Functional pentameric formation via coexpression of the Escher coli heat-labile enterotoxin B subunit and its fusion protein subunit with a neutralizing epitope of ApxIIA exotoxin improves the mucosal immugenicity = 기능적 오합체 형성에 의한 면역력 강화

Cited 9 time in scopus
Metadata Downloads
Title
Functional pentameric formation via coexpression of the Escher coli heat-labile enterotoxin B subunit and its fusion protein subunit with a neutralizing epitope of ApxIIA exotoxin improves the mucosal immugenicity = 기능적 오합체 형성에 의한 면역력 강화
Author(s)
J M Kim; S M Park; J A Kim; J A Park; M H Yi; N S Kim; J L Bae; Sung Goo Park; Y S Jang; M S Yang; D H Kim
Bibliographic Citation
Clinical and Vaccine Immunology, vol. 18, no. 12, pp. 2168-2177
Publication Year
2011
Abstract
A coexpression strategy in Saccharomyces cerevisiae using episomal and integrative vectors for the Escherichia coli heat-labile enterotoxin B subunit (LTB) and a fusion protein of an ApxIIA toxin epitope produced by Actinobacillus pleuropneumoniae coupled to LTB, respectively, was adapted for the hetero-oligomerization of LTB and the LTB fusion construct. Enzyme-linked immunosorbent assay (ELISA) with GM1 ganglioside indicated that the LTB fusion construct, along with LTB, was oligomerized to make the functional heteropentameric form, which can bind to receptors on the mucosal epithelium. The antigen-specific antibody titer of mice orally administered antigen was increased when using recombinant yeast coexpressing the pentameric form instead of recombinant yeast expressing either the LTB fusion form or antigen alone. Better protection against challenge infection with A. pleuropneumoniae was also observed for coexpression in recombinant yeast compared with others. The present study clearly indicated that the coexpression strategy enabled the LTB fusion construct to participate in the pentameric formation, resulting in an improved induction of systemic and mucosal immune responses.
ISSN
1556-6811
Publisher
Amer Soc Microbiology
DOI
http://dx.doi.org/10.1128/CVI.05230-11
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.