-4r plays an important role for the resistance of mice to various leukemia viruses. We have conferred the resistance against leukemia virus to otherwise susceptible mice by expressing Env using retrovirus vectors. We have developed a highly pathogenic influenza A virus by passaging an avirulent virus through chickens. This conversion was accompanied with the mutations in HA protein, which resulted in enhanced cleavability of the protein. This suggested that HA cleavability influenced the pathogenicity of influenza virus.
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