Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins

Hoiczyk, Egbert; Roggenkamp, Andreas; Reichenbecher, Marisa; Lupas, Andrei; Heesemann, Jürgen

doi:10.1093/emboj/19.22.5989

Cited by 359Yersinia bacterium, plague, ectoparasites researchBiochemical and Structural CharacterizationBacterial Genetics and Biotechnology

Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins

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Hoiczyk, Egbert, Roggenkamp, Andreas, Reichenbecher, Marisa, Lupas, Andrei, Heesemann, Jürgen·2000·The EMBO Journal

DOI 10.1093/emboj/19.22.5989PMC PMC305836

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Abstract

The non-fimbrial adhesins, YadA of enteropathogenic Yersinia species, and UspA1 and UspA2 of Moraxella catarrhalis, are established pathogenicity factors. In electron micrographs, both surface proteins appear as distinct 'lollipop'-shaped structures forming a novel type of surface projection on the outer membranes. These structures, amino acid sequence analysis of these molecules and yadA gene manipulation suggest a tripartite organization: an N-terminal oval head domain is followed by a putative coiled-coil rod and terminated by a C-terminal membrane anchor domain. In YadA, the head domain is involved in autoagglutination and binding to host cells and collagen. Analysis of the coiled-coil segment of YadA revealed unusual pentadecad repeats with a periodicity of 3.75, which differs significantly from the 3.5 periodicity found in the Moraxella UspAs and other canonical coiled coils. These findings predict that the surface projections are formed by oligomers containing right- (Yersinia) or left-handed (Moraxella) coiled coils. Strikingly, sequence comparison revealed that related proteins are found in many proteobacteria, both human pathogenic and environmental species, suggesting a common role in adaptation to specific ecological niches.

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In the case of trimeric autotransporter adhesins (TAAs), electron microscopy shows the sticky, globular head domains of the lollipop-like molecules interacting in a zipper-like fashion.
“In the case of TAAs, electron microscopy shows the sticky, globular head domains of the lollipop-like molecules interacting in a zipper-like fashion (Figure 1D) [34],[40],[78],[84].”
From Bacterial autoaggregation (2018) · cites this paper as [78]

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Authors: Hoiczyk, E., Roggenkamp, A., Reichenbecher, M., Lupas, A., & Heesemann, J.
Affiliations: Max-von-Pettenkofer-Institut für Hygiene und Medizinische Mikrobiologie (DE)
Corresponding author: Heesemann, Jürgen
ORCID: Hoiczyk, Egbert
Lupas, Andrei
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2000-11-15
Volume: 19
Issue: 22
Pages: 5989-5999
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1093/emboj/19.22.5989
PMC: PMC305836
OpenAlex: W2071393605
Cited by: 359
References: 51
Citations by year: 2026: 3 · 2025: 3 · 2024: 4 · 2023: 8 · 2022: 5 · 2021: 4 · 2020: 4 · 2019: 13 · 2018: 9 · 2017: 8 · 2016: 11 · 2015: 12 · 2014: 14 · 2013: 17 · 2012: 17
FWCI: 6.05
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
MPG.PuRe (Max Planck Society) (submittedVersion)
Funders: University of Washington
Deutsche Forschungsgemeinschaft
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Yersinia bacterium, plague, ectoparasites research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords: YadA, Yersinia, Moraxella catarrhalis, coiled-coil proteins, autoagglutination, collagen binding, protein oligomerization, Proteobacteria
MeSH terms: Amino Acid Sequence, Bacterial Outer Membrane Proteins, Moraxella catarrhalis, Cell Membrane, Genes, Bacterial, Humans, Microscopy, Electron, Molecular Sequence Data, Mutation, Virulence, Yersinia enterocolitica, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Adhesins, Bacterial

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Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins

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