ArticleInfection and immunity2014
Streptococcus pneumoniae ClpL modulates adherence to A549 human lung cells through Rap1/Rac1 activation.
Article in Infection and immunity, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- 3' UTR-mediated regulation of a protein chaperone by the pspA mRNA in Streptococcus pneumoniae.Nucleic acids research · 2026Article
- EspP2 Regulates the Adhesion ofInternational journal of molecular sciences · 2024Article
- Comparison of the adherence of nontypeable haemophilus influenzae to lung epithelial cells.BMC infectious diseases · 2024Article
- Negative Cross-Talk between TLR2/4-Independent AMPKα1 and TLR2/4-Dependent JNK RegulatesJournal of immunology (Baltimore, Md. : 1950) · 2022Article
- The pneumococcal two-component system SirRH is linked to enhanced intracellular survival of Streptococcus pneumoniae in influenza-infected pulmonary cells.PLoS pathogens · 2020Article
- Impairment of the Cell Wall Ligase, LytR-CpsA-Psr Protein (LcpC), in Methicillin ResistantFrontiers in microbiology · 2020Article
- Article
- Prophage Excision inFrontiers in microbiology · 2019Article
- Transcriptional Profiling of Host Cell Responses to VirulentInternational journal of molecular sciences · 2018Article
- Small-Volume Flow Cytometry-Based Multiplex Analysis of the Activity of Small GTPases.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Stress responses in Streptococcus species and their effects on the host.Journal of microbiology (Seoul, Korea) · 2015Review
- TLR4 mediates pneumolysin-induced ATF3 expression through the JNK/p38 pathway in Streptococcus pneumoniae-infected RAW 264.7 cells.Molecules and cells · 2015Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Caseinolytic protease L (ClpL) is a member of the HSP100/Clp chaperone family, which is found mainly in Gram-positive bacteria. ClpL is highly expressed during infection for refolding of stress-induced denatured proteins, some of which are important for adherence. However, the role of ClpL in modulating pneumococcal virulence is poorly understood. Here, we show that ClpL impairs pneumococcal adherence to A549 lung cells by inducing and activating Rap1 and Rac1, thus increasing phosphorylation of cofilin (inactive form). Moreover, infection with a clpL mutant (ΔclpL) causes a greater degree of filopodium formation than D39 wild-type (WT) infection. Inhibition of Rap1 and Rac1 impairs filopodium formation and pneumococcal adherence. Therefore, ClpL can reduce pneumococcal adherence to A549 cells, likely via modulation of Rap1- and Rac1-mediated filopodium formation. These results demonstrate a potential role for ClpL in pneumococcal resistance to host cell adherence during infection. This study provides insight into further understanding the interactions between hosts and pathogens.
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