Related Experiment Video
Updated: Apr 26, 2026

11:48
Generation, Amplification, and Titration of Recombinant Respiratory Syncytial Viruses
Published on: April 4, 2019
16.3K
Human rhinovirus 16 causes Golgi apparatus fragmentation without blocking protein secretion
Aurelie Mousnier1, Dawid Swieboda1, Anaïs Pinto1
1Airway Disease Infection Section, National Heart and Lung Institute, Imperial College, London, United Kingdom.
Journal of Virology
|August 8, 2014
Summary
Human rhinovirus (HRV) nonstructural proteins fragment the Golgi apparatus and block secretion in cells. However, HRV16 infection fragments the Golgi apparatus without blocking protein secretion, impacting host defense understanding.
Area of Science:
- Virology
- Cell Biology
- Immunology
Background:
- Picornaviruses, including human rhinovirus (HRV), disrupt the host cell's secretory pathway, affecting Golgi apparatus structure and function.
- This disruption has implications for host defense mechanisms, potentially inhibiting cytokine and interferon secretion.
- Previous studies show conflicting results regarding whether individual viral proteins or live virus infection causes secretory pathway disruption.
Purpose of the Study:
- To investigate the effects of human rhinovirus 16 (HRV16) nonstructural proteins and live virus infection on Golgi apparatus fragmentation and protein secretion in HeLa cells.
- To clarify discrepancies between studies using expressed viral proteins versus live virus infection in understanding HRV's impact on the secretory pathway.
Main Methods:
- Expressed individual HRV16 nonstructural proteins in HeLa cells to assess their cellular localization and effects on endoplasmic reticulum and Golgi apparatus architecture.
- Quantified the impact on the secretory pathway by measuring Gaussia luciferase reporter protein secretion.
- Examined Golgi apparatus structure and protein secretion following infection with live HRV16 virus.
Main Results:
- Expression of HRV16 3A, 3AB, and to a lesser extent 2B nonstructural proteins caused Golgi apparatus dispersal and inhibited protein secretion.
- Live HRV16 infection led to significant Golgi apparatus dispersal but did not inhibit protein secretion.
- Discrepancies observed between effects of expressed proteins and live virus infection highlight the complexity of HRV's impact on the secretory pathway.
Conclusions:
- Individual HRV16 nonstructural proteins can independently disrupt Golgi apparatus structure and block protein secretion.
- Live HRV16 infection causes Golgi fragmentation but maintains protein secretion, suggesting a more nuanced mechanism than previously assumed.
- Findings emphasize the importance of considering the viral context (individual proteins vs. replication) when interpreting mechanistic studies of HRV's effects on host cell function.
Related Concept Videos
Vesicular Tubular Clusters
2.4K
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...
2.4K
Rab Proteins
4.0K
Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
4.0K
Transport Across the Golgi
5.2K
While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
5.2K
Rab Cascades
2.8K
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
2.8K
Influenza
79
Influenza is an acute, highly communicable viral disease that affects the respiratory tract and is responsible for seasonal epidemics worldwide. Influenza A is the most prevalent type associated with widespread outbreaks and is subtyped based on two surface glycoproteins: hemagglutinin (H) and neuraminidase (N), as in H1N1. These glycoproteins are essential for viral infectivity, transmission, and immune recognition. Transmission occurs primarily through respiratory droplets and contaminated...
79
Golgi Matrix Proteins
1.7K
Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
1.7K

