%0 Journal Article %A Walsh, Edward E. %A Falsey, Ann R. %A Sullender, Wayne M. %T Monoclonal antibody neutralization escape mutants of respiratory syncytial virus with unique alterations in the attachment (G) protein. %D 1998 %J Journal of General Virology, %V 79 %N 3 %P 479-487 %@ 1465-2099 %R https://doi.org/10.1099/0022-1317-79-3-479 %I Microbiology Society, %X Five monoclonal antibody (MAb) neutralization escape mutants of respiratory syncytial virus (RSV) were produced by growing the Long strain RSV (group A virus) in the presence of a neutralizing, group cross-reactive MAb specific for the attachment protein (G). Four viruses (RSV-2, −6, −14 and −15) had amino acid replacements clustered within a highly conserved centrally located 13 amino acid region (position 164–176). Reactivity with group A- specific MAbs and with polyclonal anti-G serum was maintained and growth kinetics were unaffected. An additional virus (RSV-3) had four amino acid substitutions in the cytoplasmic tail and transmembrane region of G, and had restricted growth and formed small syncytia. Immunofluorescent and Western blot analysis indicated that G protein was not membrane associated and had reduced incorporation into the virion, thereby escaping neutralization by L9 and polyclonal anti-G serum. The predominant form of G produced by RSV-3 was found in infected cell supernatants, consistent with the size of secreted G. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-79-3-479