A panel of 19 monoclonal antibodies (MAbs) were used to probe the antigenic relationships between the G (attachment) proteins of A and B respiratory syncytial virus (RSV) subtypes (G and G). At least three and two antigenic sites were present on G and G, respectively, including a shared neutralizing site. Most of the antibodies had some degree of complement-independent neutralizing capacity, but in common was a large neutralization-resistant fraction of virus (range 13 to 78%). Passive administration of MAbs to the cross-reactive antigenic site reduced pulmonary virus titres of both A and B subtype virus in the cotton rat model. Protection with subtype-specific MAbs, however, did not always correlate with neutralizing capacity. The cross-reactive antigenic site appears to be stable to denaturation by polyacrylamide gel electrophoresis and is present on the unglycosylated and partially glycosylated forms of G and G by Western blot analysis of infected cell lysates.


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