Evidence for cholera aggregation on GM1-decorated lipid bilayers

Rong Wang, Jeane Shi, Atul N. Parikh, Andrew P. Shreve, Liaohai Chen, Basil I. Swanson

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

The binding properties of cholera toxin B (CTB) oligomer to substrate supported membrane bilayer, containing physiologically relevant concentrations of receptor glycolipids, viz. monosialoganglioside (GM1), have been extensively studied by the atomic force microscopy (AFM). Two distinct classes of GM1 containing membrane-mimetic surfaces were prepared: supported lipid bilayer membranes (sBLMs) on freshly cleaved mica and hybrid lipid bilayer membranes (hBLMs) on octadecyltrichlorosilane (OTS) derivatized silicon substrates. On sBLMs, aggregates with a well-defined ordered arrangement of individual CTB molecules were observed at all GM1 and cholera concentrations studied. In sharp contrast, features consistent with randomly distributed adsorbed individual CTB molecules were seen on a bare mica surface. On the hBLMs, the aggregate structures were only observed when the bilayer was formed onto ordered OTS surfaces, offering continuous and defect-free lipid membrane for the lateral diffusion of GM1. Ill-packed and disordered OTS monolayers yielded a random distribution of adsorbed proteins comparable to that observed for CTB binding on bare mica substrates. These observations strongly support that the aggregation of CTB-GM1 complex is a result of the specific interaction of CTB molecules with GM1 receptors in the fluid membrane bilayers. The high mobility of GM1 allows lateral diffusion of the complex to form ordered aggregates.

Original languageEnglish (US)
Pages (from-to)45-51
Number of pages7
JournalColloids and Surfaces B: Biointerfaces
Volume33
Issue number1
DOIs
StatePublished - Jan 1 2004

Fingerprint

cholera
Lipid bilayers
Cholera
Cholera Toxin
Lipid Bilayers
lipids
Membrane Lipids
Agglomeration
membranes
Membranes
Mica
mica
Molecules
Substrates
Silicon
Atomic Force Microscopy
Oligomers
molecules
Monolayers
Atomic force microscopy

Keywords

  • Atomic force microscopy
  • Cholera toxin B oligomer
  • Protein aggregation

ASJC Scopus subject areas

  • Biotechnology
  • Colloid and Surface Chemistry
  • Physical and Theoretical Chemistry
  • Surfaces and Interfaces

Cite this

Wang, R., Shi, J., Parikh, A. N., Shreve, A. P., Chen, L., & Swanson, B. I. (2004). Evidence for cholera aggregation on GM1-decorated lipid bilayers. Colloids and Surfaces B: Biointerfaces, 33(1), 45-51. https://doi.org/10.1016/j.colsurfb.2003.09.001

Evidence for cholera aggregation on GM1-decorated lipid bilayers. / Wang, Rong; Shi, Jeane; Parikh, Atul N.; Shreve, Andrew P.; Chen, Liaohai; Swanson, Basil I.

In: Colloids and Surfaces B: Biointerfaces, Vol. 33, No. 1, 01.01.2004, p. 45-51.

Research output: Contribution to journalArticle

Wang, R, Shi, J, Parikh, AN, Shreve, AP, Chen, L & Swanson, BI 2004, 'Evidence for cholera aggregation on GM1-decorated lipid bilayers', Colloids and Surfaces B: Biointerfaces, vol. 33, no. 1, pp. 45-51. https://doi.org/10.1016/j.colsurfb.2003.09.001
Wang, Rong ; Shi, Jeane ; Parikh, Atul N. ; Shreve, Andrew P. ; Chen, Liaohai ; Swanson, Basil I. / Evidence for cholera aggregation on GM1-decorated lipid bilayers. In: Colloids and Surfaces B: Biointerfaces. 2004 ; Vol. 33, No. 1. pp. 45-51.
@article{87fd7296b53a4594979ce0d0348817ff,
title = "Evidence for cholera aggregation on GM1-decorated lipid bilayers",
abstract = "The binding properties of cholera toxin B (CTB) oligomer to substrate supported membrane bilayer, containing physiologically relevant concentrations of receptor glycolipids, viz. monosialoganglioside (GM1), have been extensively studied by the atomic force microscopy (AFM). Two distinct classes of GM1 containing membrane-mimetic surfaces were prepared: supported lipid bilayer membranes (sBLMs) on freshly cleaved mica and hybrid lipid bilayer membranes (hBLMs) on octadecyltrichlorosilane (OTS) derivatized silicon substrates. On sBLMs, aggregates with a well-defined ordered arrangement of individual CTB molecules were observed at all GM1 and cholera concentrations studied. In sharp contrast, features consistent with randomly distributed adsorbed individual CTB molecules were seen on a bare mica surface. On the hBLMs, the aggregate structures were only observed when the bilayer was formed onto ordered OTS surfaces, offering continuous and defect-free lipid membrane for the lateral diffusion of GM1. Ill-packed and disordered OTS monolayers yielded a random distribution of adsorbed proteins comparable to that observed for CTB binding on bare mica substrates. These observations strongly support that the aggregation of CTB-GM1 complex is a result of the specific interaction of CTB molecules with GM1 receptors in the fluid membrane bilayers. The high mobility of GM1 allows lateral diffusion of the complex to form ordered aggregates.",
keywords = "Atomic force microscopy, Cholera toxin B oligomer, Protein aggregation",
author = "Rong Wang and Jeane Shi and Parikh, {Atul N.} and Shreve, {Andrew P.} and Liaohai Chen and Swanson, {Basil I.}",
year = "2004",
month = "1",
day = "1",
doi = "10.1016/j.colsurfb.2003.09.001",
language = "English (US)",
volume = "33",
pages = "45--51",
journal = "Colloids and Surfaces B: Biointerfaces",
issn = "0927-7765",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Evidence for cholera aggregation on GM1-decorated lipid bilayers

