Crystal structure of Lyme disease variable surface antigen VlsE of Borrelia burgdorferi.
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.
Eicken
Christoph
C
Center for Structural Biology, Texas A&M University, College Station, Texas 77843-2128, USA.
Sharma
Vivek
V
Klabunde
Thomas
T
Lawrenz
Matthew B
MB
Hardham
John M
JM
Norris
Steven J
SJ
Sacchettini
James C
JC
D000595:Amino Acid Sequence; D000818:Animals; D000942:Antigens, Bacterial / Q000737:chemistry*; D000954:Antigens, Surface / Q000737:chemistry*; D001426:Bacterial Proteins; D025065:Borrelia burgdorferi / Q000378:metabolism*; D018360:Crystallography, X-Ray; D008074:Lipoproteins / Q000737:chemistry*; D008193:Lyme Disease / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D000942:Antigens, Bacterial; D000954:Antigens, Surface; D001426:Bacterial Proteins; D008074:Lipoproteins; D011994:Recombinant Proteins; C105546:VlsE protein, Borrelia burgdorferi