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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
Leaky Scanning02:28

Leaky Scanning

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 stands for...
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Diversity of Antigen Receptors

Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
Immune Response Against Viral Pathogens01:29

Immune Response Against Viral Pathogens

The immune system's response to viral infections is a complex and coordinated process involving natural killer (NK) cells, T cell-mediated responses, and antibody-mediated responses.
NK Cells
NK cells are a crucial part of our innate immune system, acting as the first line of defense against viral infections. These cells can recognize and kill infected cells without prior exposure to the virus, effectively slowing down the spread of infection. Additionally, NK cells produce proinflammatory...
Protein Complex Assembly02:41

Protein Complex Assembly

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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Engineering Antiviral Agents via Surface Plasmon Resonance
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Specificity switching in virus-receptor complexes.

Thilo Stehle1, José M Casasnovas

  • 1Interfaculty Institute for Biochemistry, University of Tuebingen, Hoppe-Seyler-Strasse 4, Tuebingen, Germany. thilo.stehle@uni-tuebingen.de

Current Opinion in Structural Biology
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Structural studies reveal how viral attachment proteins bind cellular receptors, explaining how viruses adapt to infect different hosts. This knowledge aids in understanding viral spread, disease, and vaccine development.

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Area of Science:

  • Structural biology
  • Virology
  • Molecular biology

Background:

  • Recent determination of viral attachment protein-receptor complex structures enhances understanding of molecular recognition.
  • These structures reveal viral protein adaptability in engaging diverse cellular receptors within a single virus family.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying viral receptor binding specificity.
  • To link viral tropism, spread, and pathogenicity to receptor engagement.
  • To inform the design of viral gene delivery vectors and novel vaccine targets.

Main Methods:

  • X-ray crystallography or Cryo-electron microscopy (Cryo-EM) of viral attachment protein-receptor complexes.
  • Bioinformatic analysis of structural and sequence data.
  • Functional assays to assess viral tropism and pathogenicity.

Main Results:

  • Detailed structural insights into the molecular interactions between viral attachment proteins and cellular receptors.
  • Identification of key structural features enabling viral proteins to switch receptor specificity.
  • Correlation between altered receptor binding and changes in viral tropism and pathogenicity.

Conclusions:

  • Understanding viral attachment protein-receptor interactions is crucial for predicting and controlling viral spread and disease.
  • Structural data provides a foundation for engineering viruses with modified tropism for gene therapy applications.
  • Targeting specific viral-receptor interfaces may lead to the development of broadly effective vaccines.