Related Experiment Video
Updated: Jul 24, 2025

09:08
Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
Published on: July 27, 2021
3.8K
Enterovirus D68 capsid formation and stability requires acidic compartments
Ganna Galitska1, Alagie Jassey1, Michael A Wagner1
1Department of Microbiology and Immunology, University of Maryland School of Medicine, 685 W. Baltimore St, Baltimore, MD 21201, USA.
Biorxiv : the Preprint Server for Biology
|July 3, 2023
Summary
Enterovirus D68 requires specific organelle acidification for capsid formation. Inhibiting this process disrupts viral replication and causes cellular changes, unlike poliovirus.
Area of Science:
- Virology
- Cell Biology
Background:
- Enterovirus D68 (EV-D68) is a picornavirus linked to acute flaccid myelitis (AFM).
- Understanding EV-D68 pathogenesis is limited, often relying on poliovirus models.
- Low pH promotes poliovirus capsid maturation, but EV-D68's requirements are less understood.
Approach:
- Investigated the role of compartment acidification in EV-D68 infection.
- Examined cellular and viral phenotypes upon inhibition of acidification.
- Identified a critical time window for acidification's role in EV-D68 lifecycle.
Key Points:
- Inhibiting compartment acidification during a specific window (3-4hpi) impairs EV-D68 capsid formation and maintenance.
- This leads to altered viral replication organelles clustering.
- Acidification is crucial during the transition from RNA replication to virion assembly.
Conclusions:
- EV-D68 has distinct acidification requirements compared to poliovirus.
- Compartment acidification is a critical, time-sensitive step in EV-D68 virion production.
- Findings reveal novel insights into EV-D68 replication dynamics and potential therapeutic targets.
Related Concept Videos
Intralumenal Vesicles and Multivesicular Bodies
3.6K
Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
3.6K
Viral Structure
62.6K
Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
62.6K
Overview of Secretory Vesicles
8.6K
Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
8.6K
Vesicular Tubular Clusters
2.5K
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...
2.5K
Protein Complex Assembly
10.7K
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...
10.7K
Pinching-off of Coated Vesicles
3.2K
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
3.2K

