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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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Conjugated Proteins02:50

Conjugated Proteins

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Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
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Introduction to Virus01:28

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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...
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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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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.
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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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Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
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The SARS coronavirus nucleocapsid protein--forms and functions.

Chung-ke Chang1, Ming-Hon Hou2, Chi-Fon Chang3

  • 1Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan, ROC.

Antiviral Research
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Summary

The SARS-CoV N protein

Keywords:
Capsid packagingCoronavirusIntrinsic disorderNucleocapsid proteinRNPSARS

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Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • The severe acute respiratory syndrome coronavirus (SARS-CoV) nucleocapsid phosphoprotein (N protein) is crucial for packaging the viral genome into ribonucleocapsids (RNPs).
  • Understanding the N protein's structure and nucleic acid interactions is vital for comprehending viral assembly and developing antivirals.

Purpose of the Study:

  • To review and synthesize current knowledge on the SARS-CoV N protein's structure, function, and nucleic acid interactions.
  • To propose a model for the SARS-CoV ribonucleoprotein (RNP) structure.

Main Methods:

  • Review of existing literature on SARS-CoV N protein structure and function.
  • Analysis of structural data and protein-nucleic acid interaction mechanisms.
  • Development of a computational model for the SARS-CoV RNP.

Main Results:

  • The N protein exhibits modular organization and intrinsic disorder, facilitating protein-protein and protein-nucleic acid interactions.
  • N protein binds nucleic acid at multiple sites via a coupled-allostery mechanism.
  • Visualization of the RNP structure within SARS-CoV virions.

Conclusions:

  • The SARS-CoV N protein's modularity and disorder are critical for dynamic RNP capsid formation and function.
  • The proposed RNP model aligns with existing data and resembles other viral RNP structures.
  • This research contributes to understanding highly pathogenic human coronaviruses like SARS and MERS.