RT Journal Article SR Electronic(1) A1 Palomo, Concepción A1 García-Barreno, Blanca A1 Peñas, Concepción A1 Melero, José A.YR 1991 T1 The G protein of human respiratory syncytial virus: significance of carbohydrate side-chains and the C-terminal end to its antigenicity JF Journal of General Virology, VO 72 IS 3 SP 669 OP 675 DO https://doi.org/10.1099/0022-1317-72-3-669 PB Microbiology Society, SN 1465-2099, AB 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., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-72-3-669