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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.
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
COP Coated Vesicles00:59

COP Coated Vesicles

Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of different...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Introduction to Virus01:28

Introduction to Virus

Viruses are unique biological entities that blur the boundary between living and non-living systems. Although they lack cellular structure and metabolic processes, they can exhibit characteristics of life when infecting a host. Their defining feature is a nucleic acid core, composed of either DNA or RNA, encapsulated within a protein coat called a capsid. This simple structure allows them to invade host cells and use their machinery for replication efficiently.Viral Structure and...
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...

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Averaging of Viral Envelope Glycoprotein Spikes from Electron Cryotomography Reconstructions using Jsubtomo
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Published on: October 21, 2014

Multishell structures of virus coat proteins.

Peter Prinsen1, Paul van der Schoot, William M Gelbart

  • 1Department of Chemistry and Biochemistry, University of California, Los Angeles, 607 Charles E. Young Drive East, Los Angeles, California 90095-1569, USA. prinsen@lorentz.leidenuniv.nl

The Journal of Physical Chemistry. B
|April 8, 2010
PubMed
Summary
This summary is machine-generated.

Cowpea chlorotic mottle virus (CCMV) coat proteins self-assemble into multishell structures. Stability depends on ionic strength, pH, and protein charge, driven by counterion release and shell elasticity.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Virology

Background:

  • Purified cowpea chlorotic mottle virus (CCMV) coat proteins form spherical multishell structures without viral RNA under specific low ionic strength and pH conditions (3.7-5.0).
  • These structures exhibit oppositely charged surfaces: negatively charged outer surfaces and positively charged inner surfaces due to a disordered, arginine-rich N-terminal domain.

Purpose of the Study:

  • To elucidate the stabilizing forces behind CCMV multishell formation.
  • To understand the role of protein charge, shell elasticity, and solution conditions in multishell stability.
  • To predict conditions for multishell stability in CCMV mutants and other viruses.

Main Methods:

  • Analysis of forces stabilizing multishells, including counterion release and charge density effects related to shell curvature.
  • Calculation of free energy for shells with non-optimal radii of curvature based on elastic properties.
  • Investigation of factors influencing inter-shell spacing, primarily entropic elasticity of RNA-binding motifs.

Main Results:

  • Multishell stability is governed by counterion release and reduced charge density on larger outer shells, compensating for non-optimal curvature.
  • Structures are stable at low ionic strengths and pHs where outer surfaces are negatively charged.
  • Inter-shell spacing is dictated by the entropic elasticity of RNA-binding motifs.

Conclusions:

  • CCMV multishell formation is a complex interplay of electrostatic interactions, counterion effects, and protein elasticity.
  • The study provides a framework for predicting multishell stability across different protein charges, shell stiffness, and solution conditions.
  • Findings offer insights into viral self-assembly mechanisms and potential for engineered protein structures.