通过氨基酸序列比对在两种锥虫表面糖蛋白中检测到的结构保守性。

Conservation of structure detected in two trypanosome surface glycoproteins by amino acid sequence alignment.

作者信息

Barbet A F

出版信息

Mol Biochem Parasitol. 1985 Feb;14(2):175-85. doi: 10.1016/0166-6851(85)90036-2.

Abstract

The predominant molecule exposed to antibody on the surface of Trypanosoma brucei is a glycoprotein of about 60 000 molecular weight which varies in amino acid sequence. The complete sequences of two such variable surface glycoproteins (VSGs) from randomly isolated, different antigenic types of trypanosomes were compared by amino acid sequence alignment. Homologous sequences were found distributed over various regions of the VSGs. Particularly good homology was observed between residues 16-34, 91-115, 177-194 and 254-345 from the N-terminus, in addition to the known conserved region close to the C-terminus. Homology was also demonstrated in the corresponding regions of the cDNA sequences by matrix analysis.

摘要

布氏锥虫表面与抗体接触的主要分子是一种分子量约为60000的糖蛋白，其氨基酸序列存在差异。通过氨基酸序列比对，比较了从随机分离的不同抗原类型锥虫中获得的两种此类可变表面糖蛋白（VSG）的完整序列。发现同源序列分布在VSG的各个区域。除了靠近C端的已知保守区域外，在N端的16 - 34、91 - 115、177 - 194和254 - 345位残基之间观察到特别好的同源性。通过矩阵分析在cDNA序列的相应区域也证实了同源性。