Effect of cytochalasin B on the maturation of enveloped viruses

Insights

Cytochalasin B treatment affects viral glycoprotein synthesis and function but does not impede enveloped virus infectivity. These findings suggest viral maturation does not require an intact actin cytoskeleton.

Area of Science:

  • Virology
  • Cell Biology
  • Biochemistry

Background:

  • Viral maturation and release are complex processes often involving host cell machinery.
  • The role of the actin cytoskeleton in enveloped virus assembly and egress remains an area of investigation.

Purpose of the Study:

  • To investigate the impact of cytochalasin B (CB) on the maturation and infectivity of influenza and vesicular stomatitis viruses.
  • To determine if an intact actin cytoskeleton is essential for enveloped virus assembly and release.

Main Methods:

  • Enveloped viruses (influenza, vesicular stomatitis) were cultured in cells treated with cytochalasin B.
  • Viral infectivity, glycoprotein synthesis (hemagglutinin, neuraminidase), glycosylation, and enzymatic activity were analyzed.
  • Electrophoretic analysis was used to assess glycoprotein alterations.

Main Results:

  • Cytochalasin B treatment did not affect viral infectivity, indicating polymerized actin is not required for functional viral components.
  • CB treatment inhibited influenza virus release, linked to aberrant neuraminidase (NA) glycoprotein synthesis and a 90% reduction in NA activity.
  • Viral glycoproteins showed altered electrophoretic mobility and heterogeneity, with inhibited glucosamine incorporation, impacting NA function but not hemagglutination.

Conclusions:

  • Enveloped virus maturation, including assembly and release, is not dependent on an intact actin cytoskeletal network.
  • Alterations in viral glycoprotein glycosylation due to CB treatment can affect specific viral functions like neuraminidase activity without significantly impacting infectivity.

Related Concept Videos

Lytic Cycle of Bacteriophages01:30

Lytic Cycle of Bacteriophages

Bacteriophages, also known as phages, are specialized viruses that infect bacteria. A key characteristic of phages is their distinctive “head-tail” morphology. A phage begins the infection process (i.e., lytic cycle) by attaching to the outside of a bacterial cell. Attachment is accomplished via proteins in the phage tail that bind to specific receptor proteins on the outer surface of the bacterium. The tail injects the phage’s DNA genome into the bacterial cytoplasm. In the lytic replication...
Maturation of Endosomes01:28

Maturation of Endosomes

The early endosome containing internalized molecules matures through transformations in its location, morphology, intraluminal pH, and membrane protein composition. Together, these changes result in a more acidic late endosome that contains multiple intraluminal vesicles; therefore, the late endosome is also called a multivesicular body (MVB).
Changes in location
The maturing endosome moves along microtubules from the periphery of the cell towards the perinuclear region. This movement of the...
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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...
Inhibitors Of Virion Release01:25

Inhibitors Of Virion Release

Viral replication and dissemination rely on efficient mechanisms for host cell entry, genome replication, assembly, and release. Influenza viruses, such as types A and B, are negative-sense single-stranded RNA viruses with a segmented genome, that depend on two critical surface glycoproteins to carry out these processes: hemagglutinin (HA) and neuraminidase (NA). HA initiates infection by binding to sialic acid residues on the surface of host epithelial cells, facilitating receptor-mediated...
Inhibitors of Virion Maturation and Assembly01:19

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...