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Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
Published on: November 16, 2016
Inhibition of Orientia tsutsugamushi infection by a truncated recombinant 56-kDa outer membrane protein
1Division of Zoonoses, Center for Immunology and Pathology, National Institute of Health, Seoul, Korea.
Aims:
The objective of this study was to evaluate recombinant 56-kDa outer membrane protein as a potential inhibitor to infection from Orientia tsutsugamushi.
Methods And Results:
The 56-kDa protein was cloned and expressed in an Escherichia coli system, and the degree of target cell attachment to immobilized 56-kDa protein was measured in a cell adhesion assay. The results showed that the 56-kDa protein has an ability to attach HeLa cells. Furthermore, treatment of target cells with a truncated 56-kDa 1-418 (amino acid residues) protein inhibited target cell infection by O. tsutsugamushi, demonstrated with an indirect immunofluorescence antibody assay.
Conclusions:
The truncated 56-kDa protein (a.a. 1-418) plays an important role in O. tsutsugamushi infection, and the 56-kDa protein could be useful and effective in the inhibition of O. tsutsugamushi attachment and infection.
Significance And Impact Of The Study:
The attachment of the 56-kDa protein to target cells was directly determined by in vitro adherence test, and the invasion of target cells by O. tsutsugamushi was inhibited by treating the target cells with a truncated 56-kDa protein.
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