Structural requirements for glycosaminoglycan recognition by the Lyme disease spirochete, Borrelia burgdorferi.
Borrelia burgdorferi, the Lyme disease agent, binds glycosaminoglycans (GAGs) such as heparin, heparan sulfate, and dermatan sulfate. Heparin or heparan sulfate fractions separated by size or charge were tested for their ability to inhibit attachment of B. burgdorferi to Vero cells. GAG chains of increasing length and/or charge showed increasing inhibitory potency, and detectable heparin inhibition of bacterial binding required a minimum of 16 residues. The ability of a given heparin fraction to inhibit binding to Vero cells was strongly predictive of its ability to inhibit hemagglutination, suggesting that hemagglutination reflects the capacity of B. burgdorferi to bind to GAGs.
Leong
J M
JM
Department of Molecular Genetics and Microbiology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655, USA. john.leong@banyan.ummed.edu
Robbins
D
D
Rosenfeld
L
L
Lahiri
B
B
Parveen
N
N
D000818:Animals; D001422:Bacterial Adhesion; D001667:Binding, Competitive; D025065:Borrelia burgdorferi; D015748:Borrelia burgdorferi Group / Q000378:metabolism*; D002522:Chlorocebus aethiops; D006025:Glycosaminoglycans / Q000378:metabolism*; D006386:Hemagglutination Tests; D006493:Heparin / Q000378:metabolism; D013329:Structure-Activity Relationship; D014709:Vero Cells
D006025:Glycosaminoglycans; D006493:Heparin