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Atomic Force Microscopy

Atomic Force Microscopy

Atomic force microscopy (AFM) is a type of scanning probe microscopy that can analyze topographic details of various specimens like ceramics, glass, polymers, and biological samples. AFM offers over 1000 times more resolution than the optical imaging system. Images generated from AFM are three-dimensional surface profiles, offering an advantage over the flat, two-dimensional images from other imaging techniques.
The AFM Probe
The probe is regarded as the heart of any AFM setup and comprises the...

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Updated: Jun 4, 2025

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Published on: December 20, 2013

Probing SARS-CoV-2 membrane binding peptide via single-molecule AFM-based force spectroscopy.

Qingrong Zhang¹, Raissa S L Rosa², Ankita Ray¹

¹Louvain Institute of Biomolecular Science and Technology, Université catholique de Louvain, Croix du sud 4-5, L7.07.07, Louvain-la-Neuve, Belgium.

Nature Communications

|January 2, 2025

Summary

This summary is machine-generated.

The SARS-CoV-2 spike protein’s membrane-binding peptide (MBP) binds to cholesterol-rich cell membranes. Stabilizing this peptide’s disulfide bridge enhances viral entry, suggesting new therapeutic targets.

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Last Updated: Jun 4, 2025

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Published on: February 27, 2015

Area of Science:

Virology
Structural Biology
Biochemistry

Background:

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein mediates viral entry by fusing with host cell membranes.
A membrane-binding peptide (MBP) near the TMPRSS2 cleavage site is crucial for this process.
Understanding the MBP's interaction with host membranes is key to identifying viral entry mechanisms.

Purpose of the Study:

To investigate the interaction of the SARS-CoV-2 spike protein's MBP with host cell membranes.
To determine the role of membrane composition, specifically cholesterol, in viral entry.
To elucidate the structural contribution of the MBP's disulfide bridge to membrane binding and viral infectivity.

Main Methods:

In vitro binding assays to study MBP-membrane interactions.
Computational modeling to analyze peptide-membrane dynamics.
Cholesterol depletion experiments to assess its impact on viral infectivity.
Analysis of both primed (TMPRSS2-cleaved) and unprimed MBP variants.

Main Results:

The MBP preferentially binds to cholesterol-rich membranes.
Cholesterol depletion significantly reduces SARS-CoV-2 infectivity.
The conserved disulfide bridge within the MBP stabilizes its membrane interaction.
The disulfide bridge plays a structural role in facilitating viral entry.

Conclusions:

Host cell membrane cholesterol content is critical for SARS-CoV-2 infectivity.
The MBP's disulfide bridge is a key structural element for membrane binding and viral entry.
Targeting the MBP disulfide bridge represents a potential therapeutic strategy to inhibit SARS-CoV-2 infection.