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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
Intracellular Movement of Viruses and Bacteria01:10

Intracellular Movement of Viruses and Bacteria

Intracellular bacteria and viruses often comprise a group of highly infectious pathogens that can cause several diseases. Bacterial pathogens include those belonging to the genus Rickettsia responsible for conditions such as rocky mountain spotted fever and the Mediterranean spotted fever; Chlamydia, a genus responsible for a sexually transmitted disease; Coxiella burnetii, an agent responsible for Q fever. Viral pathogens include vaccinia—a poxvirus, and herpes simplex virus—a virus that...
Precipitate Formation and Particle Size Control01:16

Precipitate Formation and Particle Size Control

In precipitation gravimetry, the precipitating agent should react specifically or selectively with the analyte. While a specific reagent reacts with the analyte alone, a selective reagent can react with a limited number of chemical species.
The obtained precipitate should be either a pure substance of known composition or easily converted to one by a simple process, such as ignition or drying. In addition, the precipitate should be insoluble and easily filterable. In general, filterability...
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.

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Advancing High-Resolution Imaging of Virus Assemblies in Liquid and Ice
08:31

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Modeling the competition between aggregation and self-assembly during virus-like particle processing.

Yong Ding1, Yap Pang Chuan, Lizhong He

  • 1Australian Institute for Bioengineering and Nanotechnology, The University of Queensland, Centre for Biomolecular Engineering, St Lucia, QLD 4072, Australia.

Biotechnology and Bioengineering
|June 4, 2010
PubMed
Summary
This summary is machine-generated.

Controlling protein aggregation during virus-like particle (VLP) production is crucial for vaccine development. A new mathematical model predicts aggregation, revealing up to 38% product loss and enabling rational scale-up strategies.

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

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Last Updated: Jun 12, 2026

Advancing High-Resolution Imaging of Virus Assemblies in Liquid and Ice
08:31

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Published on: July 20, 2022

Open-source Single-particle Analysis for Super-resolution Microscopy with VirusMapper
07:38

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Published on: April 9, 2017

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

Area of Science:

  • Biotechnology
  • Biophysics
  • Pharmaceutical Science

Background:

  • Protein aggregation is a critical challenge in biopharmaceutical development, impacting product yield, potency, and safety.
  • Virus-like particles (VLPs) are promising vaccine candidates, but their production is susceptible to aggregation, limiting efficacy and increasing costs.

Purpose of the Study:

  • To develop a mechanistic mathematical model for VLP self-assembly that accurately predicts aggregation.
  • To quantify product loss due to aggregation and understand its impact on VLP production.

Main Methods:

  • Developed a mechanistic mathematical model for VLP self-assembly.
  • Incorporated subunit partitioning between productive assembly and aggregation pathways.
  • Analyzed aggregation kinetics and concentration dependence.

Main Results:

  • Unproductive aggregation can lead to significant product loss (up to 38%) by competing with productive VLP nucleation and growth.
  • Protein subunit aggregation follows an apparent second-order concentration dependence, suggesting dimerization is a key step.
  • The model provides a realistic and simplified approach to predict protein aggregation behavior.

Conclusions:

  • The developed mathematical model accurately describes VLP self-assembly and aggregation.
  • Understanding and controlling aggregation pathways is essential for optimizing VLP production.
  • The model's amenability to different reactor formats facilitates rational scale-up strategies for biomolecular assembly products.