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Related Concept Videos

Proteomics01:33

Proteomics

10.1K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
10.1K
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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Protein Complex Assembly02:41

Protein Complex Assembly

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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.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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Conjugated Proteins02:50

Conjugated Proteins

29.7K
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...
29.7K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

5.5K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
5.5K
Size and Structure of Viral Genomes01:26

Size and Structure of Viral Genomes

1.0K
Viral genomes exhibit remarkable diversity in size, structure, and composition, influencing their replication strategies and interactions with host cells. These genomes consist of either DNA or RNA and may be linear or circular. Additionally, they can be single-stranded or double-stranded, with each configuration affecting how the virus propagates within a host. RNA viruses, for instance, generally have smaller genomes than DNA viruses, a factor that contributes to their high mutation rates and...
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Related Experiment Video

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Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins
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Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins

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Structural Proteomics of Herpesviruses.

Baptiste Leroy1, Laurent Gillet2, Alain Vanderplasschen3

  • 1Laboratory of Proteomic and Microbiology, Research Institute of Biosciences, University of MONS, 4000 Mons, Belgium. baptiste.leroy@umons.ac.be.

Viruses
|February 25, 2016
PubMed
Summary

Mass spectrometry is revealing the protein composition of herpesviruses, aiding in understanding their complex lifecycle and immune evasion. This research is crucial for developing new antiviral therapies against these prevalent infections.

Keywords:
herpesvirushost proteinsproteomicstructural proteins

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Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
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Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy

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Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
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Area of Science:

  • Virology
  • Proteomics
  • Mass Spectrometry

Background:

  • Herpesviruses are widespread and cause significant pathologies in humans and animals.
  • Current antiviral strategies are often ineffective due to herpesviral immune evasion mechanisms.
  • A deeper understanding of herpesvirus structure and lifecycle is needed.

Purpose of the Study:

  • To review mass spectrometry-based approaches for analyzing herpesvirus virion composition.
  • To highlight recent advancements in understanding herpesvirus proteomes.
  • To discuss strategies for identifying structural proteins and host factors.

Main Methods:

  • Review of mass spectrometry techniques applied to herpesvirus research.
  • Description of sample preparation and fractionation strategies for protein localization.
  • Analysis of post-translational modifications and protein abundance.

Main Results:

  • Mass spectrometry has enabled fundamental discoveries in herpesvirus proteomics.
  • Methods for distinguishing structural from non-structural proteins have been refined.
  • Insights into the role of host proteins in herpesvirus structure are emerging.

Conclusions:

  • Mass spectrometry is a powerful tool for elucidating herpesvirus virion composition.
  • Further quantitative proteomic studies are necessary to understand the dynamics of herpesvirus structural proteins.
  • This knowledge is essential for developing novel therapeutic strategies against herpesvirus infections.