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Oligomerization of Friend spleen focus-forming virus (SFFV) env glycoproteins
1Department of Genetics, University of Tokyo, Japan.
Abstract:
The glycoprotein gp55 and its processed form gp65, which are encoded by the env gene of Friend spleen focus-forming virus (SFFV), have been implicated in the initiation of the murine acute erythroleukemia induced by Friend virus (FV). Analyses of these glycoproteins by chemical crosslinking and nonreducing/reducing two-dimensional electrophoresis showed that both gp55 and gp65 exist as monomer and disulfide-bonded dimer and trimer. These oligomers could be detected in various FV-infected erythroleukemia cell lines, as well as in the spleen cells of FV-induced erythroleukemic mice, suggesting that oligomerization is an intrinsic feature of SFFV env glycoproteins.
Insights
Friend spleen focus-forming virus (SFFV) glycoproteins gp55 and gp65 form monomers, dimers, and trimers. This oligomerization is intrinsic to SFFV env glycoproteins and implicated in murine erythroleukemia.
Area of Science:
- Virology
- Molecular Biology
- Oncology
Background:
- Friend spleen focus-forming virus (SFFV) causes murine acute erythroleukemia.
- The SFFV env gene encodes glycoproteins gp55 and gp65, implicated in disease initiation.
Purpose of the Study:
- To investigate the oligomeric state of SFFV env glycoproteins gp55 and gp65.
- To determine if glycoprotein oligomerization is an intrinsic feature of SFFV env.
Main Methods:
- Chemical crosslinking was used to analyze SFFV glycoproteins.
- Nonreducing/reducing two-dimensional electrophoresis identified glycoprotein forms.
Main Results:
- Both gp55 and gp65 exist as monomers and disulfide-bonded dimers and trimers.
- These oligomers were detected in FV-infected cell lines and spleen cells of affected mice.
Conclusions:
- Oligomerization is an intrinsic characteristic of SFFV env glycoproteins.
- Glycoprotein oligomerization may play a role in the initiation of Friend virus-induced erythroleukemia.