Determination of Borrelia Surface lipoprotein anchor topology by surface proteolysis

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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. © 2011, American Society for Microbiology.

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APA

Chen, S., Kumru, O. S., & Zückert, W. R. (2011, November). Determination of Borrelia Surface lipoprotein anchor topology by surface proteolysis. Journal of Bacteriology. https://doi.org/10.1128/JB.05849-11

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