IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v16y2025i1d10.1038_s41467-025-63426-x.html
   My bibliography  Save this article

Secretins of type-two secretion systems are necessary for exopolymeric slime secretion in cyanobacteria and myxobacteria

Author

Listed:
  • David M. Zuckerman

    (Iona University)

  • Jeffery Man To So

    (University of Sheffield)

  • Egbert Hoiczyk

    (University of Sheffield)

Abstract

Cyanobacteria and myxobacteria display gliding motility associated with the secretion of an exopolymeric slime through nozzle-like structures. Here, we use biochemical and structural assays to show that these nozzles are composed of secretins of the PilQ/GspD family, which are known to form outer membrane gates in type-two secretion systems (T2SSs) and other bacterial protein secretion systems. We show that gspD is an essential gene in Myxococcus xanthus, and its downregulation by conditional knockdown renders this bacterium defective in both slime secretion and gliding motility. In cyanobacteria, available data suggest that the exopolymeric slime is a polysaccharide, although the precise nature of the slime in myxobacteria remains unclear. Our results, therefore, indicate that secretins may be required for the secretion of non-proteinaceous polymers in certain bacteria.

Suggested Citation

  • David M. Zuckerman & Jeffery Man To So & Egbert Hoiczyk, 2025. "Secretins of type-two secretion systems are necessary for exopolymeric slime secretion in cyanobacteria and myxobacteria," Nature Communications, Nature, vol. 16(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-63426-x
    DOI: 10.1038/s41467-025-63426-x
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-025-63426-x
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-025-63426-x?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Benjamin Wiseman & Ram Gopal Nitharwal & Göran Widmalm & Martin Högbom, 2021. "Structure of a full-length bacterial polysaccharide co-polymerase," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    2. Yun Yang & Jiwei Liu & Bradley R. Clarke & Laura Seidel & Jani R. Bolla & Philip N. Ward & Peijun Zhang & Carol V. Robinson & Chris Whitfield & James H. Naismith, 2021. "The molecular basis of regulation of bacterial capsule assembly by Wzc," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    3. Changjiang Dong & Konstantinos Beis & Jutta Nesper & Anne L. Brunkan-LaMontagne & Bradley R. Clarke & Chris Whitfield & James H. Naismith, 2006. "Wza the translocon for E. coli capsular polysaccharides defines a new class of membrane protein," Nature, Nature, vol. 444(7116), pages 226-229, November.
    4. Salim T Islam & Israel Vergara Alvarez & Fares Saïdi & Annick Guiseppi & Evgeny Vinogradov & Gaurav Sharma & Leon Espinosa & Castrese Morrone & Gael Brasseur & Jean-François Guillemot & Anaïs Benarouc, 2020. "Modulation of bacterial multicellularity via spatio-specific polysaccharide secretion," PLOS Biology, Public Library of Science, vol. 18(6), pages 1-31, June.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Yun Yang & Mariana Batista & Bradley R. Clarke & Michelle R. Agyare-Tabbi & Haigang Song & Noah M. Kuehfuss & Audrey Bas & Carol V. Robinson & Chris Whitfield & Phillip J. Stansfeld & James H. Naismit, 2025. "Molecular basis for the phosphorylation of bacterial tyrosine kinase Wzc," Nature Communications, Nature, vol. 16(1), pages 1-13, December.
    2. Robby Concha-Eloko & Beatriz Beamud & Pilar Domingo-Calap & Rafael Sanjuán, 2025. "Unlocking data in Klebsiella lysogens to predict capsular type-specificity of phage depolymerases," Nature Communications, Nature, vol. 16(1), pages 1-14, December.
    3. Smrithi Krishnan R & Kalyanashis Jana & Amina H. Shaji & Karthika S. Nair & Anjali Devi Das & Devika Vikraman & Harsha Bajaj & Ulrich Kleinekathöfer & Kozhinjampara R. Mahendran, 2022. "Assembly of transmembrane pores from mirror-image peptides," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    4. Salim T Islam & Israel Vergara Alvarez & Fares Saïdi & Annick Guiseppi & Evgeny Vinogradov & Gaurav Sharma & Leon Espinosa & Castrese Morrone & Gael Brasseur & Jean-François Guillemot & Anaïs Benarouc, 2020. "Modulation of bacterial multicellularity via spatio-specific polysaccharide secretion," PLOS Biology, Public Library of Science, vol. 18(6), pages 1-31, June.
    5. Jinsheng Tang & Mengru Guo & Min Chen & Bin Xu & Tingting Ran & Weiwu Wang & Zhe Ma & Huixing Lin & Hongjie Fan, 2023. "A link between STK signalling and capsular polysaccharide synthesis in Streptococcus suis," Nature Communications, Nature, vol. 14(1), pages 1-22, December.
    6. Amandine Nucci & Eduardo P. C. Rocha & Olaya Rendueles, 2022. "Adaptation to novel spatially-structured environments is driven by the capsule and alters virulence-associated traits," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-63426-x. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.