Cell entry of BmCPV can be promoted by tyrosine-protein kinase Src64B-like protein

Yiling Zhang1, Liyuan Zhu2, Guangli Cao3

  • 1School of Biology and Basic Medical Sciences, Soochow University, Suzhou, 215123, China; School of Biotechnology, Jiangsu University of Science and Technology, Zhenjiang, 212018, China.

Insights

The study reveals that tyrosine-protein kinase Src64B-like is crucial for Bombyx mori cytoplasmic polyhedrosis virus (BmCPV) entry into cells. Silencing Src64B-like significantly reduces BmCPV infection, highlighting its role in viral cell entry.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Bombyx mori cytoplasmic polyhedrosis virus (BmCPV) is a non-enveloped dsRNA virus infecting the silkworm midgut.
  • BmCPV utilizes clathrin-dependent endocytosis and β1 integrin for cell entry.
  • The precise cellular mechanisms governing BmCPV entry remain incompletely understood.

Purpose of the Study:

  • To investigate the potential involvement of tyrosine-protein kinase Src64B-like in the cell entry process of BmCPV.
  • To elucidate the role of Src64B-like in facilitating BmCPV infection in Bombyx mori.

Main Methods:

  • Cloning and expression of the Src64B-like gene in E. coli.
  • Generation of anti-Src64B-like polyclonal antibody.
  • RNA interference (RNAi) to silence Src64B-like gene expression.
  • In vitro and in vivo BmCPV infection assays.
  • Immunofluorescence assays to assess protein localization.

Main Results:

  • Silencing Src64B-like gene expression reduced BmCPV infection by 59.48% in vitro and 92.22% in vivo.
  • Conversely, increased Src64B-like expression enhanced BmCPV infection.
  • Immunofluorescence data indicated no direct co-localization between Src64B-like and BmCPV during infection.

Conclusions:

  • Src64B-like protein plays a significant role in the cell entry mechanism of BmCPV.
  • Src64B-like facilitates BmCPV infection independently of direct physical interaction with the virus.

Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
15.1K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

4.5K
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
18.6K
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
8.5K
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.7K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
14.4K