ArticleThe Journal of biological chemistry2013
The 2.5 Å structure of the enterococcus conjugation protein TraM resembles VirB8 type IV secretion proteins.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 58 citations in OpenAlex.
- Type IV secretion systems: reconciling diversity through a unified nomenclature.FEMS microbiology reviews · 2026Review
- The type IV secretion system ofMicrobial genomics · 2025Article
- Inner membrane components of the plasmid pKM101 type IV secretion system TraE and TraD are DNA-binding proteins.Scientific reports · 2025Article
- Elucidating assembly and function of VirB8 cell wall subunits refines the DNA translocation model in Gram-positive T4SSs.Science advances · 2025Article
- Small Things Matter: The 11.6-kDa TraB Protein is Crucial for Antibiotic Resistance Transfer Among Enterococci.Frontiers in molecular biosciences · 2022Article
- Structural and Biochemical Analysis of OrfG: The VirB8-like Component of the Conjugative Type IV Secretion System of ICEFrontiers in molecular biosciences · 2021Article
- Protein interactions within and between two F-type type IV secretion systems.Molecular microbiology · 2020Article
- TraN: A novel repressor of an Enterococcus conjugative type IV secretion system.Nucleic acids research · 2018Article
- VirB8 homolog TraE from plasmid pKM101 forms a hexameric ring structure and interacts with the VirB6 homolog TraD.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Type IV secretion in Gram-negative and Gram-positive bacteria.Molecular microbiology · 2018Review
- Article
- Fragment-based screening identifies novel targets for inhibitors of conjugative transfer of antimicrobial resistance by plasmid pKM101.Scientific reports · 2017Article
- Structural Analysis and Inhibition of TraE from the pKM101 Type IV Secretion System.The Journal of biological chemistry · 2016Article
- The Mosaic Type IV Secretion Systems.EcoSal Plus · 2016Review
- The Rickettsia type IV secretion system: unrealized complexity mired by gene family expansion.Pathogens and disease · 2016Article
- VirB8-like protein TraH is crucial for DNA transfer in Enterococcus faecalis.Scientific reports · 2016Article
- Article
- Critical Components of the Conjugation Machinery of the Integrative and Conjugative Element ICEBs1 of Bacillus subtilis.Journal of bacteriology · 2015Article
- Molecular and structural analysis of Legionella DotI gives insights into an inner membrane complex essential for type IV secretion.Scientific reports · 2015Article
- Two novel membrane proteins, TcpD and TcpE, are essential for conjugative transfer of pCW3 in Clostridium perfringens.Journal of bacteriology · 2015Article
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Authors and funding
11 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conjugative plasmid transfer is the most important means of spreading antibiotic resistance and virulence genes among bacteria and therefore presents a serious threat to human health. The process requires direct cell-cell contact made possible by a multiprotein complex that spans cellular membranes and serves as a channel for macromolecular secretion. Thus far, well studied conjugative type IV secretion systems (T4SS) are of Gram-negative (G-) origin. Although many medically relevant pathogens (e.g., enterococci, staphylococci, and streptococci) are Gram-positive (G+), their conjugation systems have received little attention. This study provides structural information for the transfer protein TraM of the G+ broad host range Enterococcus conjugative plasmid pIP501. Immunolocalization demonstrated that the protein localizes to the cell wall. We then used opsonophagocytosis as a novel tool to verify that TraM was exposed on the cell surface. In these assays, antibodies generated to TraM recruited macrophages and enabled killing of pIP501 harboring Enteroccocus faecalis cells. The crystal structure of the C-terminal, surface-exposed domain of TraM was determined to 2.5 Å resolution. The structure, molecular dynamics, and cross-linking studies indicated that a TraM trimer acts as the biological unit. Despite the absence of sequence-based similarity, TraM unexpectedly displayed a fold similar to the T4SS VirB8 proteins from Agrobacterium tumefaciens and Brucella suis (G-) and to the transfer protein TcpC from Clostridium perfringens plasmid pCW3 (G+). Based on the alignments of secondary structure elements of VirB8-like proteins from mobile genetic elements and chromosomally encoded T4SS from G+ and G- bacteria, we propose a new classification scheme of VirB8-like proteins.
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