Surface expression,single-channel analysis and membrane topology of recombinant <Emphasis Type="Italic">Chlamydia trachomatis</Emphasis> Major Outer Membrane Protein |
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Authors: | Heather?E?Findlay Heather?McClafferty Email author" target="_blank">Richard?H?AshleyEmail author |
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Institution: | (1) Division of Biomedical Sciences, University of Edinburgh Medical School, George Square, EH8 9XD Edinburgh, UK;(2) Department of Biochemistry, School of Medical Sciences, University of Bristol, BS8 1TD Bristol, UK |
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Abstract: | Background Chlamydial bacteria are obligate intracellular pathogens containing a cysteine-rich porin (Major Outer Membrane Protein, MOMP)
with important structural and, in many species, immunity-related roles. MOMP forms extensive disulphide bonds with other chlamydial
proteins, and is difficult to purify. Leaderless, recombinant MOMPs expressed in E. coli have yet to be refolded from inclusion bodies, and although leadered MOMP can be expressed in E. coli cells, it often misfolds and aggregates. We aimed to improve the surface expression of correctly folded MOMP to investigate
the membrane topology of the protein, and provide a system to display native and modified MOMP epitopes. |
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