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Related Concept Videos

Viral Structure00:56

Viral Structure

Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
Inhibitors of Virion Maturation and Assembly01:19

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...

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Related Experiment Video

Updated: May 29, 2026

Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly
09:47

Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly

Published on: March 1, 2012

Applying Distinct CDMS Strategies to Observe Nonclassical Virus Capsid Assembly.

Lars Thiede1,2, Anisha Haris3, Tomislav Damjanović1,2

  • 1CSSB Centre for Structural Systems Biology, Deutsches Elektronen-Synchrotron DESY & Leibniz Institute of Virology (LIV) & University of Luebeck, Hamburg, Germany.

Journal of Mass Spectrometry : JMS
|May 28, 2026
PubMed
Summary
This summary is machine-generated.

Charge detection mass spectrometry (CDMS) accurately measured masses of human norovirus capsids. This study highlights CDMS capabilities for analyzing complex viral structures and reveals novel capsid assemblies.

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Related Experiment Videos

Last Updated: May 29, 2026

Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly
09:47

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Published on: March 1, 2012

Alternative In Vitro Methods for the Determination of Viral Capsid Structural Integrity
12:57

Alternative In Vitro Methods for the Determination of Viral Capsid Structural Integrity

Published on: November 16, 2017

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
09:08

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus

Published on: July 27, 2021

Area of Science:

  • Structural biology
  • Mass spectrometry
  • Virology

Background:

  • Conventional native mass spectrometry (MS) struggles with heterogeneous, high-mass samples like viral capsids, limiting accurate mass determination.
  • Charge detection mass spectrometry (CDMS) simultaneously measures mass-to-charge ratio (m/z) and charge (z), enabling analysis of complex biomolecules.
  • Human noroviruses form heterogeneous T=3 and T=4 capsids, posing challenges for precise structural characterization.

Purpose of the Study:

  • To compare the performance of two commercial CDMS systems (Orbitrap-based DMT and ELIT-based Xevo) for analyzing human norovirus capsids.
  • To investigate the structural heterogeneity and mass distribution of GI.1 Norwalk and GII.17 Kawasaki norovirus strains.
  • To identify potential nonclassical capsid assemblies and interactions affecting viral structure.

Main Methods:

  • Analysis of human norovirus capsids (GI.1 Norwalk and GII.17 Kawasaki) using Orbitrap-based Direct Mass Technology (DMT) and Xevo CDMS.
  • Comparison of experimental mass data with theoretical masses for T=3 and T=4 capsid structures.
  • Confirmation of structural findings using cryogenic electron microscopy (cryo-EM) and proteomics.

Main Results:

  • Both CDMS systems successfully determined similar masses for both norovirus strains.
  • GII.17 Kawasaki exhibited both T=3 and T=4 particles, with Xevo CDMS providing measurements closer to theoretical mass.
  • GII.17 Kawasaki displayed nonclassical mass distributions and an oval capsid shape, confirmed by cryo-EM. GI.1 Norwalk showed mass exceeding theoretical T=3 by 8-10%, potentially due to expression system protein interactions.

Conclusions:

  • CDMS is a powerful technique for characterizing heterogeneous viral capsids, with distinct instruments offering complementary data.
  • The study identified the first nonclassical capsid assembly in a GII.17 noroviral capsid, revealing an oval shape.
  • GI.1 Norwalk capsids may engage in interactions with expression system proteins, contributing to observed mass heterogeneity.