Inhibition of Orientia tsutsugamushi infection by a truncated recombinant 56-kDa outer membrane protein

The objective of this study was to evaluate recombinant 56-kDa outer membrane protein as a potential inhibitor to infection from Orientia tsutsugamushi. 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 w...

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Bibliographic Details
Published in:Letters in applied microbiology 2010-05, Vol.50 (5), p.445-451
Main Authors: Park, S, Hwang, K.J, Chu, H, Park, S.H, Shim, S.K, Choi, Y.S, Kim, J.S, Park, M.Y
Format: Article
Language:English
Subjects:
Animals
Bacterial Outer Membrane Proteins - genetics
Bacterial Outer Membrane Proteins - metabolism
Biological and medical sciences
Cell Adhesion
Down-Regulation
Escherichia coli
Fundamental and applied biological sciences. Psychology
HeLa Cells
Humans
Mice
Microbiology
Orientia tsutsugamushi
Orientia tsutsugamushi - genetics
Orientia tsutsugamushi - physiology
Orientia tsutsugamushi infection
outer membrane protein
Protein Binding
recombinant 56-kDa protein
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Scrub Typhus - microbiology
Scrub Typhus - physiopathology
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Summary:The objective of this study was to evaluate recombinant 56-kDa outer membrane protein as a potential inhibitor to infection from Orientia tsutsugamushi. 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. 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. 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.
ISSN:0266-8254
1472-765X
DOI:10.1111/j.1472-765X.2010.02814.x