Vaccinia virus recombinants expressing either wild-type or mutant forms of human respiratory syncytial (RS) virus (Long strain) fusion (F) glycoprotein were obtained. Proteolytic processing of the precursor, F, and cell surface transport of the F glycoprotein were unaffected in the recombinants, except in those that contained the replacement Phe → Ser at position 237 of the F subunit. In recombinants containing this mutation, either alone or in combination with others, the traffic of the F molecule was arrested at some intermediate step of its transport to the cell surface and, consequently, the endoproteolytic cleavage of the F precursor was inhibited. Immunofluorescence staining of infected cells and endoglycosidase H (Endo-H) sensitivity assays indicated that the arrest occurred before the mid-Golgi compartment. Dimerization and folding of the F protein were also affected by the Phe → Ser substitution. Other amino acid replacements at positions 236 or 237 of the F subunit had various effects upon F maturation. These results are discussed in terms of the maturation requirements for the RS virus F molecule.


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