ArticleMicrobial pathogenesis2012
The Mycobacterium avium ESX-5 PPE protein, PPE25-MAV, interacts with an ESAT-6 family Protein, MAV_2921, and localizes to the bacterial surface.
Article in Microbial pathogenesis, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Virulence ofVeterinary medicine international · 2026Article
- Delineating transcriptional crosstalk between Mycobacterium avium subsp. paratuberculosis and human THP-1 cells at the early stage of infection via dual RNA-seq analysis.Veterinary research · 2022Article
- Review
- Genetic Involvement ofInternational journal of molecular sciences · 2021Review
- Non-tuberculous mycobacteria and the rise of Mycobacterium abscessus.Nature reviews. Microbiology · 2020Review
- Characterization of membrane vesicles released by Mycobacterium avium in response to environment mimicking the macrophage phagosome.Future microbiology · 2019Article
- Quantitative analysis ofClinical proteomics · 2019Article
- The Voltage-Dependent Anion Channels (VDAC) of Mycobacterium avium phagosome are associated with bacterial survival and lipid export in macrophages.Scientific reports · 2017Article
- Identification of Mycobacterium avium subsp. hominissuis secreted proteins using an in vitro system mimicking the phagosomal environment.BMC microbiology · 2016Article
- The environment of "Mycobacterium avium subsp. hominissuis" microaggregates induces synthesis of small proteins associated with efficient infection of respiratory epithelial cells.Infection and immunity · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Previous research has demonstrated that inactivation of the Mycobacterium avium gene, PPE25-MAV (MAV_2928), leads to a significant attenuation of virulence in both in vitro and in vivo models. PPE25-MAV encodes for a PPE family protein, a family from which many members have been implicated in both bacterial virulence and host immune recognition. Recent research has shown that many PPE family proteins are exported by a specialized Type VII secretion system in mycobacteria. In this context, the mechanisms of PPE25-MAV in M. avium pathogenesis were investigated. A mycobacterial 2-hybrid system was used to perform a directed search for M. avium proteins that interact directly with PPE25-MAV. An interaction was observed between PPE25-MAV and the ESAT-6 family protein, MAV_2921, and was further defined by 2-hybrid analysis of truncated PPE25-MAV, and confirmed by co-immunoprecipitation. Localization of the PPE25-MAV protein was analyzed in Mycobacterium smegmatis expressing the recombinant protein and a significant percentage of PPE25-MAV was shown to be exposed at the bacterial surface by surface biotinylation and trypsin protection assays. Finally, transcriptional analysis of PPE25-MAV and its associated operon suggested that nutrient limitation, a condition which occurs in the phagosome, plays a role in regulating expression of the PPE25-MAV gene.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.