ArticleBMC molecular biology2009
Identification of two proteins that interact with the Erp virulence factor from Mycobacterium tuberculosis by using the bacterial two-hybrid system.
Article in BMC molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
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- Discovery of potent antimycobacterial agents targeting lumazine synthase (RibH) of Mycobacterium tuberculosis.Scientific reports · 2024Article
- Study of the Rv1417 and Rv2617c Membrane Proteins and Their Interactions with Nicotine Derivatives as Potential Inhibitors of Erp Virulence-Associated Factor inBiomolecules · 2023Article
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- Rv2617c and P36 are virulence factors of pathogenic mycobacteria involved in resistance to oxidative stress.Virulence · 2019Article
- In Vivo Methods to Study Protein-Protein Interactions as Key Players inPathogens (Basel, Switzerland) · 2019Review
- Endogenous and Exogenous KdpF Peptide Increases Susceptibility ofFrontiers in cellular and infection microbiology · 2017Article
- Interaction of Erp Protein of Mycobacterium tuberculosis with Rv2212 Enhances Intracellular Survival of Mycobacterium smegmatis.Journal of bacteriology · 2016Article
- The Bacterial Two-Hybrid System Uncovers the Involvement of Acetylation in Regulating of Lrp Activity inFrontiers in microbiology · 2016Article
- Identification of Novel Potential Vaccine Candidates against Tuberculosis Based on Reverse Vaccinology.BioMed research international · 2015Article
- Striking the Right Balance Determines TB or Not TB.Frontiers in immunology · 2014Review
- Article
- One-plasmid tunable coexpression for mycobacterial protein-protein interaction studies.Protein science : a publication of the Protein Society · 2009Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe exported repetitive protein (erp) gene encodes a secreted 36-kDa protein with a central domain containing several proline-glycine-leucine-threonine-serine (PGLTS) repeats. It has been demonstrated that erp is a virulence-associated factor since the disruption of this gene impairs the growth of Mycobacterium bovis and Mycobacterium tuberculosis in mice.
resultsIn order to elucidate the function of Erp we searched for Erp-binding proteins from M. tuberculosis by using a bacterial two-hybrid system. Our results indicate that Erp interacts specifically with two putative membrane proteins, Rv1417 and Rv2617c. Further analysis revealed that the latter two interact with each other, indicating that Rv1417, Rv2617c and Erp are connected through multiple interactions. While Rv1417 is disseminated in several Actinomycetales genera, orthologues of Rv2617c are exclusively present in members of the M. tuberculosis complex (MTC). The central and amino-terminal regions of Erp were determined to be involved in the interaction with Rv1417 and Rv2627c. Erp forms from Mycobacterium smegmatis and Mycobacterium leprae were not able to interact with Rv2617c in two-hybrid assays. Immunolocalization experiments showed that Rv1417 and Rv2617c are found on the cell membrane and Erp on the bacterial cell wall. Finally, comparative genomics and expression studies revealed a possible role of Rv1417 in riboflavin metabolism.
conclusionWe identified interactive partners of Erp, an M. tuberculosis protein involved in virulence, which will be the focus of future investigation to decipher the function of the Erp family protein.
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