Format

Send to

Choose Destination
See comment in PubMed Commons below
J Bacteriol. 2011 Nov;193(22):6379-83. doi: 10.1128/JB.05849-11. Epub 2011 Sep 9.

Determination of Borrelia surface lipoprotein anchor topology by surface proteolysis.

Author information

  • 1Department 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.

PMID:
21908659
PMCID:
PMC3209212
DOI:
10.1128/JB.05849-11
[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Support Center