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A morphological study of the M-protein of Sendai virus
Abstract:
A purification scheme is described for the M-protein of Sendai virus and an electron microscope study of the isolated protein is presented. The protein exists as subunits of 6 nm in diam., which possess a central hole; the subunits may be dimers of the polypeptide. They are able to form filamentous aggregates which wind around one another to form a helical structure. It is suggested that these filaments may be the form adopted by the protein in the virus, the filaments lying parallel to one another just beneath the virus membrane to form a shell, but that the helical form is likely to be a property only of the isolated protein.
Insights
Researchers purified and studied Sendai virus M-protein. Isolated M-protein forms helical filaments, suggesting a structural role beneath the virus membrane.
Area of Science:
- Virology
- Structural Biology
- Protein Biochemistry
Background:
- Sendai virus is an important paramyxovirus.
- The M-protein's structure and function within the virus are not fully understood.
Purpose of the Study:
- To purify and characterize the M-protein of Sendai virus.
- To investigate the structural properties of the isolated M-protein using electron microscopy.
Main Methods:
- Purification of Sendai virus M-protein.
- Electron microscopy of purified M-protein.
Main Results:
- Purified M-protein consists of 6 nm diameter subunits with a central hole.
- Subunits may represent polypeptide dimers.
- M-protein subunits self-assemble into filamentous aggregates.
- These filaments can form helical structures.
- Filaments may lie parallel beneath the virus membrane in the intact virus, forming a shell.
Conclusions:
- The M-protein of Sendai virus has been successfully purified.
- Isolated M-protein exhibits a propensity to form helical filamentous structures.
- These findings suggest a potential structural role for M-protein filaments within the virus, possibly forming a shell beneath the membrane.