THE PURIFICATION OF 4 RESPIRATORY SYNCYTIAL VIRUS PROTEINS AND THEIR EVALUATION AS PROTECTIVE AGENTS AGAINST EXPERIMENTAL-INFECTION IN BALB/C MICE
THE PURIFICATION OF 4 RESPIRATORY SYNCYTIAL VIRUS PROTEINS AND THEIR EVALUATION AS PROTECTIVE AGENTS AGAINST EXPERIMENTAL-INFECTION IN BALB/C MICE
复制标题
DOI:
10.1099/0022-1317-69-2-293
复制
发表时间:
1988-02-01
影响因子:
3.8
通讯作者:
TOMS, GL
中科院分区:
文献类型:
--
作者:
ROUTLEDGE, EG;WILLCOCKS, MM;TOMS, GL
The fusion (F) glycoprotein, large-glyco- (G) protein, phospho- (P) protein and 22K protein of respiratory syncytial (RS) virus A2 strain were purified by a combination of immunoaffinity adsorption and preparative SDS-PAGE. All four proteins elicited serum antibody in mice after repeated inoculation in adjuvant, although the magnitude of the response as measured by ELISA varied from mouse to mouse. The F protein generated neutralizing antibodies in only 50% of the mice determined to be seropositive by ELISA. The G protein also induced neutralizing antibodies but in this instance neutralization tests and ELISA titres were more closely correlated. No neutralizing activity was detected in mice immunized with the P or 22K proteins although all produced antibody detectable by ELISA. Mice immunized with either the F or the G protein were found to be protected against subsequent RS virus challenge, whether they had developed neutralizing antibody or not. Mice inoculated with the P or 22K proteins were not protected.