Selected Papers from the Lakeside Conference on Protein Toxins and Effectors 2022

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Bacterial Toxins".

Deadline for manuscript submissions: closed (20 December 2023) | Viewed by 2267

Special Issue Editors


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Guest Editor
Microbiology and Immunology, Medical College of Wisconsin, 8701 Watertown Plank Rd., Microbiology and Immunology, BSB-255, Milwaukee, WI 53226, USA
Interests: protein toxins; type-III effectors; structure-based mechanisms of toxin action; botulinum toxins; tetanus toxin; cellular microbiology
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Guest Editor
Dept. of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA
Interests: bacterial pathogenesis; biochemistry of proteins; cellular microbiology; cytoskeleton; global health; immunology; bacterial infectious diseases; structural biology

Special Issue Information

Dear Colleagues,

The International Conference, Lakeside Conference on Protein Toxins and Effectors (LakesidePTE) focuses on mechanistic studies on protein toxins and effectors. The next LakesidePTE Conference will be held on 2-4 October 2022 at the Abbey Resort in Lake Geneva, WI, USA.

The Organizing Committee is collaborating with Toxins to call for a Special Issue related to the research presented during LakesidePTE. We are inviting, in person or virtual, registrants of the conference to submit a manuscript or review that has not been previously published.  We will accept research articles, short communications, and review articles. We anticipate that articles will contain new and important findings discussed during the conference including mechanistic aspects of protein toxin and effector action, the discovery of new protein toxins or effectors, and the study of protein toxin or effector action within cells, and will engage in interbacterial competition, using cellular microbiology approaches. All submissions will be peer-reviewed.  

Link to the LakesidePTE Conference 2022: http://event.fourwaves.com/lakesidePTE2022

Prof. Dr. Joseph Barbieri
Prof. Dr. Karla J. F. Satchell
Guest Editors

Manuscript Submission Information

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Keywords

  • protein toxins
  • effectors
  • structure-based mechanisms of protein toxin or effector action
  • discovery of new protein toxins or effectors
  • cellular microbiology approaches to study protein toxin or effector action in host cells
  • how microbes secrete and inject toxins to engage in interbacterial competition

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Published Papers (1 paper)

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Research

11 pages, 3616 KiB  
Article
Dynamics and Molecular Interactions of GPI-Anchored CD59
by Tomas B. Voisin, Emma C. Couves, Edward W. Tate and Doryen Bubeck
Toxins 2023, 15(7), 430; https://doi.org/10.3390/toxins15070430 - 30 Jun 2023
Cited by 2 | Viewed by 1643
Abstract
CD59 is a GPI-anchored cell surface receptor that serves as a gatekeeper to controlling pore formation. It is the only membrane-bound inhibitor of the complement membrane attack complex (MAC), an immune pore that can damage human cells. While CD59 blocks MAC pores, the [...] Read more.
CD59 is a GPI-anchored cell surface receptor that serves as a gatekeeper to controlling pore formation. It is the only membrane-bound inhibitor of the complement membrane attack complex (MAC), an immune pore that can damage human cells. While CD59 blocks MAC pores, the receptor is co-opted by bacterial pore-forming proteins to target human cells. Recent structures of CD59 in complexes with binding partners showed dramatic differences in the orientation of its ectodomain relative to the membrane. Here, we show how GPI-anchored CD59 can satisfy this diversity in binding modes. We present a PyLipID analysis of coarse-grain molecular dynamics simulations of a CD59-inhibited MAC to reveal residues of complement proteins (C6:Y285, C6:R407 C6:K412, C7:F224, C8β:F202, C8β:K326) that likely interact with lipids. Using modules of the MDAnalysis package to investigate atomistic simulations of GPI-anchored CD59, we discover properties of CD59 that encode the flexibility necessary to bind both complement proteins and bacterial virulence factors. Full article
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