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.
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. tsutsugamushiinfection, 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.
Authors: Pasquale Mansueto; Giustina Vitale; Antonio Cascio; Aurelio Seidita; Ilenia Pepe; Antonio Carroccio; Salvatore di Rosa; Giovam Battista Rini; Enrico Cillari; David H Walker Journal: Clin Dev Immunol Date: 2011-09-06
Authors: Sangho Choi; Hang Jin Jeong; Kyu-Jam Hwang; Byoungchul Gill; Young Ran Ju; Yeong Seon Lee; Jeongmin Lee Journal: Am J Trop Med Hyg Date: 2017-07 Impact factor: 2.345