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Related Concept Videos

Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Activation of Integrins01:15

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Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
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Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
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Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
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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.
Clathrin-Mediated Endocytosis of LDL
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Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting
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Published on: March 1, 2019

Alpha5beta1-integrin controls ebolavirus entry by regulating endosomal cathepsins.

Kathryn L Schornberg1, Charles J Shoemaker, Derek Dube

  • 1Department of Microbiology, University of Virginia, Charlottesville, VA 22908-0734, USA.

Proceedings of the National Academy of Sciences of the United States of America
|May 7, 2009
PubMed
Summary

Alpha(5)beta(1)-integrin is crucial for efficient ebolavirus glycoprotein entry into cells by regulating endosomal cathepsins. Integrin-deficient cells lack cathepsin B and L, hindering viral infection unless the glycoprotein is pre-activated.

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Published on: September 27, 2014

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Integrins mediate viral binding and internalization for both enveloped and nonenveloped viruses.
  • Ebolavirus glycoprotein (GP) priming by endosomal cathepsins B and L (CatB and CatL) is essential for viral fusion.

Purpose of the Study:

  • To investigate the role of alpha(5)beta(1)-integrin in ebolavirus infection.
  • To determine the relationship between alpha(5)beta(1)-integrin and endosomal cathepsin activity.
  • To elucidate the mechanism by which integrins influence ebolavirus entry.

Main Methods:

  • Utilized three cell systems: CHO cells lacking alpha(5)beta(1)-integrin, HeLa cells with siRNA knockdown of alpha(5)-integrin, and mouse beta(1)-integrin knockout fibroblasts.
  • Assessed viral entry, binding, and internalization using pseudovirions bearing ebolavirus GP.
  • Investigated the expression and activity of CatB and CatL in integrin-positive and integrin-negative cells.

Main Results:

  • Alpha(5)beta(1)-integrin is required for efficient ebolavirus GP pseudovirion entry, but not for binding or internalization.
  • Integrin-deficient cells lacked double-chain (DC) forms of CatB and CatL, correlating with reduced CatL activity.
  • Pre-priming of GP pseudovirions in vitro bypassed the requirement for alpha(5)beta(1)-integrin for infection.

Conclusions:

  • Alpha(5)beta(1)-integrin regulates endosomal cathepsins, which are necessary for priming ebolavirus GP for fusion.
  • The absence of DC forms of CatB and CatL in integrin-deficient cells renders them refractory to ebolavirus infection.
  • Integrins play a previously unrecognized role in viral entry by modulating cathepsin activity, impacting viral cell tropism.