Open AccessCrystallization and preliminary crystallographic analysis of BbCRASP‐1, a complement regulator‐acquiring surface protein of Borrelia burgdorferi
Author(s) -
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.
Publication year - 2004
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s090744490400472x
Subject(s) - borrelia burgdorferi , borrelia , regulator , microbiology and biotechnology , pathogen , lyme disease , complement (music) , selenium , substructure , crystallization , complement system , immune system , factor h , biology , antibody , chemistry , virology , immunology , biochemistry , mutant , organic chemistry , structural engineering , complementation , gene , engineering
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.