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J. Biol. Chem., Vol. 276, Issue 1, 457-463, January 5, 2001
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From the Vsp surface lipoproteins are serotype-defining
antigens of relapsing fever spirochetes that undergo multiphasic
antigenic variation to avoid the immune response. One of these
proteins, VspA of Borrelia turicatae, is also associated
with neurotropism in infected mice. Vsp proteins are highly polymorphic
in sequence, which may relate to their specific antibody reactivities
and host cell interactions. To determine whether sequence variations
affect protein structure, we compared B. turicatae VspA
with three related proteins: VspB of B. turicatae, Vsp26 of
the relapsing fever agent Borrelia hermsii, and OspC of the
Lyme disease spirochete Borrelia burgdorferi. Recombinant
non-lipidated proteins were purified by affinity or ion exchange
chromatography. Circular dichroism spectra revealed similar, highly
Structural Conservation of Neurotropism-associated VspA within
the Variable Borrelia Vsp-OspC Lipoprotein Family*
§,,§
Departments of Microbiology & Molecular
Genetics and Medicine, University of California at Irvine, College of
Medicine, Irvine, California 92697 and the ¶ Department of
Chemistry, Rutgers, The State University of New Jersey,
Piscataway, New Jersey 08854
-helical secondary structures for all four proteins. In
vitro assays demonstrated protease-resistant, thermostable Vsp
cores starting at a conserved serine at position 34 (Ser34). All proteins aggregate as dimers in solution.
In situ trypsin treatment and surface protein cross-linking
showed that the native lipoproteins also form protease-resistant
dimers. These findings indicate that Vsp proteins have a common compact
fold and that their established functions are based on localized
polymorphisms. Two forms of VspA crystals suitable for structure
determination by x-ray diffraction methods have been obtained.
*
This work was supported by the National Institutes of Health
Grant AI24424 (to A. G. B).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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