A multi-epitope chimeric protein elicited a strong antibody response and partial protection against Edwardsiella ictaluri in Nile tilapia
Edwardsiella ictaluri infects several fish species and protection of the all the susceptible fish hosts from the pathogen using a monovalent vaccine is impossible because the species is composed of host-based genotypes that are genetic, serological and antigenic heterogenous. Here, immunoinformatic...
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th-mahidol.731692022-08-04T11:56:42Z A multi-epitope chimeric protein elicited a strong antibody response and partial protection against Edwardsiella ictaluri in Nile tilapia Vimbai Irene Machimbirike Natapol Pornputtapong Saengchan Senapin Eakapol Wangkahart Prapansak Srisapoome Pongsak Khunrae Triwit Rattanarojpong Chulalongkorn University Kasetsart University Mahidol University Thailand National Center for Genetic Engineering and Biotechnology King Mongkut's University of Technology Thonburi Mahasarakham University Agricultural and Biological Sciences Veterinary Edwardsiella ictaluri infects several fish species and protection of the all the susceptible fish hosts from the pathogen using a monovalent vaccine is impossible because the species is composed of host-based genotypes that are genetic, serological and antigenic heterogenous. Here, immunoinformatic approach was employed to design a cross-immunogenic chimeric EiCh protein containing multi-epitopes. The chimeric EiCh protein is composed of 11 B-cell epitopes and 7 major histocompatibility complex class II epitopes identified from E. ictaluri immunogenic proteins previously reported. The 49.32 kDa recombinant EiCh protein was expressed in vitro in Escherichia coli BL-21 (DE3) after which inclusion bodies were successfully solubilized and refolded. Ab initio protein modelling revealed secondary and tertiary structures. Secondary structure was confirmed by circular dichroism spectroscopy. Antigenicity of the chimeric EiCh protein was exhibited by strong reactivity with serum from striped catfish and Nile tilapia experimentally infected with E. ictaluri. Furthermore, immunogenicity of the chimeric EiCh protein was investigated in vivo in Nile tilapia juveniles and it was found that the protein could strongly induce production of specific antibodies conferring agglutination activity and partially protected Nile tilapia juveniles with a relative survival percentage (RPS) of 42%. This study explored immunoinformatics as reverse vaccinology approach in vaccine design for aquaculture to manage E. ictaluri infections. 2022-08-04T03:37:45Z 2022-08-04T03:37:45Z 2022-01-01 Article Journal of Fish Diseases. Vol.45, No.1 (2022), 1-18 10.1111/jfd.13525 13652761 01407775 2-s2.0-85114049322 https://repository.li.mahidol.ac.th/handle/123456789/73169 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85114049322&origin=inward |
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Agricultural and Biological Sciences Veterinary Vimbai Irene Machimbirike Natapol Pornputtapong Saengchan Senapin Eakapol Wangkahart Prapansak Srisapoome Pongsak Khunrae Triwit Rattanarojpong A multi-epitope chimeric protein elicited a strong antibody response and partial protection against Edwardsiella ictaluri in Nile tilapia |
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Edwardsiella ictaluri infects several fish species and protection of the all the susceptible fish hosts from the pathogen using a monovalent vaccine is impossible because the species is composed of host-based genotypes that are genetic, serological and antigenic heterogenous. Here, immunoinformatic approach was employed to design a cross-immunogenic chimeric EiCh protein containing multi-epitopes. The chimeric EiCh protein is composed of 11 B-cell epitopes and 7 major histocompatibility complex class II epitopes identified from E. ictaluri immunogenic proteins previously reported. The 49.32 kDa recombinant EiCh protein was expressed in vitro in Escherichia coli BL-21 (DE3) after which inclusion bodies were successfully solubilized and refolded. Ab initio protein modelling revealed secondary and tertiary structures. Secondary structure was confirmed by circular dichroism spectroscopy. Antigenicity of the chimeric EiCh protein was exhibited by strong reactivity with serum from striped catfish and Nile tilapia experimentally infected with E. ictaluri. Furthermore, immunogenicity of the chimeric EiCh protein was investigated in vivo in Nile tilapia juveniles and it was found that the protein could strongly induce production of specific antibodies conferring agglutination activity and partially protected Nile tilapia juveniles with a relative survival percentage (RPS) of 42%. This study explored immunoinformatics as reverse vaccinology approach in vaccine design for aquaculture to manage E. ictaluri infections. |
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Chulalongkorn University |
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Chulalongkorn University Vimbai Irene Machimbirike Natapol Pornputtapong Saengchan Senapin Eakapol Wangkahart Prapansak Srisapoome Pongsak Khunrae Triwit Rattanarojpong |
format |
Article |
author |
Vimbai Irene Machimbirike Natapol Pornputtapong Saengchan Senapin Eakapol Wangkahart Prapansak Srisapoome Pongsak Khunrae Triwit Rattanarojpong |
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Vimbai Irene Machimbirike |
title |
A multi-epitope chimeric protein elicited a strong antibody response and partial protection against Edwardsiella ictaluri in Nile tilapia |
title_short |
A multi-epitope chimeric protein elicited a strong antibody response and partial protection against Edwardsiella ictaluri in Nile tilapia |
title_full |
A multi-epitope chimeric protein elicited a strong antibody response and partial protection against Edwardsiella ictaluri in Nile tilapia |
title_fullStr |
A multi-epitope chimeric protein elicited a strong antibody response and partial protection against Edwardsiella ictaluri in Nile tilapia |
title_full_unstemmed |
A multi-epitope chimeric protein elicited a strong antibody response and partial protection against Edwardsiella ictaluri in Nile tilapia |
title_sort |
multi-epitope chimeric protein elicited a strong antibody response and partial protection against edwardsiella ictaluri in nile tilapia |
publishDate |
2022 |
url |
https://repository.li.mahidol.ac.th/handle/123456789/73169 |
_version_ |
1763490983246299136 |