ArticleFEMS microbiology letters2017
Protein aggregation in Ehrlichia chaffeensis during infection of mammalian cells.
Article in FEMS microbiology letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Article
- Hsp100 Molecular Chaperone ClpB and Its Role in Virulence of Bacterial Pathogens.International journal of molecular sciences · 2021Review
- The Role of ClpB in Bacterial Stress Responses and Virulence.Frontiers in molecular biosciences · 2021Review
- AAA+ Molecular Chaperone ClpB inInternational journal of molecular sciences · 2020Review
- Proteome Analysis Revealed Changes in Protein Expression Patterns Caused by Mutations inFrontiers in cellular and infection microbiology · 2019Article
- Protein and DNA synthesis demonstrated in cell-free Ehrlichia chaffeensis organisms in axenic medium.Scientific reports · 2018Article
- Impact of Three Different Mutations in Ehrlichia chaffeensis in Altering the Global Gene Expression Patterns.Scientific reports · 2018Article
- Repurposing p97 inhibitors for chemical modulation of the bacterial ClpB-DnaK bichaperone system.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ehrlichia chaffeensis is an obligatory intracellular pathogen transmitted through infected ticks to humans and other vertebrates. We investigated the extent of protein aggregation in E. chaffeensis during infection of canine macrophage cell line, DH82. We discovered that the size of the aggregated fraction of E. chaffeensis proteins increased during the first 48 h post infection. We also incubated the infected cells with guanidinium chloride (GuHCl), a known inhibitor of the protein-disaggregating molecular chaperone ClpB. Up to 0.5 mM GuHCl had no impact on the host cells, whereas the viability of the pathogen was reduced by ∼60% in the presence of the inhibitor. Furthermore, we found that the size of the aggregated protein fraction in E. chaffeensis increased significantly in cultures supplemented with 0.5 mM GuHCl, which also resulted in the preferential accumulation of ClpB with the aggregated proteins. Altogether, our results suggest that an exposure of E. chaffeensis to the stressful environment of a host cell results in an increased aggregation of the pathogen's proteins, which is exacerbated upon inhibition of ClpB. Our studies establish a link between protein quality control and pathogen survival during infection of a host.
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