Functional identification of α1-giardin as an annexin of Giardia lamblia

被引:18
作者
Bauer, B [1 ]
Engelbrecht, S [1 ]
Bakker-Grunwald, T [1 ]
Scholze, H [1 ]
机构
[1] Univ Osnabruck, Dept Biol Chem, D-49069 Osnabruck, Germany
关键词
Giardia lamblia; giardin; annexin; calcium binding; phospholipid binding;
D O I
10.1016/S0378-1097(99)00064-6
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A protein with a relative molecular mass of 31 kDa was specifically extracted by EGTA from a detergent-insoluble fraction of Giardia lamblia. N-terminal sequencing showed this protein to be identical to alpha 1-giardin, a component of the ventral disc which, based on its predicted amino acid sequence, has been classified as annexin XIX. Purified alpha 1-giardin associated with multilamellar phosphatidyl serine-containing vesicles in a Ca2+-dependent manner, confirming that it is a functional annexin. Molecular modelling of the amino acid sequence of the giardial annexin into the X-ray structure of annexin V suggests that the Ca2+-binding sites, which, as in other annexins, are all located on the convex surface of the molecule, are of the low-affinity type III. (C) 1999 Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:147 / 153
页数:7
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