Crystal Structure of Lyme Disease Variable Surface Antigen VlsE of Borrelia burgdorferi | Academic Article individual record
abstract

VlsE is an outer surface lipoprotein of Borrelia burgdorferi that undergoes antigenic variation through an elaborate gene conversion mechanism and is thought to play a major role in the immune response to the Lyme disease borellia. The crystal structure of recombinant variant protein VlsE1 at 2.3-A resolution reveals that the six variable regions form loop structures that constitute most of the membrane distal surface of VlsE, covering the predominantly alpha-helical, invariant regions of the protein. The surface localization of the variable amino acid segments appears to protect the conserved regions from interaction with antibodies and hence may contribute to immune evasion.

author list (cited authors)
Eicken, C., Sharma, V., Klabunde, T., Lawrenz, M. B., Hardham, J. M., Norris, S. J., & Sacchettini, J. C.
publication date
2002
keywords
  • Molecular Sequence Data
  • Bacterial Proteins
  • Sequence Homology, Amino Acid
  • Crystallography, X-Ray
  • Lipoproteins
  • Amino Acid Sequence
  • Protein Structure, Secondary
  • Models, Molecular
  • Antigens, Bacterial
  • Protein Structure, Tertiary
  • Borrelia Burgdorferi
  • Recombinant Proteins
  • Antigens, Surface
  • Animals
  • Lyme Disease
altmetric score

3.0

citation count

97