Induction of neutralizing antibody in mice by immunization with recombinant 56 kDa protein of Orientia tsutsugamushi

Seong, Seung Yong; Kim, H.R.; Huh, Myung Soo; Park, S.G.; Kang, Jae-Seung; Han, Tae Hee; Choi, Myung Sik; Chang, William; Kim, I.S.

doi:10.1016/s0264-410x(97)00112-6

Cited by 40 publications

(31 citation statements)

References 18 publications

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“…However, 19/21 (90.4%) serum samples of patients reacted with the TSA56 protein in the titer of 1:100, but the positive antibody responses to the TSA47 and TSA22 proteins was 13/21 (61.9%) and 10/21 (47.6%), respectively (data not shown). These data indicate that the TSA56 protein has a strong antibody response in scrub typhus patients in Taiwan in spite of the dilution factors of the patients' sera, which is consistent with other reports (26,(38)(39)(40)(41).…”

Section: Discussionsupporting

confidence: 91%

Molecular characterization of three major outer membrane proteins, TSA56, TSA47 and TSA22, in Orientia tsutsugamushi

et al. 2012

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Abstract. Orientia tsutsugamushi (O. tsutsugamushi), the causative agent of scrub typhus, is an obligate intracellular pathogen. Recent studies have demonstrated the complete genome of O. tsutsugamushi. However, the route and detailed molecular mechanism for O. tsutsugamushi to get accessed into mammalian cells remains unclear. In this study, we demonstrated different adhesive properties of three major outer membrane proteins of O. tsutsugamushi, TSA56, TSA47 and TSA22. TSA56 showed higher antibody responses against patient serum samples compared with those of TSA47 and TSA22. In the adhesion assay, TSA56 exhibited a relative higher adhesion to host cells than TSA47 and TSA22, suggesting that TSA56 is the major outer membrane protein required for O. tsutsugamushi adhesion. Furthermore, the antigen domain (AD) I (residues 19-114) corresponding to the extracellular domain of TSA56 demonstrated a relative high antibody response against the patients' sera than the previously reported ADIII (residues 237-366), which has been suggested to facilitate the invasion of O. tsutsugamushi through interaction with fibronectin. Taken together, our results consistently showed that TSA56 of O. tsutsugamushi is important in the adhesion of Escherichia coli (E. coli) transformants to Vero cells. Moreover, in contrast to known ADIII-fibronectin interactions, TSA56-ADI may also play a role in the adhesion and/or invasion of O. tsutsugamushi to its host cells through unidentified receptors. A further study aimed at delineating the receptor of TSA56-ADI during O. tsutsugamushi infection is warranted.

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Section: Discussionsupporting

confidence: 91%

Molecular characterization of three major outer membrane proteins, TSA56, TSA47 and TSA22, in Orientia tsutsugamushi

et al. 2012

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“…Among them, the type-specific antigen (TSA), a 56 kDa protein, has long been tested as a vaccine candidate since it is highly immunogenic and plays an important role in O . tsutsugamushi attachment to and invasion into host cells [38,49,50]. Thus far, TSA56 has been the best antigen to provide protective immunity in mouse infection models, but only to homologous strain infection due to its antigenic diversity [23].…”

Section: Discussionmentioning

confidence: 99%

Immunization with an Autotransporter Protein of Orientia tsutsugamushi Provides Protective Immunity against Scrub Typhus

Sharma

Kim

et al. 2015

PLoS Negl Trop Dis

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BackgroundScrub typhus is an acute febrile disease caused by Orientia tsutsugamushi infection. Recently, the rapid increase of scrub typhus incidence in several countries within the endemic region has become a serious public health issue. Despite the wide range of preventative approaches that have been attempted in the past 70 years, all have failed to develop an effective prophylactic vaccine. Currently, the selection of the proper antigens is one of the critical barriers to generating cross-protective immunity against antigenically-variable strains of O. tsutsugamushi.Methodology/Principal FindingsWe examined the potential role of ScaA protein, an autotransporter protein of O. tsutsugamushi, in bacterial pathogenesis and evaluated the protective attributes of ScaA immunization in lethal O. tsutsugamushi infection in mice. Our findings demonstrate that ScaA functions as a bacterial adhesion factor, and anti-ScaA antibody significantly neutralizes bacterial infection of host cells. In addition, immunization with ScaA not only provides protective immunity against lethal challenges with the homologous strain, but also confers significant protection against heterologous strains when combined with TSA56, a major outer membrane protein of O. tsutsugamushi.Conclusions/SignificanceImmunization of ScaA proteins provides protective immunity in mice when challenged with the homologous strain and significantly enhanced protective immunity against infection with heterologous strains. To our knowledge, this is the most promising result of scrub typhus vaccination trials against infection of heterologous strains in mouse models thus far.

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“…It is known that sera from most patients with scrub typhus recognize this protein, and mice immunized with the 56-kDa protein could generate neutralizing antibodies and showed in-creased resistance to homologous O. tsutsugamushi infection (more than 160 times the 50% minimal lethal dose). These data suggest that it is a suitable diagnostic antigen and vaccine candidate (15,16). …”

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confidence: 91%

Recombinant 56-Kilodalton Major Outer Membrane Protein Antigen of Orientia tsutsugamushi Shanxi and Its Antigenicity

et al. 2003

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Induction of neutralizing antibody in mice by immunization with recombinant 56 kDa protein of Orientia tsutsugamushi

Cited by 40 publications

References 18 publications

Molecular characterization of three major outer membrane proteins, TSA56, TSA47 and TSA22, in Orientia tsutsugamushi

Molecular characterization of three major outer membrane proteins, TSA56, TSA47 and TSA22, in Orientia tsutsugamushi

Immunization with an Autotransporter Protein of Orientia tsutsugamushi Provides Protective Immunity against Scrub Typhus

Recombinant 56-Kilodalton Major Outer Membrane Protein Antigen of Orientia tsutsugamushi Shanxi and Its Antigenicity

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