Journal Article

PUBDB-2015-01287

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Carbohydrate Conformation and Lipid Condensation in Monolayers Containing Glycosphingolipid Gb3: Influence of Acyl Chain Structure

Watkins, E. (Corresponding Author) ; Gao, H.>Extern* ; Dennison, A. C. ; Chopin, N. ; Struth, B.DESY* ; Arnold, T. ; Florent, J.-C. ; Johannes, L.>Extern*

2014
Rockefeller Univ. Press New York, NY

This record in other databases:      

Please use a persistent id in citations: doi:10.1016/j.bpj.2014.07.023

Abstract: Globotriaosylceramide (Gb3), a glycosphingolipid found in the plasma membrane of animal cells, is the endocytic receptor of the bacterial Shiga toxin. Using x-ray reflectivity (XR) and grazing incidence x-ray diffraction (GIXD), lipid monolayers containing Gb3 were investigated at the air-water interface. XR probed Gb3 carbohydrate conformation normal to the interface, whereas GIXD precisely characterized Gb3’s influence on acyl chain in-plane packing and area per molecule (APM). Two phospholipids, 1,2-distearoyl-sn-glycero-3-phosphocholine (DSPC) and 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine (DPPE), were used to study Gb3 packing in different lipid environments. Furthermore, the impact on monolayer structure of a naturally extracted Gb3 mixture was compared to synthetic Gb3 species with uniquely defined acyl chain structures. XR results showed that lipid environment and Gb3 acyl chain structure impact carbohydrate conformation with greater solvent accessibility observed for smaller phospholipid headgroups and long Gb3 acyl chains. In general, GIXD showed that Gb3 condensed phospholipid packing resulting in smaller APM than predicted by ideal mixing. Gb3’s capacity to condense APM was larger for DSPC monolayers and exhibited different dependencies on acyl chain structure depending on the lipid environment. The interplay between Gb3-induced changes in lipid packing and the lipid environment’s impact on carbohydrate conformation has broad implications for glycosphingolipid macromolecule recognition and ligand binding.

Note: (c) by the Biophysical Society. Post referee full text in progress.

---

Contributing Institute(s):

1. FS-Photon Science (FS-PS)
2. DOOR-User (DOOR)

Research Program(s):

1. DORIS Beamline BW1 (POF2-54G13) (POF2-54G13)
2. GALECTCOMPART - Endocytic Membrane Compartmentalization by Galectins (340485) (340485)

Experiment(s):

1. DORIS Beamline BW1 (DORIS III)

Appears in the scientific report 2014

---

Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

---