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Related Concept Videos

Viral Structure00:56

Viral Structure

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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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Retroviruses have a single-stranded RNA genome that undergoes a special form of replication. Once the retrovirus has entered the host cell, an enzyme called reverse transcriptase synthesizes double-stranded DNA from the retroviral RNA genome. This DNA copy of the genome is then integrated into the host’s genome inside the nucleus via an enzyme called integrase. Consequently, the retroviral genome is transcribed into RNA whenever the host’s genome is transcribed, allowing the...
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RNA viruses are categorized into positive-strand, negative-strand, or double-stranded groups based on their genomic structure and replication mechanisms. This classification dictates how they exploit host cellular machinery for protein synthesis and replication. Some RNA viruses also utilize reverse transcription as part of their life cycle, further diversifying their replication strategies.Positive-Strand RNA VirusesPositive-strand RNA viruses have genomes that function directly as messenger...
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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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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.
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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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Related Experiment Video

Updated: Apr 24, 2026

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

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Picornavirus morphogenesis.

Ping Jiang1, Ying Liu1, Hsin-Chieh Ma1

  • 1Department of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, New York, USA.

Microbiology and Molecular Biology Reviews : MMBR
|September 4, 2014
PubMed
Summary
This summary is machine-generated.

Picornaviruses assemble via a protein-protein interaction, not an RNA signal, revealing new insights into viral morphogenesis. This study details encapsidation intermediates, factors, and inhibitors for these disease-causing RNA viruses.

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Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Picornaviridae are small, plus-strand RNA viruses responsible for significant human and animal diseases.
  • Viral morphogenesis, particularly encapsidation, is poorly understood due to its coupling with translation and replication.
  • Previous studies on enteroviruses, like poliovirus, provide limited mechanistic details on assembly regulation.

Purpose of the Study:

  • To review and summarize current knowledge on picornavirus morphogenesis and encapsidation.
  • To elucidate the mechanism and regulatory factors governing viral assembly.
  • To present a model for enterovirus encapsidation and compare it with other plus-strand RNA viruses.

Main Methods:

  • Review of existing literature on picornavirus assembly and related plus-strand RNA viruses.
  • Analysis of recent findings, particularly regarding poliovirus encapsidation specificity.
  • Synthesis of information on encapsidation intermediates, factors, and inhibitors.

Main Results:

  • Picornavirus encapsidation specificity is unexpectedly governed by viral protein-protein interactions.
  • This interaction does not rely on a canonical RNA packaging signal, challenging previous assumptions.
  • The review covers key aspects including intermediates, specificity determinants, viral/cellular factors, and inhibitors.

Conclusions:

  • Viral protein interactions play a crucial role in governing the specificity of picornavirus encapsidation.
  • Understanding these mechanisms offers potential targets for antiviral strategies.
  • Further research is needed to fully delineate the complexities of picornavirus morphogenesis.