Crystallization and preliminary crystallographic analysis of BbCRASP-1, a complement regulator-acquiring surface protein of Borrelia burgdorferi

Authors: Cordes, Frank S.; Kraiczy, Peter; Roversi, Pietro; Skerka, Christine; Kirschfink, Michael; Simon, Markus M.; Brade, Volker; Lowe, Edward D.; Zipfel, Peter; Wallich, Reinhard; Lea, Susan M.

Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 929-932(4)

Publisher: Blackwell Publishing

Key:

- Free Content

- New Content

- Subscribed Content

- Free Trial Content

Abstract:

Borrelia burgdorferi is the causative agent of Lyme disease. Serum-resistant strains of the pathogen are able to reduce the host's immune response to infection by recruiting fluid-phase complement regulators from the serum. B. burgdorferi complement regulator-acquiring surface protein-1 (BbCRASP-1) binds factor H and factor-H-like protein-1 to the bacterial surface, where they actively down-regulate complement response. Crystals of native and selenomethionine-substituted BbCRASP-1 have been obtained and a native data set to 2.7 Å as well as selenomethionine MAD data to 3.2 Å resolution have been collected. The selenium substructure has been solved and initial phases have been refined to 3.0 Å by density-modification methods. Model building and refinement are under way.

Keywords: Borrelia burgdorferi; complement; factor H; innate immunity; immune evasion

Document Type: Research article

DOI: 10.1107/S090744490400472X

The full text electronic article is available for purchase. You will be able to download the full text electronic article after payment.

$50.16 plus tax Refund Policy