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Related Concept Videos

Receptor-mediated Endocytosis01:20

Receptor-mediated Endocytosis

Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
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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 stands for...

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A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation
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Spiking the MERS-coronavirus receptor.

Berend Jan Bosch1, V Stalin Raj, Bart L Haagmans

  • 1Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3508 TD Utrecht, the Netherlands.

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|August 14, 2013
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Summary

Middle East respiratory syndrome coronavirus (MERS-CoV) causes severe respiratory illness. Researchers have determined the crystal structure of the MERS-CoV receptor-binding domain interacting with the human CD26 receptor.

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Area of Science:

  • Virology
  • Structural Biology
  • Infectious Diseases

Background:

  • A novel coronavirus, Middle East respiratory syndrome coronavirus (MERS-CoV), has emerged via zoonotic transmission.
  • MERS-CoV causes severe lower respiratory tract infections in humans.

Purpose of the Study:

  • To characterize the crystal structure of the MERS-CoV receptor-binding domain (RBD).
  • To elucidate the interaction between the MERS-CoV RBD and its host cell receptor, CD26.

Main Methods:

  • X-ray crystallography was used to determine the complex structure.
  • Structural analysis of the MERS-CoV RBD in complex with human CD26.

Main Results:

  • The crystal structure of the MERS-CoV RBD bound to the human CD26 receptor was determined.
  • Detailed atomic interactions between the virus and host receptor were revealed.

Conclusions:

  • Structural insights into MERS-CoV and CD26 interaction provide a basis for understanding viral entry.
  • This characterization can inform the development of antiviral strategies against MERS-CoV.