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Related Concept Videos

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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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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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Translational regulation in prokaryotes ensures efficient protein synthesis by controlling ribosome access to mRNA. This regulation is mediated by secondary RNA structures, including translational riboswitches, RNA thermometers, and small RNAs (sRNAs), which respond to intracellular and environmental signals to modulate gene expression.Translational RiboswitchesRiboswitches in the leader region of mRNAs can regulate translation by altering the accessibility of the Shine-Dalgarno (SD) sequence,...
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Viruses with RNA Genomes01:29

Viruses with RNA Genomes

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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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Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Protein post-translational modification in SARS-CoV-2 and host interaction.

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  • 1China-Japan Union Hospital, Jilin University, Changchun, Jilin Province, China.

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|January 30, 2023
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Summary

Post-translational modifications (PTMs) in SARS-CoV-2 are crucial for viral entry, replication, and immune evasion. Understanding these PTMs informs strategies for COVID-19 treatment and vaccine development.

Keywords:
ADP-ribosylationSARS-CoV-2acylationglycosylationmethylationphosphorylationubiquitination

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Area of Science:

  • Virology and Molecular Biology
  • Immunology
  • Biochemistry

Background:

  • Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) causes significant respiratory and multi-system diseases.
  • Post-translational modifications (PTMs) are critical for SARS-CoV-2 pathogenesis and viral lifecycle.
  • Common PTMs include glycosylation, phosphorylation, acylation, ubiquitination, and methylation, affecting viral proteins like Spike (S), Nucleocapsid (N), Membrane (M), and Envelope (E).

Purpose of the Study:

  • To review the diverse effects of PTMs on SARS-CoV-2.
  • To elucidate the role of PTMs in host cell interactions and immune responses.
  • To highlight the implications of PTMs for antiviral strategies and vaccine development.

Main Methods:

  • Literature review of studies investigating SARS-CoV-2 PTMs.
  • Analysis of PTMs on key viral proteins (S, N, M, E, NSP3, ORF7a).
  • Examination of PTMs' impact on viral entry, replication, assembly, and host immune modulation.

Main Results:

  • Glycosylation of S protein facilitates cell entry and immune evasion.
  • Phosphorylation and methylation of N protein enhance viral RNA binding and replication.
  • Acylation (succinylation, palmitoylation, myristoylation) and ubiquitination of viral proteins modulate assembly, infectivity, and host immune signaling (e.g., IFN-α).

Conclusions:

  • PTMs play fundamental roles across the SARS-CoV-2 lifecycle, from entry to replication and assembly.
  • PTMs significantly influence host-pathogen interactions, including immune evasion and inflammation.
  • Targeting PTMs presents a promising avenue for developing effective antiviral therapies and vaccines against COVID-19.