AFRICAN SWINE FEVER VIRUS ATTACHMENT PROTEIN

被引:43
作者
CARRASCOSA, AL [1 ]
SASTRE, I [1 ]
VINUELA, E [1 ]
机构
[1] UNIV AUTONOMA MADRID, FAC CIENCIAS, CSIC, CTR BIOL MOLEC, CANTO BLANCO, E-28049 MADRID, SPAIN
关键词
D O I
10.1128/JVI.65.5.2283-2289.1991
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Treatment of African swine fever virus particles with nonionic detergents released proteins p35, p17, p14, and p12 from the virion. Of these proteins, only p12 bound to virus-sensitive Vero cells but not to virus-resistant L or IBRS2 cells. The binding of p12 was abolished by whole African swine fever virus and not by similar concentrations of subviral particles that lacked the external proteins. A monoclonal antibody (24BB7) specific for p12 precipitated a protein that, when analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence of 2-mercaptoethanol, showed a molecular mass of 17 kDa (p17*) instead of 12 kDa as found in the presence of 2-mercaptoethanol. The relationship between these two proteins was confirmed by the conversion of p17* to p12 when the former was isolated from polyacrylamide gels in the absence of 2-mercaptoethanol and subsequently treated with the reducing agent. The supernatant obtained after immunoprecipitation with the p12-specific antibody lacked the virus-binding protein.
引用
收藏
页码:2283 / 2289
页数:7
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