Japanese encephalitis virus capsid protein interacts with non-lipidated MAP1LC3 on replication membranes and lipid

Riya Sarkar1, Kiran Bala Sharma1,2, Anita Kumari1

  • 1Translational Health Science & Technology Institute, NCR Biotech Science Cluster, Faridabad, Haryana, India.

Insights

Microtubule-associated protein 1 light chain 3 (MAP1LC3) binds to Japanese encephalitis virus (JEV) capsid protein, inhibiting viral replication. This interaction occurs on replication complexes and lipid droplets, independent of autophagy pathways.

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Microtubule-associated protein 1 light chain 3 (MAP1LC3) plays roles in autophagy and other cellular processes.
  • MAP1LC3 is a known host-dependency factor for various viral infections.
  • Japanese encephalitis virus (JEV) replication is linked to endoplasmic reticulum-derived membranes and lipid metabolism.

Purpose of the Study:

  • To further characterize the role of MAP1LC3 in JEV replication.
  • To investigate the interaction between MAP1LC3 and JEV proteins.
  • To identify the molecular mechanisms underlying JEV replication and host-cell involvement.

Main Methods:

  • Immunofluorescence microscopy to visualize protein localization.
  • Immunoprecipitation assays to detect protein-protein interactions.
  • High-resolution protein-protein docking studies to predict interaction sites.

Main Results:

  • MAP1LC3 (LC3-I) interacts with the JEV capsid protein in infected cells.
  • This interaction occurs on replication complexes and lipid droplets (LDs).
  • JEV infection reduces LDs, suggesting a link between lipid metabolism and viral replication. A specific LC3-interacting region (FTAL) was identified on the capsid protein.

Conclusions:

  • MAP1LC3 is crucial for JEV replication, interacting directly with the viral capsid protein.
  • The capsid-LC3 interaction is independent of autophagy pathways and specific to LC3.
  • Understanding this interaction may reveal new targets for antiviral therapies against JEV.

Related Concept Videos

Leaky Scanning02:28

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
5.5K
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...
4.1K
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
5.5K
Viral Structure00:56

Viral Structure

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.
72.2K
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
12.0K
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...
4.7K