Open AccessDetermination of Borrelia Surface Lipoprotein Anchor Topology by Surface Proteolysis
Author(s) -
Shiyong Chen,
Ozan S. Kumru,
Wolfram R. Zückert
Publication year - 2011
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.05849-11
Subject(s) - biology , proteolysis , borrelia , microbiology and biotechnology , lipoprotein , surface protein , computational biology , biochemistry , genetics , borrelia burgdorferi , virology , cholesterol , antibody , enzyme
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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