title: Determination of Borrelia surface lipoprotein anchor topology by surface proteolysis.
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.
authors: Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Mail Stop 3029, 3901 Rainbow Boulevard, Kansas City, KS 66160, USA.
authors: Shiyong
authors: S
authors: Chen
authors: Ozan S
authors: OS
authors: Kumru
authors: Wolfram R
authors: WR
authors: Zückert
mesh_terms: D000954:Antigens, Surface / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001428:Bacterial Vaccines / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D025065:Borrelia burgdorferi / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008074:Lipoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008193:Lyme Disease / Q000382:microbiology; D011485:Protein Binding; D059748:Proteolysis
chemical_list: D000954:Antigens, Surface; D001425:Bacterial Outer Membrane Proteins; D001428:Bacterial Vaccines; D008074:Lipoproteins; C072045:OspA protein