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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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Plaque Assay for Murine Norovirus
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Structural Studies on the Shapeshifting Murine Norovirus.

Michael B Sherman1, Alexis N Williams1, Hong Q Smith1

  • 1Department of Biochemistry and Molecular Biology, University of Texas Medical Branch at Galveston, 301 University Boulevard, 5.104D Basic Science Building, Route 0645, Galveston, TX 77555, USA.

Viruses
|November 27, 2021
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Noroviruses change shape in response to environmental cues. This viral shapeshifting helps noroviruses (Norovirus) bind to cells and evade antibody neutralization, a novel immune evasion strategy.

Keywords:
antibodiesbileneutralizationnorovirus

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Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • Noroviruses cause significant global gastroenteritis.
  • The norovirus capsid protein (VP1) has N-terminal (N), shell (S), and C-terminal protruding (P) domains.
  • The P domain's P2 subdomain binds cellular receptors and antibodies.

Purpose of the Study:

  • To investigate how murine norovirus (MNV) capsid structure changes in response to physiological cues.
  • To understand the functional implications of these structural changes for viral infection and immune evasion.

Main Methods:

  • Review of studies on murine norovirus (MNV).
  • Analysis of capsid conformational changes induced by bile, pH, Mg2+, and Ca2+.

Main Results:

  • MNV capsid undergoes significant conformational changes in the intestine (low pH, high bile/metal).
  • These changes contract the P domain, enhance receptor binding, and block antibody neutralization.
  • In serum (neutral pH, low bile/metal), the P domain is open, favoring antibody binding but reducing receptor interaction.

Conclusions:

  • MNV exhibits environmentally-induced conformational changes (shapeshifting).
  • This mechanism optimizes cellular attachment in the intestine and facilitates immune evasion.
  • This is the first reported instance of a virus using shapeshifting to escape the immune response.