Modulation by glycosphingolipids of membrane-membrane interactions induced by myelin basic protein and melittin

Bruno Maggio, Robert K Yu

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

The effect of glycosphingolipids (GSLs) with oligosaccharide chains of different length and charge on membrane-membrane interactions induced by myelin basic protein (MBP) or melittin (Mel) was comparatively investigated with small unilamellar vesicles. MBP induces a fast vesicle aggregation and close membrane apposition. Merging of lipid bilayers and vesicle fusion induced by MBP are slower and less extensive processes compared to membrane apposition. The changes of membrane permeability concomitant to these phenomena are small. The Trp region of MBP remains in a rather polar environment when interacting with vesicles; its accessibility to NO3 or acrylamide quenching depends on the type of GSLs in the membrane. The Trp region of Mel is inserted more deeply into the lipid bilayer and its accessibility to the aqueous quenchers is less dependent on variations of the oligosaccharide chain of the GSLs. Mel induces a faster and more extensive membrane apposition and bilayer merging than does MBP. Extensive vesicle disruption occurs in the presence of Mel. Negatively charged GSLs facilitate membrane proximity and vesicle aggregation but an increase of the oligosaccharide chain length of either neutral or acidic GSLs decreases the interaction among vesicles that are induced by either protein. This effect is independent of the different mode of insertion of MBP and Mel into the membrane. Our results suggest that the modulation by the oligosaccharide chain on the protein-induced interactions between bilayers containing GSLs is probably exerted beyond the level of local molecular interactions between the basic proteins and the lipids.

Original languageEnglish (US)
Pages (from-to)105-114
Number of pages10
JournalBBA - Biomembranes
Volume1112
Issue number1
DOIs
StatePublished - Nov 23 1992

Fingerprint

Melitten
Glycosphingolipids
Myelin Basic Protein
Modulation
Membranes
Oligosaccharides
Lipid bilayers
Lipid Bilayers
Merging
Acidic Glycosphingolipids
Agglomeration
Neutral Glycosphingolipids
Unilamellar Liposomes
Proteins
Molecular interactions
Acrylamide
Chain length
Quenching
Permeability
Fusion reactions

Keywords

  • Ganglioside
  • Glycosphingolipid
  • Melittin
  • Membrane fusion
  • Myelin basic protein
  • Sulfatide

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

Cite this

Modulation by glycosphingolipids of membrane-membrane interactions induced by myelin basic protein and melittin. / Maggio, Bruno; Yu, Robert K.

In: BBA - Biomembranes, Vol. 1112, No. 1, 23.11.1992, p. 105-114.

Research output: Contribution to journalArticle

@article{aad4c4135a8a40dd8a273dab2ac888b4,
title = "Modulation by glycosphingolipids of membrane-membrane interactions induced by myelin basic protein and melittin",
abstract = "The effect of glycosphingolipids (GSLs) with oligosaccharide chains of different length and charge on membrane-membrane interactions induced by myelin basic protein (MBP) or melittin (Mel) was comparatively investigated with small unilamellar vesicles. MBP induces a fast vesicle aggregation and close membrane apposition. Merging of lipid bilayers and vesicle fusion induced by MBP are slower and less extensive processes compared to membrane apposition. The changes of membrane permeability concomitant to these phenomena are small. The Trp region of MBP remains in a rather polar environment when interacting with vesicles; its accessibility to NO3 or acrylamide quenching depends on the type of GSLs in the membrane. The Trp region of Mel is inserted more deeply into the lipid bilayer and its accessibility to the aqueous quenchers is less dependent on variations of the oligosaccharide chain of the GSLs. Mel induces a faster and more extensive membrane apposition and bilayer merging than does MBP. Extensive vesicle disruption occurs in the presence of Mel. Negatively charged GSLs facilitate membrane proximity and vesicle aggregation but an increase of the oligosaccharide chain length of either neutral or acidic GSLs decreases the interaction among vesicles that are induced by either protein. This effect is independent of the different mode of insertion of MBP and Mel into the membrane. Our results suggest that the modulation by the oligosaccharide chain on the protein-induced interactions between bilayers containing GSLs is probably exerted beyond the level of local molecular interactions between the basic proteins and the lipids.",
keywords = "Ganglioside, Glycosphingolipid, Melittin, Membrane fusion, Myelin basic protein, Sulfatide",
author = "Bruno Maggio and Yu, {Robert K}",
year = "1992",
month = "11",
day = "23",
doi = "10.1016/0005-2736(92)90260-S",
language = "English (US)",
volume = "1112",
pages = "105--114",
journal = "Biochimica et Biophysica Acta - Biomembranes",
issn = "0005-2736",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Modulation by glycosphingolipids of membrane-membrane interactions induced by myelin basic protein and melittin

