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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Intracellular processing of measles virus fusion protein.

Intracellular processing of measles virus fusion (F) protein was studied by radiolabeling and immunoprecipitation with a monoclonal antibody against F protein. The cleavage of F protein into F1 and F2 subunits was complete after 5 hours of chase during which the growth of oligosaccharide chains on the F2 domain of F protein continued. The addition of terminal sialic acid conferred a strong negative charge on the F2 subunit. F protein expressed on the cell surface was removed by a fungal semi-alkaline protease, providing a method to follow the kinetics of its transport to the cell surface. The transport of the F protein was faster than that of the hemagglutinin (HA) protein. Uncleaved F protein, as well as cleaved subunits became digestible by the protease, indicating that a portion of the F protein reaches the cell surface uncleaved. The treatment of measles virus-infected cells with tunicamycin resulted in the synthesis of unglycosylated HA (65 kilodaltons, Kd) and F (48 Kd) proteins. Unglycosylated F protein was not cleaved into smaller subunits, nor was it transported to the cell surface. Unglycosylated HA protein likewise failed to reach the cell surface.[1]

References

  1. Intracellular processing of measles virus fusion protein. Sato, T.A., Kohama, T., Sugiura, A. Arch. Virol. (1988) [Pubmed]
 
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