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Adherens Junctions01:24

Adherens Junctions

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.
Adherens Junctions are Dynamic
The endothelial cells...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Cell Adhesion Molecules - Types and Functions01:20

Cell Adhesion Molecules - Types and Functions

Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
CAM Families
The Integrin family of proteins is primarily  involved in a...
Cell Adhesion Molecules - Types and Functions01:20

Cell Adhesion Molecules - Types and Functions

Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
CAM Families
The Integrin family of proteins is primarily  involved in a...
Integrins01:10

Integrins

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.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
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.
Some...

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Related Experiment Video

Updated: Jul 15, 2026

Determination of Biofilm Initiation on Virus-infected Cells by Bacteria and Fungi
12:33

Determination of Biofilm Initiation on Virus-infected Cells by Bacteria and Fungi

Published on: July 6, 2016

Reovirus binding determinants in junctional adhesion molecule-A.

Kristen M Guglielmi1, Eva Kirchner, Geoffrey H Holm

  • 1Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA.

The Journal of Biological Chemistry
|April 25, 2007
PubMed
Summary

Junctional adhesion molecule-A (JAM-A) is a receptor for reoviruses. Reovirus binds to JAM-A monomers, not dimers, using specific residues on beta-strands C and C' for efficient interaction.

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Use of Viral Entry Assays and Molecular Docking Analysis for the Identification of Antiviral Candidates against Coxsackievirus A16

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Last Updated: Jul 15, 2026

Determination of Biofilm Initiation on Virus-infected Cells by Bacteria and Fungi
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Determination of Biofilm Initiation on Virus-infected Cells by Bacteria and Fungi

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Use of Viral Entry Assays and Molecular Docking Analysis for the Identification of Antiviral Candidates against Coxsackievirus A16

Published on: July 15, 2019

Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • Junctional adhesion molecule-A (JAM-A) functions as a serotype-independent receptor for mammalian orthoreoviruses (reoviruses).
  • The D1 domain of JAM-A is crucial for homodimerization and binding to the reovirus attachment protein sigma1.
  • Understanding the JAM-A-reovirus interaction is key to deciphering viral entry mechanisms and pathogenesis.

Purpose of the Study:

  • To elucidate the specific determinants of reovirus binding to JAM-A through structure-guided mutational analysis.
  • To investigate the role of JAM-A dimerization in reovirus attachment protein sigma1 binding.
  • To identify key residues and interaction interfaces involved in reovirus-JAM-A complex formation.

Main Methods:

  • Structure-guided mutational analysis of the JAM-A dimer interface.
  • Purification of mutant JAM-A ectodomains for binding studies.
  • Surface plasmon resonance (SPR) and solution-phase binding assays.
  • Expression of full-length JAM-A mutants in Chinese hamster ovary (CHO) cells to assess reovirus binding and infectivity.

Main Results:

  • Mutations disrupting JAM-A dimer interface salt-bridge or hydrogen-bond interactions abolished dimerization.
  • JAM-A mutants incapable of dimerization still formed complexes with the sigma1 head, indicating monomeric binding.
  • Specific residues (Glu61, Lys63 on beta-strand C; Leu72 on beta-strand C') are critical for efficient binding of type 3 Dearing reovirus sigma1.
  • Alterations in neighboring residues affected the kinetics of sigma1-JAM-A binding.
  • Different reovirus strains (type 1 Lang, type 2 Jones, type 3 Dearing) exhibited similar, though not identical, JAM-A binding requirements.

Conclusions:

  • Reoviruses engage JAM-A monomers via residues located primarily on beta-strands C and C' within the dimer interface.
  • JAM-A dimerization is not required for reovirus sigma1 binding.
  • Differences in JAM-A binding contacts may contribute to the distinct disease phenotypes observed with different reovirus strains in vivo.