TOXOPLASMA-GONDII STRUCTURE VARIATIONS OF THE ANTIGEN P-30

被引：5

作者：

BONHOMME, A ^{[1
]}

THIRION, C ^{[1
]}

BOULANGER, F ^{[1
]}

CHARTON, F ^{[1
]}

BURLET, H ^{[1
]}

PINON, JM ^{[1
]}

ALIX, AJP ^{[1
]}

机构：

[1] UNIV REIMS,CHU HOP MAISON BLANCHE,INSERM,U314,SPECT & STRUCT BIOMOLEC LAB,F-51092 REIMS,FRANCE

来源：

PARASITOLOGY | 1994年 / 108卷

关键词：

TOXOPLASMA GONDII; ANTIGEN P-30; CIRCULAR DICHROISM; MOLECULAR CONFORMATION;

D O I：

10.1017/S0031182000076125

中图分类号：

R38 [医学寄生虫学]; Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ; 100103 ;

摘要：

The major surface immunodominant antigen (P30) of Toxoplasma gondii was purified by two methods (i) SDS-PAGE and (ii) immunoaffinity chromatography. The secondary elements within this protein were assessed by circular dichroism and spectra obtained were compared to those proposed by Manavalan & Johnson (1983). The results allowed us to determine an all beta protein status for this antigen. This experimental result was in agreement with the predicted secondary structures deduced from the P30 primary sequence. Modifications in conformation according to pH and temperature were recorded without any change in immunoactivity. The epitope, which was always recognized by a monoclonal antibody against P30, could be a linear epitope.

引用

页码：281 / 287

页数：7

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