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

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

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)5989-5999
Number of pages11
JournalThe EMBO journal
Volume19
Issue number22
StatePublished - Nov 15 2000
Externally publishedYes

Fingerprint

Moraxella
Yersinia
Periodicity
Sequence Analysis
Head
Membranes
Moraxella (Branhamella) catarrhalis
Proteobacteria
Protein Sequence Analysis
Virulence Factors
Anchors
Oligomers
Membrane Proteins
Collagen
Genes
Electrons
Amino Acids
Molecules
Proteins

Keywords

  • Bacterial adhesin
  • Coiled coils
  • Electron microscopy
  • Pathogenicity
  • Proteobacteria

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

Hoiczyk, E., Roggenkamp, A., Reichenbecher, M., Lupas, A., & Heesemann, J. (2000). Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins. The EMBO journal, 19(22), 5989-5999.

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.

In: The EMBO journal, Vol. 19, No. 22, 15.11.2000, p. 5989-5999.

Research output: Contribution to journalArticle

Hoiczyk, E, Roggenkamp, A, Reichenbecher, M, Lupas, A & Heesemann, J 2000, 'Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins', The EMBO journal, vol. 19, no. 22, pp. 5989-5999.
Hoiczyk E, Roggenkamp A, Reichenbecher M, Lupas A, Heesemann J. Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins. The EMBO journal. 2000 Nov 15;19(22):5989-5999.
Hoiczyk, Egbert ; Roggenkamp, Andreas ; Reichenbecher, Marisa ; Lupas, Andrei ; Heesemann, Jürgen. / Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins. In: The EMBO journal. 2000 ; Vol. 19, No. 22. pp. 5989-5999.
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