期刊
JOURNAL OF BACTERIOLOGY
卷 193, 期 22, 页码 6379-6383出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.05849-11
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资金
- National Institutes of Health [R01 AI063261]
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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