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Determination of Borrelia surface lipoprotein anchor topology by surface proteolysis
Authors:Chen Shiyong  Kumru Ozan S  Zückert Wolfram R
Affiliation:Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Mail Stop 3029, 3901 Rainbow Boulevard, Kansas City, KS 66160, USA.
Abstract:We used a surface trypsinolysis assay to probe accessibility of the membrane-proximal N-terminal tether peptides of Borrelia surface lipoproteins OspA and Vsp1. Our findings with both wild-type and mutant proteins are only compatible with the anchoring of these surface lipoproteins in the outer leaflet of the outer spirochetal membrane.
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