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1 University of Rochester, School of Medicine and Dentistry, Rochester, New York 14642
The2 Rochester General Hospital, Department of Medicine, 1425 Portland Avenue, Rochester, New York 14621
and3 Praxis Biologics, 30 Corporate Woods, Rochester, New York 14623, U.S.A.
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 (GA and GB). At least three and two antigenic sites were present on GA and GB, 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 in vitro 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 GA and GB by Western blot analysis of infected cell lysates.
Keywords: RSV, attachment protein, epitope mapping, animal protection
Received 14 February 1989;
accepted 9 July 1989.
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