CADM1 and CADM2 Trigger Neuropathogenic Measles Virus-Mediated Membrane Fusion by Acting in cis

Yuta Shirogane1, Ryuichi Takemoto1, Tateki Suzuki1

  • 1Department of Virology, Faculty of Medicine, Kyushu University, Fukuoka, Japan.

Journal of Virology
|April 29, 2021
PubMed

Insights

Measles virus (MeV) spreads between neurons by using cell adhesion molecules CADM1 and CADM2. These molecules trigger viral fusion, explaining how MeV causes subacute sclerosing panencephalitis (SSPE) in the brain.

Area of Science:

  • Virology
  • Neuroscience
  • Cell Biology

Background:

  • Measles virus (MeV) causes significant childhood morbidity and mortality worldwide.
  • Persistent MeV infection can lead to fatal subacute sclerosing panencephalitis (SSPE), a progressive neurological disorder.
  • The mechanism of MeV spread within neurons, which lack known MeV receptors, remains poorly understood.

Purpose of the Study:

  • To elucidate the molecular mechanism by which MeV propagates transsynaptically between neurons.
  • To identify host factors involved in MeV-induced membrane fusion and spread in the brain.
  • To explain the viral spread leading to subacute sclerosing panencephalitis (SSPE).

Main Methods:

  • Investigated the role of cell adhesion molecules CADM1 and CADM2 in MeV infection.
  • Utilized knockdown experiments to assess the impact of CADM1 and CADM2 on syncytium formation and virus transmission.
  • Analyzed the interaction of CADM1/CADM2 with the MeV attachment protein and fusion protein.

Main Results:

  • CADM1 and CADM2 were identified as host factors enabling MeV membrane fusion and spread in neurons lacking canonical receptors.
  • Unlike typical viral receptors, CADM1 and CADM2 interact in cis with the MeV attachment protein, triggering the fusion protein.
  • Knockdown of CADM1 and CADM2 significantly inhibited MeV-induced syncytium formation and neuronal transmission.

Conclusions:

  • MeV utilizes a novel 'receptor-mimicking cis-acting fusion triggering' mechanism involving CADM1 and CADM2 for transsynaptic spread in neurons.
  • This mechanism explains how MeV propagates in the brain to cause fatal SSPE.
  • The findings may reveal similar mechanisms in other viral infections.

Related Concept Videos

Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
4.0K
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
11.7K
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
15.7K
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.5K