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Structure of the head of the Bartonella adhesin BadA

Pawel Szczesny1, Dirk Linke, Astrid Ursinus

  • 1Department of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.

Plos Pathogens
|August 9, 2008
PubMed

Insights

Trimeric autotransporter adhesins (TAAs) are key bacterial adhesion proteins. Structural analysis of Bartonella henselae BadA reveals its head is a mosaic of domains from other TAAs, showcasing pathogen evolution.

Area of Science:

  • Microbiology
  • Structural Biology
  • Protein Science

Background:

  • Trimeric autotransporter adhesins (TAAs) are crucial virulence factors enabling pathogenic proteobacteria to adhere to host tissues.
  • TAAs are characterized by a conserved head-stalk-anchor structure, with the head domain mediating host cell attachment and autoagglutination.

Purpose of the Study:

  • To elucidate the three-dimensional structure of the head domain of Bartonella henselae BadA, a major adhesin.
  • To understand the structural basis of adhesion and autoagglutination mediated by BadA.

Main Methods:

  • X-ray crystallography was employed to determine the structure of the BadA head domains to a resolution of 1.1 Å.
  • Bioinformatic analyses were performed to compare the determined structures with known TAA domains.

Main Results:

  • The BadA head comprises three domains; the N-terminal domain shares similarity with Yersinia YadA.
  • The other two domains, determined via crystallography, are beta-prisms with unique fold architectures.
  • Structural comparison revealed similarities to domains from Haemophilus Hia, despite low sequence homology, suggesting domain permutation.

Conclusions:

  • The BadA head is a chimera, integrating domains from different TAAs (YadA and Hia).
  • This highlights a combinatorial evolutionary strategy in bacterial adhesin development.
  • Understanding TAA structure-function relationships is vital for developing novel anti-adhesion therapies.

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