1887

Abstract

The post-translational maturation of the fusion protein (F) of human respiratory syncytial virus was investigated. Chemical cross-linking experiments indicated that F forms homotetramers and provided evidence that the intermonomer contacts involve primarily the F subunit. Homooligomerization as measured by sedimentation in sucrose gradients was insensitive to carbonyl cyanide -chlorophenylhydrazone, indicating that it occurs in the endoplasmic reticulum. Cleavage of the F precursor to yield the F and F subunits was blocked by monensin or brefeldin A, indicating that it takes place in distal cisternae of the trans Golgi compartment or in the more distal trans Golgi network. The F precursor was not detected at the cell surface in surface immunoprecipitation experiments, indicating that cleavage is intracellular. The appearance of the cleaved F protein at the cell surface was concurrent with that of the attachment glycoprotein (G); this and other information indicated that the type 2 membrane orientation of G is not obligatorily associated with a reduced transit rate. Examination of F maturation in the presence of tunicamycin provided evidence that its expression at the cell surface depends upon cleavage and not directly upon glycosylation.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-72-12-3095
1991-12-01
2019-11-19
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-72-12-3095
Loading

Most Cited This Month

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error