Interaction of RTX toxins with the host cell plasma membrane
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Feby M. Chacko
Feby M. Chacko did her integrated bachelor’s and master’s degree in Biology and Chemistry from Indian Institute of Science Education and Research, Thiruvananthapuram. For her master’s thesis, she screened for membrane fission catalysts in bacterial cells using Supported Membrane Tube (SMrT) assay system. After her graduation in 2019 from India, she moved to Germany in 2020 and started pursuing her PhD in Institute of Biochemistry, Heinrich Heine University Düsseldorf. Her work focused on the mechanism of RTX toxins.
Lutz Schmitt did his master’s in Chemistry at the University of Freiburg and obtained his PhD from the Technical University Munich. After a Post Doc at Stanford University, he moved as a DFG-funded Emmy Noether fellow to the University of Marburg and University of Frankfurt. In 2005 he was appointed as Professor of Biochemistry at Heinrich Heine University Düsseldorf. His research interest are recognition processes at membranes and transport across membranes with an emphasis on ABC transporters.
Abstract
Repeats in ToXins (RTX) protein family is a group of exoproteins secreted by Type 1 secretion system (T1SS) of several Gram-negative bacteria. The term RTX is derived from the characteristic nonapeptide sequence (GGxGxDxUx) present at the C-terminus of the protein. This RTX domain binds to calcium ions in the extracellular medium after being secreted out of the bacterial cells, and this facilitates folding of the entire protein. The secreted protein then binds to the host cell membrane and forms pores via a complex pathway, which eventually leads to the cell lysis. In this review, we summarize two different pathways in which RTX toxins interact with host cell membrane and discuss the possible reasons for specific and unspecific activity of RTX toxins to different types of host cells.
Funding source: Jürgen Manchot Stiftung
Award Identifier / Grant number: MOI IV
About the authors
Feby M. Chacko did her integrated bachelor’s and master’s degree in Biology and Chemistry from Indian Institute of Science Education and Research, Thiruvananthapuram. For her master’s thesis, she screened for membrane fission catalysts in bacterial cells using Supported Membrane Tube (SMrT) assay system. After her graduation in 2019 from India, she moved to Germany in 2020 and started pursuing her PhD in Institute of Biochemistry, Heinrich Heine University Düsseldorf. Her work focused on the mechanism of RTX toxins.
Lutz Schmitt did his master’s in Chemistry at the University of Freiburg and obtained his PhD from the Technical University Munich. After a Post Doc at Stanford University, he moved as a DFG-funded Emmy Noether fellow to the University of Marburg and University of Frankfurt. In 2005 he was appointed as Professor of Biochemistry at Heinrich Heine University Düsseldorf. His research interest are recognition processes at membranes and transport across membranes with an emphasis on ABC transporters.
Acknowledgements
We thank all current and former members of the Institute of Biochemistry, the Center of Advanced Imaging (CAi), and the Center for Structural Studies (CSS), Heinrich Heine University Düsseldorf for support and stimulating discussions. Research on RTX toxins is supported by the Jürgen Manchot Graduate School “Molecules of Infections” (to L.S.).
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Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.
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Research funding: This work was financially supported by the Jürgen Manchot Stiftung (MOI IV).
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Conflict of interest statement: The authors declare no conflicts of interest regarding this article.
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© 2023 Walter de Gruyter GmbH, Berlin/Boston
Artikel in diesem Heft
- Frontmatter
- Highlight: Membrane Proteins from Structure to Function
- The Rauischholzhausen Transport Colloquium: membrane proteins from structure to function
- Determination of membrane protein orientation upon liposomal reconstitution down to the single vesicle level
- Interaction of RTX toxins with the host cell plasma membrane
- Interactions of Na+/taurocholate cotransporting polypeptide with host cellular proteins upon hepatitis B and D virus infection: novel potential targets for antiviral therapy
- Mycobacterial type VII secretion systems
- Lipid exchange among electroneutral Sulfo-DIBMA nanodiscs is independent of ion concentration
- Membrane-anchored substrate binding proteins are deployed in secondary TAXI transporters
- ATP binding and ATP hydrolysis in full-length MsbA monitored via time-resolved Fourier transform infrared spectroscopy
Artikel in diesem Heft
- Frontmatter
- Highlight: Membrane Proteins from Structure to Function
- The Rauischholzhausen Transport Colloquium: membrane proteins from structure to function
- Determination of membrane protein orientation upon liposomal reconstitution down to the single vesicle level
- Interaction of RTX toxins with the host cell plasma membrane
- Interactions of Na+/taurocholate cotransporting polypeptide with host cellular proteins upon hepatitis B and D virus infection: novel potential targets for antiviral therapy
- Mycobacterial type VII secretion systems
- Lipid exchange among electroneutral Sulfo-DIBMA nanodiscs is independent of ion concentration
- Membrane-anchored substrate binding proteins are deployed in secondary TAXI transporters
- ATP binding and ATP hydrolysis in full-length MsbA monitored via time-resolved Fourier transform infrared spectroscopy