AU - Wang, Rong

AU - Shi, Jeane

AU - Parikh, Atul N.

AU - Shreve, Andrew P.

AU - Chen, Liaohai

AU - Swanson, Basil I.

PY - 2004/1/1

Y1 - 2004/1/1

N2 - The binding properties of cholera toxin B (CTB) oligomer to substrate supported membrane bilayer, containing physiologically relevant concentrations of receptor glycolipids, viz. monosialoganglioside (GM1), have been extensively studied by the atomic force microscopy (AFM). Two distinct classes of GM1 containing membrane-mimetic surfaces were prepared: supported lipid bilayer membranes (sBLMs) on freshly cleaved mica and hybrid lipid bilayer membranes (hBLMs) on octadecyltrichlorosilane (OTS) derivatized silicon substrates. On sBLMs, aggregates with a well-defined ordered arrangement of individual CTB molecules were observed at all GM1 and cholera concentrations studied. In sharp contrast, features consistent with randomly distributed adsorbed individual CTB molecules were seen on a bare mica surface. On the hBLMs, the aggregate structures were only observed when the bilayer was formed onto ordered OTS surfaces, offering continuous and defect-free lipid membrane for the lateral diffusion of GM1. Ill-packed and disordered OTS monolayers yielded a random distribution of adsorbed proteins comparable to that observed for CTB binding on bare mica substrates. These observations strongly support that the aggregation of CTB-GM1 complex is a result of the specific interaction of CTB molecules with GM1 receptors in the fluid membrane bilayers. The high mobility of GM1 allows lateral diffusion of the complex to form ordered aggregates.

AB - The binding properties of cholera toxin B (CTB) oligomer to substrate supported membrane bilayer, containing physiologically relevant concentrations of receptor glycolipids, viz. monosialoganglioside (GM1), have been extensively studied by the atomic force microscopy (AFM). Two distinct classes of GM1 containing membrane-mimetic surfaces were prepared: supported lipid bilayer membranes (sBLMs) on freshly cleaved mica and hybrid lipid bilayer membranes (hBLMs) on octadecyltrichlorosilane (OTS) derivatized silicon substrates. On sBLMs, aggregates with a well-defined ordered arrangement of individual CTB molecules were observed at all GM1 and cholera concentrations studied. In sharp contrast, features consistent with randomly distributed adsorbed individual CTB molecules were seen on a bare mica surface. On the hBLMs, the aggregate structures were only observed when the bilayer was formed onto ordered OTS surfaces, offering continuous and defect-free lipid membrane for the lateral diffusion of GM1. Ill-packed and disordered OTS monolayers yielded a random distribution of adsorbed proteins comparable to that observed for CTB binding on bare mica substrates. These observations strongly support that the aggregation of CTB-GM1 complex is a result of the specific interaction of CTB molecules with GM1 receptors in the fluid membrane bilayers. The high mobility of GM1 allows lateral diffusion of the complex to form ordered aggregates.

KW - Atomic force microscopy

KW - Cholera toxin B oligomer

KW - Protein aggregation

UR - http://www.scopus.com/inward/record.url?scp=0346728764&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0346728764&partnerID=8YFLogxK

U2 - 10.1016/j.colsurfb.2003.09.001

DO - 10.1016/j.colsurfb.2003.09.001

M3 - Article

VL - 33

SP - 45

EP - 51

JO - Colloids and Surfaces B: Biointerfaces

JF - Colloids and Surfaces B: Biointerfaces

SN - 0927-7765

IS - 1

ER -