Mutations of respiratory syncytial virus attachment glycoprotein G associated with resistance to neutralization by primate polyclonal antibodies

Citation
Wm. Sullender et Kg. Edwards, Mutations of respiratory syncytial virus attachment glycoprotein G associated with resistance to neutralization by primate polyclonal antibodies, VIROLOGY, 264(1), 1999, pp. 230-236
Citations number
52
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Microbiology
Journal title
VIROLOGY
ISSN journal
0042-6822 → ACNP
Volume
264
Issue
1
Year of publication
1999
Pages
230 - 236
Database
ISI
SICI code
0042-6822(19991110)264:1<230:MORSVA>2.0.ZU;2-S
Abstract
The respiratory syncytial (RS) virus attachment glycoprotein G is a type II transmembrane glycoprotein and an important target of the host immune resp onse. Antigenic variability of the G protein is postulated to contribute to the ability of the virus to evade established immune responses. A glycopro tein G monospecific polyclonal antiserum from a nonhuman primate was used t o select for an antibody resistant RS virus. The mutant virus was resistant to neutralization by the selecting antiserum and by the sera from three ot her G-protein immunized primates. G-protein amino acid changes were found a t residues 61 (Phe to Leu), 174 (Ser to Cys), and 183 (Trp to Leu). Thus th e mutant protein had amino acid changes in the transmembrane domain (61) an d the central ectodomain (174 and 183). The change at amino acid 174 result ed in five rather than the usual four Cys found in the conserved central re gion of the ectodomain. These data demonstrate that an RS virus with resist ance to neutralization by polyclonal antibodies can be selected readily in cell culture. In addition, only a limited number of amino acid changes is r equired to produce the resistant phenotype. (C) 1999 Academic Press.