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Characterization of a diagnostic Fab fragment binding trimeric Lewis X.
- Source :
- Proteins; Aug2009, Vol. 76 Issue 2, p439-447, 9p
- Publication Year :
- 2009
-
Abstract
- Lewis X trisaccharides normally function as essential cell-cell interaction mediators. However, oligomers of Lewis X trisaccharides expressed by the parasite Schistosoma mansoni seem to be related to its evasion of the immune response of its human host. Here we show that monoclonal antibody 54-5C10-A, which is used to diagnose schistosomiasis in humans, interacts with oligomers of at least three Lewis X trisaccharides, but not with monomeric Lewis X. We describe the sequence and the 2.5 Å crystal structure of its Fab fragment and infer a possible mode of binding of the polymeric Lewis X from docking studies. Our studies indicate a radically different mode of binding compared to Fab 291-2G3-A, which is specific for monomeric Lewis X, thus providing a structural explanation of the diagnostic success of 54-5C10-A. Proteins 2009. © 2008 Wiley-Liss, Inc. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 08873585
- Volume :
- 76
- Issue :
- 2
- Database :
- Complementary Index
- Journal :
- Proteins
- Publication Type :
- Academic Journal
- Accession number :
- 64229728
- Full Text :
- https://doi.org/10.1002/prot.22356