Open AccessFunctional identification of α1‐giardin as an annexin of Giardia lamblia
Author(s) -
Bauer Bettina,
Engelbrecht Siegfried,
BakkerGrunwald Tilly,
Scholze Henning
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13496.x
Subject(s) - giardia lamblia , annexin , molecular mass , peptide sequence , annexin a2 , annexin a5 , biology , biochemistry , amino acid , vesicle , sequence (biology) , microbiology and biotechnology , enzyme , genetics , in vitro , gene , membrane
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 α1‐giardin, a component of the ventral disc which, based on its predicted amino acid sequence, has been classified as annexin XIX. Purified α1‐giardin associated with multilamellar phosphatidyl serine‐containing vesicles in a Ca 2+ ‐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 Ca 2+ ‐binding sites, which, as in other annexins, are all located on the convex surface of the molecule, are of the low‐affinity type III.