Related Experiment Video
Updated: Dec 6, 2025
09:26
Production of a SARS-CoV-2 Virus-Like-Particle System to Investigate Viral Life Cycles In Vitro
Published on: June 6, 2025
902
Syncytia formation by SARS-CoV-2-infected cells
Julian Buchrieser1,2, Jérémy Dufloo1,2,3, Mathieu Hubert1,2
1Virus and Immunity Unit, Department of Virology, Institut Pasteur, Paris, France.
The EMBO Journal
|October 14, 2020
Summary
Severe COVID-19 involves lung damage and syncytia. SARS-CoV-2 Spike protein drives syncytia formation, but interferon-induced transmembrane proteins (IFITMs) inhibit this, while TMPRSS2 protease accelerates it.
Area of Science:
- Virology
- Cell Biology
- Immunology
Background:
- Severe COVID-19 is linked to lung damage and multinucleated syncytial pneumocytes.
- The mechanisms behind syncytia formation in SARS-CoV-2 infection are not fully understood.
Purpose of the Study:
- To investigate the viral and cellular mechanisms regulating SARS-CoV-2-induced syncytia formation.
- To identify host cellular proteins that modulate syncytia formation during infection.
Main Methods:
- Studied SARS-CoV-2 Spike protein expression on infected cell surfaces.
- Assessed the role of Spike protein in cell-cell fusion.
- Investigated the impact of interferon-induced transmembrane proteins (IFITMs) and TMPRSS2 protease on syncytia formation.
Main Results:
- SARS-CoV-2 Spike protein expression alone triggers syncytia formation.
- IFITM proteins, particularly IFITM1, inhibit Spike-mediated cell fusion.
- TMPRSS2 protease enhances syncytia formation by processing Spike and ACE2, overriding IFITM antiviral activity.
Conclusions:
- Cellular proteins significantly modulate SARS-CoV-2 pathological effects.
- IFITMs act as restriction factors against syncytia formation, while TMPRSS2 promotes it.
- Understanding these interactions is crucial for targeting COVID-19 pathogenesis.
More Related Videos
Related Concept Videos
00:57Viral Recombination
24.6K
Cells are sometimes infected by more than one virus at once. When two viruses disassemble to expose their genomes for replication in the same cell, similar regions of their genomes can pair together and exchange sequences in a process called recombination. Alternatively, viruses with segmented genomes can swap segments in a process called reassortment.
24.6K
01:45Vesicular Tubular Clusters
2.9K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
With the help of motor proteins such...
2.9K
01:03Rous Sarcoma Virus (RSV) and Cancer
5.9K
Rous Sarcoma virus or RSV was discovered by F. Peyton Rous in the year 1911 as a filterable transmissible agent that could cause tumors in chickens. He won a Nobel Prize for this discovery in 1966. His experiments clearly demonstrated that some cancers could be caused by infectious agents and led to the discovery of many more cancer-causing viruses in animals as well as humans.
RSV is a retrovirus that contains two copies of a plus-strand RNA genome. Its genome consists of four main open...
RSV is a retrovirus that contains two copies of a plus-strand RNA genome. Its genome consists of four main open...
5.9K
01:26Fusion of Secretory Vesicles with the Plasma Membrane
16.2K
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...
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
16.2K
02:41Protein Complex Assembly
16.0K
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...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.0K
01:43SNAREs and Membrane Fusion
12.0K
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...
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...
12.0K