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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

Authors 

J M KimS M ParkJ A KimJ A ParkM H YiN S KimJ L BaeSung Goo ParkY S JangM S YangD H Kim

Publisher 

American Society for Microbiology

Issue Date 

2011

Citation 

Clinical and Vaccine Immunology, vol. 18, no. 12, pp. 2168-2177

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

Link 

http://dx.doi.org/10.1128/CVI.05230-11

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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