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J Gen Virol. 1991 Mar;72 ( Pt 3):669-75.

The G protein of human respiratory syncytial virus: significance of carbohydrate side-chains and the C-terminal end to its antigenicity.

Author information

1
Department of Molecular Biology, Centro Nacional de Microbiología, Madrid, Spain.

Abstract

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.

PMID:
2005433
DOI:
10.1099/0022-1317-72-3-669
[Indexed for MEDLINE]

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