期刊
TOXINS
卷 14, 期 2, 页码 -出版社
MDPI
DOI: 10.3390/toxins14020135
关键词
botulinum neurotoxin; functional fragment; L-HN fragment; subunit vaccine; immunoprotective effect
In this study, the EL-HN fragment of BoNT/E was found to have high protective efficacy and contain neutralizing epitopes. EL-HN plays an important role in immune protection against BoNT/E and has the potential to be the optimal immunogen for botulinum vaccines.
Clostridium botulinum produces botulinum neurotoxin (BoNT), which is the most toxic known protein and the causative agent of human botulism. BoNTs have similar structures and functions, comprising three functional domains: catalytic domain (L), translocation domain (HN), and receptor-binding domain (Hc). In the present study, BoNT/E was selected as a model toxin to further explore the immunological significance of each domain. The EL-HN fragment (L and HN domains of BoNT/E) retained the enzymatic activity without in vivo neurotoxicity. Extensive investigations showed EL-HN functional fragment had the highest protective efficacy and contained some functional neutralizing epitopes. Further experiments demonstrated the EL-HN provided a superior protective effect compared with the EHc or EHc and EL-HN combination. Thus, the EL-HN played an important role in immune protection against BoNT/E and could provide an excellent platform for the design of botulinum vaccines and neutralizing antibodies. The EL-HN has the potential to replace EHc or toxoid as the optimal immunogen for the botulinum vaccine.
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