Bona from acinetobacter baumannii forms a divisome-localized decamer that supports outer envelope function

Tools

Grinter, Rhys and Morris, Faye C. and Dunstan, Rhys A. and Leung, Pok Man and Kropp, Ashleigh and Belousoff, Matthew and Gunasinghe, Sachith D. and Scott, Nichollas E. and Beckham, Simone and Peleg, Anton Y. and Greening, Chris and Li, Jian and Heinz, Eva and Lithgow, Trevor (2021) Bona from acinetobacter baumannii forms a divisome-localized decamer that supports outer envelope function. mBio, 12 (4). e01480-21. ISSN 2161-2129 (https://doi.org/10.1128/mBio.01480-21)

[thumbnail of grinter-et-al-2021-bona-from-acinetobacter-baumannii-forms-a-divisome-localized-decamer-that-supports-outer-envelope]
Preview
 Text. Filename: grinter-et-al-2021-bona-from-acinetobacter-baumannii-forms-a-divisome-localized-decamer-that-supports-outer-envelope.pdf
Final Published Version
License: Creative Commons Attribution 4.0 logo
Download (4MB)| Preview

Abstract

Acinetobacter baumannii is a high-risk pathogen due to the rapid global spread of multidrug-resistant lineages. Its phylogenetic divergence from other ESKAPE pathogens means that determinants of its antimicrobial resistance can be difficult to extrapolate from other widely studied bacteria. A recent study showed that A. baumannii upregulates production of an outer membrane lipoprotein, which we designate BonA, in response to challenge with polymyxins. Here, we show that BonA has limited sequence similarity and distinct structural features compared to lipoproteins from other bacterial species. Analyses through X-ray crystallography, small-angle X-ray scattering, electron microscopy, and multiangle light scattering demonstrate that BonA has a dual BON (Bacterial OsmY and Nodulation) domain architecture and forms a decamer via an unusual oligomerization mechanism. This analysis also indicates this decamer is transient, suggesting dynamic oligomerization plays a role in BonA function. Antisera recognizing BonA shows it is an outer membrane protein localized to the divisome. Loss of BonA modulates the density of the outer membrane, consistent with a change in its structure or link to the peptidoglycan, and prevents motility in a clinical strain (ATCC 17978). Consistent with these findings, the dimensions of the BonA decamer are sufficient to permeate the pepti-doglycan layer, with the potential to form a membrane-spanning complex during cell division.

ORCID iDs

Grinter, Rhys, Morris, Faye C., Dunstan, Rhys A., Leung, Pok Man, Kropp, Ashleigh, Belousoff, Matthew, Gunasinghe, Sachith D., Scott, Nichollas E., Beckham, Simone, Peleg, Anton Y., Greening, Chris, Li, Jian, Heinz, Eva ORCID logoORCID: https://orcid.org/0000-0003-4413-3756 and Lithgow, Trevor;
  • Item type:Article
    ID code:90698
    Dates:
    Date
    Event
    August 2021
    Published
    27 July 2021
    Published Online
    14 June 2021
    Accepted
    Subjects:Science > Microbiology
    Department:UNSPECIFIED
    Depositing user: Pure Administrator
    Date deposited:24 Sep 2024 15:46
    Last modified:11 Nov 2024 14:27
    Related URLs:
    URI:https://strathprints.strath.ac.uk/id/eprint/90698
CORE (COnnecting REpositories)