Nasal immunogenicity induced by STxB and STxB-IpaD antigens in laboratory rats

Author(s):
Mahdi BaranvandMahdi Baranvand, Hossein HonariHossein HonariHossein Honari ORCID,*
*Corresponding Author: Email: [email protected]

Koomesh:Vol. 16, issue 3; 397-403
Published online:Sep 28, 2015
Article type:Research Article
Received:May 02, 2014
Accepted:Dec 03, 2014
How to Cite:Baranvand M, Honari H. Nasal immunogenicity induced by STxB and STxB-IpaD antigens in laboratory rats. koomesh. 2015;16(3):e151264. doi:

Abstract

  Introduction: Shigella and E. coli bacteria are the most common cause of Diarrhea, though as yet no effective vaccine against them has been produced. IpaD protein plays an important role in invasion and infection caused by Shigella. Another major virulence factor in Shigella dysenteriae type 1 and E. coli O157: H7 is Shigella enterotoxin or (STxB). IpaD protein in combination with STxB can produce a suitable candidate vaccine. In this study, the nasal STxB and STxB-IpaD fused recombinant proteins antibody titers and their immunogenicity were assessed and compared in rats .   Materials and Methods: (pET28- stxB) and (pET28-ipaD-stxB) vectors were prepared at Biology center of the Imam Hussein University (AS). Transformation of these plasmids into E. coli BL21 DE3 bacteria were confirmed by PCR and enzymatic digestion. Production of recombinant proteins were confirmed by SDS-PAGE and Western blotting. Expression of fused STxB-IpaD and STxB antigens were performed under induction of IPTG. After protein purifications, using affinity chromatography, antigens were prescribed nasally to five groups of rats in four consecutive sessions. Later the polyclonal antibodies produced in rat sera were measured .   Results : ELISA showed that antibody titers were increased by the combination of IpaD to STxB compared to that produced against single STxB antigen. The immunized Rats with StxB antigen were able to tolerate up to six fold of LD50, while rats that were immunized with STxB-IpaD combined antigens were able tolerate up to tenfold of LD50 for E. coli O157: H7 Shiga toxin .   Conclusion: The protein produced from the fusion of ipaD and stxB genes, can increase the effect of single STxB antigen immunogenicity. Recombinant proteins fused with STxB protein without chemicals adjuvants can be recommended in the form of nasal drops as possible candidates for vaccines against E. coli and Shigella types .  

Copyright

© 2015, Author(s). This open-access article is available under the Creative Commons Attribution 4.0 (CC BY 4.0) International License (https://creativecommons.org/licenses/by/4.0/), which allows for unrestricted use, distribution, and reproduction in any medium, provided that the original work is properly cited.

Similar Articles

12
Apr
2012

Immunogenical Study of Chimeric Recombinant Intimin-Tir of Escherichia coli O157:H7 in Mice

Alavieh Yazdanparast,
Seyed Latif Mousavi,
Iraj Rasooli,
Jafar Amani,
Mohammadreza Jalalinadoushan

Yazdanparast A, Mousavi SL, Rasooli I, Amani J, Jalalinadoushan M. Immunogenical Study of Chimeric Recombinant Intimin-Tir of Escherichia coli O157:H7 in Mice. Arch Clin Infect Dis. 2012;7(2):14068. doi: https://doi.org/10.5812/archcid.14068

18
Apr
2015

Prokaryotic High-Level Expression System in Producing Adhesin Recombinant Protein E of Nontypeable Haemophilus influenzae

Minoo Tavakoli,
Saeed Bouzari,
Seyed Davar Siadat,
Shahin Najar Peerayeh,
Anis Jafari

Tavakoli M, Bouzari S, Siadat SD, Najar Peerayeh S, Jafari A. Prokaryotic High-Level Expression System in Producing Adhesin Recombinant Protein E of Nontypeable Haemophilus influenzae. Jundishapur J Microbiol. 2015;8(4):e16377. doi: https://doi.org/10.5812/jjm.8(4)2015.16377

29
Aug
2015

Molecular Cloning, Expression and Purification of Truncated hpd Fragment of Haemophilus influenzae in Escherichia coli

Ava Behrouzi,
Saeid Bouzari,
Seyed Davar Siadat,
Anis Jafari,
Shiva Irani

Behrouzi A, Bouzari S, Siadat SD, Jafari A, Irani S. Molecular Cloning, Expression and Purification of Truncated hpd Fragment of Haemophilus influenzae in Escherichia coli. Jundishapur J Microbiol. 2015;8(8):e23218. doi: https://doi.org/10.5812/jjm.23218

28
Sep
2015

Expression, extraction, purification and immunogenicity study of three recombinant proteins LTB, THc, BoNT / A and Comparison of produced antibody titer against them in laboratory animals

Hekmat Nekooei Fard,
Mojtaba Saadati,
Marzieh Ebrahimi,
gholamreza olad,
Farid Azizi Jalilian,
Jafar Salimian
,et al.

Nekooei Fard H, Saadati M, Ebrahimi M, olad G, Azizi Jalilian F, et al. Expression, extraction, purification and immunogenicity study of three recombinant proteins LTB, THc, BoNT / A and Comparison of produced antibody titer against them in laboratory animals. koomesh. 2015;16(2):e151305. doi:

15
Feb
2000

Expression of ente rotoxigenic Escherichia coli heat-labile toxin B subunit ge ne in Salmonella typhimurium G30: immunization using an oral live delivery system

MohammadReza AkbaryEiedgahi,
Bahman Torabi,
Veladimir Richinski

AkbaryEiedgahi M, Torabi B, Richinski V. Expression of ente rotoxigenic Escherichia coli heat-labile toxin B subunit ge ne in Salmonella typhimurium G30: immunization using an oral live delivery system. koomesh. 2000;1(2):e151894. doi:

Download PDF463.51 KB
Share on
Cited by
Metrics

Ordering Reprints

Articles are published under the Creative Commons license stated on each article. No permission or royalty fee is required for uses permitted by that license. CCC handles optional bulk and customized reprint orders. Any quotation covers production and delivery services only, not copyright permission. > Request Reprints from CCC