1989 Fiscal Year Final Research Report Summary
Study on Human Cytomegalovirus Proteins - specifically on 65 kDa protein -
| Project/Area Number |
63570214
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Virology
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| Research Institution | Kanazawa Medical University |
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Principal Investigator |
FURUKAWA Toru Kanazawa Medical University, Dept. of Microbiology, Professor., 医学部, 教授 (00148157)
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| Co-Investigator(Kenkyū-buntansha) |
ISHIDA Keiko Kanazawa Medical University, Dept. of Microbiology, Assistant., 医学部, 助手 (90158965)
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| Project Period (FY) |
1988 – 1989
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| Keywords | HCMV, Protein / HCMV Fc Receptor / HCMV BETA_2m Receptor |
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| Research Abstract |
The 65 kDa HCMV protein has been considered a constitute of the virion tegument, a poorly defined area located between the capsid and the outer membrane.
The study toward analysis of antigenicity of the 65 kDa protein during 2 years has revealed the results as follows.
1. Immunofluorescence assay using monospecific and monoclonal antibodies to the 65 kDa protein was carried out to monitor the expression of this protein in infected cells. Regardless of differences in the reactivity of the monoclonal antibodies, all stained cytoplasmic inclusion bodies localized to the site of the HCMV induced receptor for the Fc portion of IgG, suggesting that of the 65 kDa colocalized with HCMV induced FcR and had several different antigenic determinants.
2. FcR species of 130, 65, 50 and 36 kDa proteins were found to mediate the binding of IgG. The specificity of binding with of the 65 kDa with IgG Fc were confirmed by the blocking experiments.
3. We investigated the relationship between IgG FcR induced by HCMV and B_2 microglobulin receptor on the 65 kDa protein. Digestion of the 65 kDa protein with SV-8 protease generated six peptides. Monoclonal and monospecific antibodies to the 65 kDa were used to map the antigenic determinants on the digested peptides. Peptides with kDa of 33, 32 and 28 on which IgG FcR existed could also be bound by B_2m suggesting that B_2m shares the same binding sites with IgG Fc.
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