Viral load appears to drive disease manifestations in humans with RSV infection. The observed parallel viral and disease kinetics support a potential clinical benefit of RSV antivirals. This reproducible model facilitates the development of future RSV therapeutics.

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Monoclonal antibodies (MAbs) against the rubella virion were used to locate epitopes involved in hemagglutination and neutralization. The MAbs exhibiting high-level hemagglutination-inhibiting activity were shown by Western blot analysis to be specific for the El polypeptide; this is consistent with the presence of the hemagglutinin on the El polypeptide. Some of the El-specific MAbs also neutralized viral infectivity. However, hemagglutination-inhibiting activity and neutralizing activity did not always correlate. Three distinct functional epitopes were identified on the El polypeptide by competition analyses: (i) one which reacted with MAbs with high-level hemagglutination-inhibiting activity and with neutralizing activity, (ii) one which reacted with MAbs with low-level hemagglutination-inhibiting activity and with neutralizing activity, and (iii) one which reacted with MAbs with only hemagglutination-inhibiting activity. A MAb specific for the E2 polypeptide exhibited neutralizing activity. This E2-specific MAb and two El-specific MAbs with neutralizing activity were capable of precipitating intact virus which indicates that at least three epitopes involved in neutralization are accessible on the surface of the virion.

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Titers of antibody to rubella virus in 68 human sera were compared by hemagglutination inhibition and enzyme-linked immunosorbent assay (ELISA). In general, the titers measured by ELISA were higher than those found by hemagglutination inhibition. Although the titers differed, the two methods showed parallel trends. Use of purified rubella virus and addition of 1% bovine serum albumin to the test wash solution aided in reducing false-positive titers in ELISA.