| Summary: | 碩士 === 國立中正大學 === 分子生物研究所 === 91 === Many animal viruses take advantage of receptor-mediated endocytosis to enter their host cells. The receptor of human JC virus (JCV) has been described as a glycoprotein containing terminal α2-6-linked sialic acid. After the first step of attachment, JCV enters cells by clathrin-coated vesicles. Although the binding receptor on the cell membrane was proven, the interaction domains on JCV are unknown. VP1 is the major structural protein of JCV and 360 copies of VP1 monomer can self-assemble into a virus-like particle (VLP). VLPs have hemagglutination activity like virions. The BC、DE、HI loops of VP1 are on the surface of the virus capsid that may participate in the interaction with cellular receptor. In order to investigate the interaction domains of JCV VLP, BC、DE and HI loops of JCV VP1 were replaced with that of SV40 VP1. After replacement, six recombinant chimeric VP1s, JCVP1SVBC、JCVP1SVDE、JCVP1SVHI、SVP1JCBC、SVP1JCDE、SVP1JCHI, were expressed in yeast. The chimeric VLPs purified from yeast were used for hemagglutination assay and cell binding assay. The results showed that the hemagglutination activity and the efficiency of cell entry of JCVP1SVHI VLP were drastically decreased. These results indicate that HI loop on JCV VP1 may play a role in interacting with the cellular receptor for viral infection.
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