Publications by authors named "Varun Bhadkamkar"
The intracellular bacterial pathogen () manipulates eukaryotic host ubiquitination machinery to form its replicative vacuole. While nearly 10% of 's ∼330 secreted effector proteins are ubiquitin ligases or deubiquitinases, a comprehensive measure of temporally resolved changes in the endogenous host ubiquitinome during infection has not been undertaken. To elucidate how hijacks host cell ubiquitin signaling, we generated a proteome-wide analysis of changes in protein ubiquitination during infection.
View Article and Find Full Text PDFThe intracellular bacterial pathogen manipulates eukaryotic host ubiquitination machinery to form its replicative vacuole. While nearly 10% of 's arsenal of ~330 secreted effector proteins have been biochemically characterized as ubiquitin ligases or deubiquitinases, a comprehensive measure of temporally resolved changes in the endogenous host ubiquitinome during infection has not been undertaken. To elucidate how hijacks ubiquitin signaling within the host cell, we undertook a proteome-wide analysis of changes in protein ubiquitination during infection.
View Article and Find Full Text PDFArticle Synopsis
- During infection, Legionella pneumophila injects over 300 proteins into host cells, creating a specialized environment (LCV) for bacterial growth.
- Researchers used CRISPR-Cas9 screening on human immune cells to pinpoint both established and new host factors involved in the bacteria's ability to evade destruction.
- The study found that certain proteins like Rab10 are crucial for bacterial replication and are modified by bacterial effectors, revealing new understandings of Legionella's interaction with host cells.