AU - Maggio, Bruno

AU - Yu, Robert K

PY - 1992/11/23

Y1 - 1992/11/23

N2 - The effect of glycosphingolipids (GSLs) with oligosaccharide chains of different length and charge on membrane-membrane interactions induced by myelin basic protein (MBP) or melittin (Mel) was comparatively investigated with small unilamellar vesicles. MBP induces a fast vesicle aggregation and close membrane apposition. Merging of lipid bilayers and vesicle fusion induced by MBP are slower and less extensive processes compared to membrane apposition. The changes of membrane permeability concomitant to these phenomena are small. The Trp region of MBP remains in a rather polar environment when interacting with vesicles; its accessibility to NO3 or acrylamide quenching depends on the type of GSLs in the membrane. The Trp region of Mel is inserted more deeply into the lipid bilayer and its accessibility to the aqueous quenchers is less dependent on variations of the oligosaccharide chain of the GSLs. Mel induces a faster and more extensive membrane apposition and bilayer merging than does MBP. Extensive vesicle disruption occurs in the presence of Mel. Negatively charged GSLs facilitate membrane proximity and vesicle aggregation but an increase of the oligosaccharide chain length of either neutral or acidic GSLs decreases the interaction among vesicles that are induced by either protein. This effect is independent of the different mode of insertion of MBP and Mel into the membrane. Our results suggest that the modulation by the oligosaccharide chain on the protein-induced interactions between bilayers containing GSLs is probably exerted beyond the level of local molecular interactions between the basic proteins and the lipids.

AB - The effect of glycosphingolipids (GSLs) with oligosaccharide chains of different length and charge on membrane-membrane interactions induced by myelin basic protein (MBP) or melittin (Mel) was comparatively investigated with small unilamellar vesicles. MBP induces a fast vesicle aggregation and close membrane apposition. Merging of lipid bilayers and vesicle fusion induced by MBP are slower and less extensive processes compared to membrane apposition. The changes of membrane permeability concomitant to these phenomena are small. The Trp region of MBP remains in a rather polar environment when interacting with vesicles; its accessibility to NO3 or acrylamide quenching depends on the type of GSLs in the membrane. The Trp region of Mel is inserted more deeply into the lipid bilayer and its accessibility to the aqueous quenchers is less dependent on variations of the oligosaccharide chain of the GSLs. Mel induces a faster and more extensive membrane apposition and bilayer merging than does MBP. Extensive vesicle disruption occurs in the presence of Mel. Negatively charged GSLs facilitate membrane proximity and vesicle aggregation but an increase of the oligosaccharide chain length of either neutral or acidic GSLs decreases the interaction among vesicles that are induced by either protein. This effect is independent of the different mode of insertion of MBP and Mel into the membrane. Our results suggest that the modulation by the oligosaccharide chain on the protein-induced interactions between bilayers containing GSLs is probably exerted beyond the level of local molecular interactions between the basic proteins and the lipids.

KW - Ganglioside

KW - Glycosphingolipid

KW - Melittin

KW - Membrane fusion

KW - Myelin basic protein

KW - Sulfatide

UR - http://www.scopus.com/inward/record.url?scp=0026495315&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026495315&partnerID=8YFLogxK

U2 - 10.1016/0005-2736(92)90260-S

DO - 10.1016/0005-2736(92)90260-S

M3 - Article

VL - 1112

SP - 105

EP - 114

JO - Biochimica et Biophysica Acta - Biomembranes

JF - Biochimica et Biophysica Acta - Biomembranes

SN - 0005-2736

IS - 1

ER -