Neutralization epitopes on the antigenic domain II of the Orientia tsutsugamushi 56-kDa protein revealed by monoclonal antibodies

Seung-Yong Seong, M. K. Kim, S. M. Lee, Z. Odgerel, Myungsik Choi, T. H. Han, I. S. Kim, J. S. Kang, B. U. Lim

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Monoclonal antibodies (MoAbs) reactive with the authentic Orientia tsutsugamushi 56-kDa protein were generated. MoAb FS10 and FS15 showed in vitro, as well as, in vivo neutralizing activity upon O. tsutsugamushi infection. Deletion mutants of the gene for 56-kDa protein of O. tsutsugamushi Boryong were expressed to map the binding region. FS10 and FS15 are bound to amino acids (aa) located in an antigenic domain II, at residues 140-160 and 187-214, respectively. Computer modeling indicated that aa 146-153 were important for antigenicity against FS10. A sequence for aa 142-150 was highly homologous between oriential strains. These results suggest that the antigenic determinant for neutralizing MoAbs is an epitope within aa 140-160. Furthermore, this region may be important for the adhesion/invasion or intracellular survival of O. tsutsugamushi within host cells. (C) 2000 Elsevier Science Ltd.

Original languageEnglish
Pages (from-to)2-9
Number of pages8
JournalVaccine
Volume19
Issue number1
DOIs
StatePublished - 15 Aug 2000

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Orientia tsutsugamushi
neutralization
epitopes
Epitopes
monoclonal antibodies
Monoclonal Antibodies
Amino Acids
amino acids
Proteins
proteins
Gene Deletion
Neutralizing Antibodies
neutralizing antibodies
adhesion
Amino Acid Sequence
amino acid sequences
mutants
Infection
infection
genes

Keywords

  • 56-kDa protein
  • Neutralization
  • Orientia tsutsugamushi

Cite this

Seong, Seung-Yong ; Kim, M. K. ; Lee, S. M. ; Odgerel, Z. ; Choi, Myungsik ; Han, T. H. ; Kim, I. S. ; Kang, J. S. ; Lim, B. U. / Neutralization epitopes on the antigenic domain II of the Orientia tsutsugamushi 56-kDa protein revealed by monoclonal antibodies. In: Vaccine. 2000 ; Vol. 19, No. 1. pp. 2-9.
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Neutralization epitopes on the antigenic domain II of the Orientia tsutsugamushi 56-kDa protein revealed by monoclonal antibodies. / Seong, Seung-Yong; Kim, M. K.; Lee, S. M.; Odgerel, Z.; Choi, Myungsik; Han, T. H.; Kim, I. S.; Kang, J. S.; Lim, B. U.

In: Vaccine, Vol. 19, No. 1, 15.08.2000, p. 2-9.

Research output: Contribution to journalArticle

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T1 - Neutralization epitopes on the antigenic domain II of the Orientia tsutsugamushi 56-kDa protein revealed by monoclonal antibodies

AU - Seong, Seung-Yong

AU - Kim, M. K.

AU - Lee, S. M.

AU - Odgerel, Z.

AU - Choi, Myungsik

AU - Han, T. H.

AU - Kim, I. S.

AU - Kang, J. S.

AU - Lim, B. U.

PY - 2000/8/15

Y1 - 2000/8/15

N2 - Monoclonal antibodies (MoAbs) reactive with the authentic Orientia tsutsugamushi 56-kDa protein were generated. MoAb FS10 and FS15 showed in vitro, as well as, in vivo neutralizing activity upon O. tsutsugamushi infection. Deletion mutants of the gene for 56-kDa protein of O. tsutsugamushi Boryong were expressed to map the binding region. FS10 and FS15 are bound to amino acids (aa) located in an antigenic domain II, at residues 140-160 and 187-214, respectively. Computer modeling indicated that aa 146-153 were important for antigenicity against FS10. A sequence for aa 142-150 was highly homologous between oriential strains. These results suggest that the antigenic determinant for neutralizing MoAbs is an epitope within aa 140-160. Furthermore, this region may be important for the adhesion/invasion or intracellular survival of O. tsutsugamushi within host cells. (C) 2000 Elsevier Science Ltd.

AB - Monoclonal antibodies (MoAbs) reactive with the authentic Orientia tsutsugamushi 56-kDa protein were generated. MoAb FS10 and FS15 showed in vitro, as well as, in vivo neutralizing activity upon O. tsutsugamushi infection. Deletion mutants of the gene for 56-kDa protein of O. tsutsugamushi Boryong were expressed to map the binding region. FS10 and FS15 are bound to amino acids (aa) located in an antigenic domain II, at residues 140-160 and 187-214, respectively. Computer modeling indicated that aa 146-153 were important for antigenicity against FS10. A sequence for aa 142-150 was highly homologous between oriential strains. These results suggest that the antigenic determinant for neutralizing MoAbs is an epitope within aa 140-160. Furthermore, this region may be important for the adhesion/invasion or intracellular survival of O. tsutsugamushi within host cells. (C) 2000 Elsevier Science Ltd.

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