Journal article
Molecular cloning of Treponema pallidum outer envelope fibronectin binding proteins, P1 and P2
Genitourinary medicine, Vol.63(6), pp.355-360
12/1987
Handle:
https://hdl.handle.net/2376/108931
PMCID: PMC1194115
PMID: 2962928
Abstract
Phages directing the synthesis of Treponema pallidum fibronectin binding adhesin proteins, P1 and P2, were isolated from an EMBL-3 bacteriophage lambda library of T pallidum deoxyribonucleic acid (DNA). The recombinant phages were identified using antisera generated to treponemal proteins purified in fibronectin-Sepharose. Recombinant P1 and P2 proteins possessed the same relative molecular weights as the native surface polypeptides of spirochaetes. The structural genes for these proteins were subcloned into the plasmid vector pUC19, and transformed Escherichia coli expressed and translocated recombinant P1 and P2 to their outer membranes. Finally, the recombinant adhesin proteins, P1 and P2, were purified from detergent solubilised E coli outer membrane preparations using fibronectin-Sepharose affinity chromatography, which confirmed that the fibronectin binding properties of the cloned proteins were retained.
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Details
- Title
- Molecular cloning of Treponema pallidum outer envelope fibronectin binding proteins, P1 and P2
- Creators
- K Peterson - Department of Microbiology, University of Texas Health Science Center, San Antonio 78284J B Baseman - Department of Microbiology, University of Texas Health Science Center, San Antonio 78284J F Alderete - Department of Microbiology, University of Texas Health Science Center, San Antonio 78284
- Publication Details
- Genitourinary medicine, Vol.63(6), pp.355-360
- Academic Unit
- Molecular Biosciences, School of
- Identifiers
- 99900547496401842
- Language
- English
- Resource Type
- Journal article