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Membrane Carbohydrates

Membrane Carbohydrates

The plasma membrane is a dynamic barrier composed of lipids, proteins, and carbohydrates. It is the epicenter of many cellular processes required for cell growth and survival. Carbohydrates have unique structural and chemical properties that help the plasma membrane to carry out its functions effectively.
Membrane carbohydrates do not have any hydrophobic region and are exclusively located on the cell's outer surface. The addition of sugar molecules or glycosylation of proteins happens in...

Membrane Carbohydrates

Membrane Carbohydrates

The plasma membrane is a dynamic barrier composed of lipids, proteins, and carbohydrates. It is the epicenter of many cellular processes required for cell growth and survival. Carbohydrates have unique structural and chemical properties that help the plasma membrane to carry out its functions effectively.
Membrane carbohydrates do not have any hydrophobic region and are exclusively located on the cell's outer surface. The addition of sugar molecules or glycosylation of proteins happens in...

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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...

Multi-pass Transmembrane Proteins and β-barrels

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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
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Asymmetric Lipid Bilayer

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Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...

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The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
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Related Experiment Video

Updated: Jun 18, 2026

Analysis of SCAP N-glycosylation and Trafficking in Human Cells

Analysis of SCAP N-glycosylation and Trafficking in Human Cells

Published on: November 8, 2016

Globotriaosyl ceramide receptor function - where membrane structure and pathology intersect.

C A Lingwood¹, B Binnington, A Manis

¹Research Institute, Division of Molecular Structure and Function, The Hospital for Sick Children, Toronto, Ontario, Canada. cling@sickkids.ca

|December 2, 2009

Summary

Globotriaosyl ceramide (Gb(3)) acts as a receptor for verotoxins and HIV. Its organization in lipid rafts is key to hemolytic uremic syndrome and HIV infection, influencing disease outcomes.

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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

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Analysis of SCAP N-glycosylation and Trafficking in Human Cells

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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

Area of Science:

Biochemistry
Cell Biology
Immunology

Background:

Globotriaosyl ceramide (Gb(3)), also known as CD77 or the P(k) blood group antigen, is a glycosphingolipid.
Gb(3) serves as a crucial receptor for verotoxins (VT) and the HIV adhesin gp120.
The lipid rafts, which are ordered membrane domains, are central to the pathologies of VT-induced hemolytic uremic syndrome (HUS) and HIV infection.

Purpose of the Study:

To investigate the role of Gb(3) organization within lipid rafts in HUS and HIV infection.
To explore how fatty acid heterogeneity of Gb(3) influences its assembly into ordered membrane domains.
To determine the differential binding of verotoxins and gp120 to Gb(3) isoforms and its pathogenic implications.

Main Methods:

Utilized model and cell membranes to study Gb(3) organization and lipid raft assembly.
Analyzed the fatty acid composition of Gb(3) and its impact on membrane domain formation.
Investigated the binding interactions of verotoxins and gp120 with different Gb(3) isoforms.

Main Results:

Gb(3) organization into lipid rafts is critical for both HUS and HIV pathogenesis.
Fatty acid heterogeneity within Gb(3) dictates its incorporation into specific membrane domains.
Differential binding of VT and gp120 to Gb(3) isoforms suggests a role in determining disease outcome.
Membrane Gb(3) organization may serve as a predictor for tissue-specific pathology in HUS.

Conclusions:

Gb(3) organization within lipid rafts is a key determinant in HUS and HIV pathogenesis.
The specific fatty acid composition of Gb(3) influences its role in membrane organization and pathogen binding.
Understanding Gb(3) membrane dynamics offers insights into tissue tropism and disease progression in HUS and HIV infection.