Associating bovine herpesvirus 1 envelope glycoprotein gD with activated phospho-PLC-γ1(S1248)

Chang Liu1, Weifeng Yuan2, Hao Yang1

  • 1College of Life Sciences, Hebei University , Baoding, China.

Microbiology Spectrum
|September 1, 2023
PubMed

Insights

Bovine herpesvirus 1 infection activates phospholipase C gamma 1 (PLC-γ1) signaling, leading to its accumulation in the Golgi apparatus. This activated PLC-γ1 escorts viral particles for release, revealing a novel mechanism in virus replication.

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Phospholipase C gamma 1 (PLC-γ1) is known to localize in various cellular compartments, including the cytosol, plasma membrane, and nucleus.
  • Bovine herpesvirus 1 (BoHV-1) productive infection is associated with increased levels of phosphorylated PLC-γ1 at Ser1248 (p-PLC-γ1(S1248)), which supports viral replication.

Purpose of the Study:

  • To investigate the subcellular localization of activated p-PLC-γ1(S1248) during BoHV-1 infection.
  • To elucidate the role of p-PLC-γ1(S1248) in the BoHV-1 life cycle, particularly in relation to viral particle trafficking.

Main Methods:

  • Confocal microscopy to visualize p-PLC-γ1(S1248) localization in infected cells.
  • Coimmunoprecipitation assays to identify proteins interacting with Golgi-localized p-PLC-γ1(S1248).
  • Treatment with a PLC-γ1-specific inhibitor (U73122) to assess the functional role of PLC-γ1 signaling in viral egress.

Main Results:

  • Activated p-PLC-γ1(S1248) was found to accumulate in the Golgi apparatus during later stages of BoHV-1 infection.
  • Golgi-associated p-PLC-γ1(S1248) specifically binds to the viral protein gD, but not gC.
  • Inhibition of PLC-γ1 signaling led to the retention of viral protein gD within the Golgi apparatus, suggesting impaired virion egress.

Conclusions:

  • This study identifies the Golgi apparatus as a novel cellular compartment containing activated p-PLC-γ1(S1248) during BoHV-1 infection.
  • Activated p-PLC-γ1(S1248) is associated with both intracellular and released virions, and its interaction with gD suggests a role in viral particle transport.
  • PLC-γ1 signaling appears to facilitate the trafficking of progeny virions from the Golgi apparatus, representing a new mechanism in BoHV-1 productive infection.
Abstract

Related Concept Videos

Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
7.2K
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
12.2K
Rab Proteins01:14

Rab Proteins

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...
4.0K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
3.6K
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
12.2K