%0 Journal Article %A Palomo, Concepción %A García-Barreno, Blanca %A Peñas, Concepción %A Melero, José A. %T The G protein of human respiratory syncytial virus: significance of carbohydrate side-chains and the C-terminal end to its antigenicity %D 1991 %J Journal of General Virology, %V 72 %N 3 %P 669-675 %@ 1465-2099 %R https://doi.org/10.1099/0022-1317-72-3-669 %I Microbiology Society, %X The reactivities of eighteen monoclonal antibodies with different glycosylated forms of the human respiratory syncytial (RS) virus G protein were tested in Western blots. Only five antibodies recognized the unglycosylated precursor. The majority of antibodies, however, reacted with the O-glycosylated form of the G protein, emphasizing the importance of this type of modification for the antigenicity of the mature molecule. Human antisera, which recognized the RS virus G protein in Western blots, failed to inhibit the binding of anti-G antibodies to the virus but inhibited the binding of anti-F antibodies in the same type of assay. The human antibodies, however, did not recognize the G protein of some neutralization-resistant mutants selected with one anti-G monoclonal antibody. These mutants contain drastic amino acid sequence changes in the C-terminal end of the G molecule. The results are discussed in terms of the G protein antigenic structure. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-72-3-669