ArticlePloS one2014
Impact of protein domains on PE_PGRS30 polar localization in Mycobacteria.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Mycobacterium tuberculosis infects human peripheral hematopoietic multipotent progenitors and promotes their myeloid differentiation in vitro.Cell death & disease · 2026Article
- Unraveling the potential of graphene quantum dots againstFrontiers in microbiology · 2024Article
- Mycobacterial protein PE_PGRS30 induces macrophage apoptosis through prohibitin 2 mitochondrial function interference.Frontiers in microbiology · 2023Article
- PE_PGRS3 ensures provision of the vital phospholipids cardiolipin and phosphatidylinositols by promoting the interaction betweenVirulence · 2021Article
- Codon Optimization, Soluble Expression and Purification of PE_PGRS45 Gene fromJournal of microbiology and biotechnology · 2021Article
- Graphene nanoplatelet and graphene oxide functionalization of face mask materials inhibits infectivity of trapped SARS-CoV-2.iScience · 2021Article
- Intracellular localization of the mycobacterial stressosome complex.Scientific reports · 2021Article
- PE_PGRS proteins ofVirulence · 2020Review
- Graphene Oxide-Linezolid Combination as Potential New Anti-Tuberculosis Treatment.Nanomaterials (Basel, Switzerland) · 2020Article
- PE_PGRS31-S100A9 Interaction Promotes Mycobacterial Survival in Macrophages Through the Regulation of NF-κB-TNF-α Signaling and Arachidonic Acid Metabolism.Frontiers in microbiology · 2020Article
- A Repurposing Approach for Uncovering the Anti-Tubercular Activity of FDA-Approved Drugs with Potential Multi-Targeting Profiles.Molecules (Basel, Switzerland) · 2019Article
- Graphene oxide prevents mycobacteria entry into macrophages through extracellular entrapment.Nanoscale advances · 2019Article
- The Enigmatic PE/PPE Multigene Family of Mycobacteria and Tuberculosis Vaccination.Infection and immunity · 2017Review
- Impact ofFrontiers in cellular and infection microbiology · 2017Article
- PE_PGRS33 Contributes to Mycobacterium tuberculosis Entry in Macrophages through Interaction with TLR2.PloS one · 2016Article
Corrections and comments
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Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PE_PGRS proteins are unique to the Mycobacterium tuberculosis complex and a number of other pathogenic mycobacteria. PE_PGRS30, which is required for the full virulence of M. tuberculosis (Mtb), has three main domains, i.e. an N-terminal PE domain, repetitive PGRS domain and the unique C-terminal domain. To investigate the role of these domains, we expressed a GFP-tagged PE_PGRS30 protein and a series of its functional deletion mutants in different mycobacterial species (Mtb, Mycobacterium bovis BCG and Mycobacterium smegmatis) and analysed protein localization by confocal microscopy. We show that PE_PGRS30 localizes at the mycobacterial cell poles in Mtb and M. bovis BCG but not in M. smegmatis and that the PGRS domain of the protein strongly contributes to protein cellular localization in Mtb. Immunofluorescence studies further showed that the unique C-terminal domain of PE_PGRS30 is not available on the surface, except when the PGRS domain is missing. Immunoblot demonstrated that the PGRS domain is required to maintain the protein strongly associated with the non-soluble cellular fraction. These results suggest that the repetitive GGA-GGN repeats of the PGRS domain contain specific sequences that contribute to protein cellular localization and that polar localization might be a key step in the PE_PGRS30-dependent virulence mechanism.
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