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Aggregative adherence fimbriae form compact structures as seen by SAXS

Jønsson, Rie ; Björling, Alexander LU ; Midtgaard, Søren Roi ; Jensen, Grethe Vestergaard ; Skar-Gislinge, Nicholas ; Arleth, Lise ; Matthews, Steve ; Krogfelt, Karen Angeliki and Jenssen, Håvard (2023) In Scientific Reports 13(1).
Abstract

Bacterial colonization is mediated by fimbriae, which are thin hair-like appendages dispersed from the bacterial surface. The aggregative adherence fimbriae from enteroaggregative E. coli are secreted through the outer membrane and consist of polymerized minor and major pilin subunits. Currently, the understanding of the structural morphology and the role of the minor pilin subunit in the polymerized fimbriae are limited. In this study we use small-angle X-ray scattering to reveal the structural morphology of purified fimbriae in solution. We show that the aggregative fimbriae are compact arrangements of subunit proteins Agg5A + Agg3B which are assembled pairwise on a flexible string rather than extended in relatively straight... (More)

Bacterial colonization is mediated by fimbriae, which are thin hair-like appendages dispersed from the bacterial surface. The aggregative adherence fimbriae from enteroaggregative E. coli are secreted through the outer membrane and consist of polymerized minor and major pilin subunits. Currently, the understanding of the structural morphology and the role of the minor pilin subunit in the polymerized fimbriae are limited. In this study we use small-angle X-ray scattering to reveal the structural morphology of purified fimbriae in solution. We show that the aggregative fimbriae are compact arrangements of subunit proteins Agg5A + Agg3B which are assembled pairwise on a flexible string rather than extended in relatively straight filaments. Absence of the minor subunit leads to less compact fimbriae, but did not affect the length. The study provides novel insights into the structural morphology and assembly of the aggregative adherence fimbriae. Our study suggests that the minor subunit is not located at the tip of the fimbriae as previously speculated but has a higher importance for the assembled fimbriae by affecting the global structure.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Scientific Reports
volume
13
issue
1
article number
16516
publisher
Nature Publishing Group
external identifiers
  • pmid:37783694
  • scopus:85173027554
ISSN
2045-2322
DOI
10.1038/s41598-023-42079-0
language
English
LU publication?
yes
id
a066f367-8f68-40e5-908b-a0caf743a52a
date added to LUP
2023-12-07 08:59:19
date last changed
2024-04-20 03:22:03
@article{a066f367-8f68-40e5-908b-a0caf743a52a,
  abstract     = {{<p>Bacterial colonization is mediated by fimbriae, which are thin hair-like appendages dispersed from the bacterial surface. The aggregative adherence fimbriae from enteroaggregative E. coli are secreted through the outer membrane and consist of polymerized minor and major pilin subunits. Currently, the understanding of the structural morphology and the role of the minor pilin subunit in the polymerized fimbriae are limited. In this study we use small-angle X-ray scattering to reveal the structural morphology of purified fimbriae in solution. We show that the aggregative fimbriae are compact arrangements of subunit proteins Agg5A + Agg3B which are assembled pairwise on a flexible string rather than extended in relatively straight filaments. Absence of the minor subunit leads to less compact fimbriae, but did not affect the length. The study provides novel insights into the structural morphology and assembly of the aggregative adherence fimbriae. Our study suggests that the minor subunit is not located at the tip of the fimbriae as previously speculated but has a higher importance for the assembled fimbriae by affecting the global structure.</p>}},
  author       = {{Jønsson, Rie and Björling, Alexander and Midtgaard, Søren Roi and Jensen, Grethe Vestergaard and Skar-Gislinge, Nicholas and Arleth, Lise and Matthews, Steve and Krogfelt, Karen Angeliki and Jenssen, Håvard}},
  issn         = {{2045-2322}},
  language     = {{eng}},
  number       = {{1}},
  publisher    = {{Nature Publishing Group}},
  series       = {{Scientific Reports}},
  title        = {{Aggregative adherence fimbriae form compact structures as seen by SAXS}},
  url          = {{http://dx.doi.org/10.1038/s41598-023-42079-0}},
  doi          = {{10.1038/s41598-023-42079-0}},
  volume       = {{13}},
  year         = {{2023}},
}