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A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
Published on: July 18, 2013
Proteomic analysis identifies a novel function for galectin-3 in the cell entry of parvovirus
Pierre Garcin1, Sarah Cohen, Sanne Terpstra
1Department of Zoology, University of British Columbia, 6270 University Boulevard, Vancouver, BC, Canada V6T 1Z4.
Abstract:
Cellular factors associated with the parvovirus minute virus of mice (MVM) during infection are thought to play important roles in the MVM life cycle but only a few of these have been identified. Here we used a proteomic-based approach in order to identify host-binding partners of MVM. Using purified MVM as bait for immunoprecipitation assays, a total of 150 proteins were identified in MVM immunoprecipitates by quantitative liquid chromatography-tandem mass spectrometry. Galectin-3 was one of six proteins showing a statistically significant enrichment across replicates. Small interfering RNA depletion studies revealed an important role for galectin-3 in MVM endocytosis and infectivity in LA9 mouse fibroblast cells. Galectin-3-depleted cells were less susceptible to MVM infection than control cells and showed a significant reduction of MVM cellular uptake, but not of MVM binding to the cell surface. Our results indicate an important role for galectin-3 in the cellular uptake of MVM. We propose that galectin-3 facilitates the access of MVM to its receptor(s) at the plasma membrane and in this way promotes MVM endocytosis.
Insights
Researchers identified galectin-3 as a key cellular factor for minute virus of mice (MVM) infection. Depleting galectin-3 reduced MVM uptake and infectivity, highlighting its role in viral endocytosis.
Area of Science:
- Virology
- Cell Biology
- Proteomics
Background:
- Cellular factors are crucial for the minute virus of mice (MVM) life cycle, but few have been identified.
- Understanding host-viral interactions is key to deciphering viral pathogenesis.
Purpose of the Study:
- To identify host-binding partners of MVM using a proteomic approach.
- To investigate the role of identified host factors in MVM infection.
Main Methods:
- Purified MVM was used as bait in immunoprecipitation assays.
- Quantitative liquid chromatography-tandem mass spectrometry (LC-MS/MS) was employed to identify MVM-associated proteins.
- Small interfering RNA (siRNA) was used to deplete specific host factors, followed by infection assays.
Main Results:
- A total of 150 proteins were identified as MVM-binding partners.
- Galectin-3 was significantly enriched among the identified proteins.
- Depletion of galectin-3 reduced MVM endocytosis and infectivity in LA9 mouse fibroblast cells.
- Galectin-3 depletion decreased MVM cellular uptake but not cell surface binding.
Conclusions:
- Galectin-3 plays a significant role in MVM endocytosis.
- Galectin-3 facilitates MVM access to its receptor(s) at the plasma membrane, promoting viral entry.
