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T6SS-associated Rhs toxin-encapsulating shells: Structural and bioinformatical insights into bacterial weaponry and

Claudia S Kielkopf1, Mikhail M Shneider2, Petr G Leiman3

  • 1Structural Biology of Molecular Machines Group, Protein Structure & Function Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.

Structure (London, England : 1993)
|October 31, 2024
PubMed
Summary
This summary is machine-generated.

The bacterial type VI secretion system (T6SS) Rhs core protein forms a protective shell for toxin delivery. This structure safeguards the producing cell and facilitates intracellular toxin release into target cells.

Keywords:
PAARRhsVgrGX-ray crystallographytoxintype 6 secretion system

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Area of Science:

  • Microbiology
  • Structural Biology
  • Bacterial Pathogenesis

Background:

  • The type VI secretion system (T6SS) is a complex molecular machine used by bacteria for inter-bacterial and host cell interactions.
  • Rearrangement hotspot (Rhs) proteins are prevalent effectors delivered by the T6SS, possessing diverse C-terminal toxin domains and conserved YD-repeat-containing cores.
  • Understanding the structure of Rhs cores is crucial for elucidating their function in toxin delivery and host-pathogen interactions.

Purpose of the Study:

  • To determine the three-dimensional structures of Rhs core proteins from Salmonella bongori and Advenella mimigardefordensis.
  • To investigate the structural organization of the Rhs core and its relationship with associated toxin domains.
  • To elucidate the functional implications of the Rhs core structure in toxin delivery and bacterial defense mechanisms.

Main Methods:

  • X-ray crystallography was employed to resolve the structures of PAAR- and VgrG-linked Rhs core proteins.
  • Bioinformatics analysis was utilized to assess the intracellular localization and function of Rhs toxins.
  • Comparative structural analysis was performed to understand conserved features of the Rhs core.

Main Results:

  • The Rhs core structures were elucidated, revealing a large shell-like assembly primarily composed of beta-sheets with a negatively charged internal cavity.
  • The C-terminal toxin domain of the Salmonella bongori Rhs protein did not exhibit ordered density within the Rhs shell, suggesting it is unfolded.
  • Bioinformatics data indicated that Rhs toxins primarily function intracellularly.

Conclusions:

  • The Rhs core acts as a protective compartment, shielding the toxin from the producing cell's cytoplasm.
  • The Rhs core functions as an efficient delivery apparatus, facilitating the translocation of the toxin into target cells.
  • The structural and functional data suggest a dual role for the Rhs core: a self-protection mechanism and a specialized toxin delivery system.