Premium
Inhibition of Orientia tsutsugamushi infection by a truncated recombinant 56‐kDa outer membrane protein
Author(s) -
Park S.,
Hwang K.J.,
Chu H.,
Park S.H.,
Shim S.K.,
Choi Y.S.,
Kim J.S.,
Park M.Y.
Publication year - 2010
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.2010.02814.x
Subject(s) - orientia tsutsugamushi , recombinant dna , biology , microbiology and biotechnology , hela , bacterial outer membrane , antibody , escherichia coli , in vitro , scrub typhus , virology , biochemistry , immunology , gene
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.