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Application of a liposomal subunit vaccine in chickens for reduction of Campylobacter gut colonisation

Anna Łasica

Anna Łasica

Department of Bacterial Genetics, Institute of MicrobiologyWarszawa, Poland
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Łasica, Anna
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Renata Godlewska

Renata Godlewska

Department of Bacterial Genetics, Institute of MicrobiologyWarszawa, Poland
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Godlewska, Renata
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Jerzy Gubernator

Jerzy Gubernator

Department of Lipids and Liposomes, Faculty of Biotechnology, University of WroclawWrocław, Poland
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Gubernator, Jerzy
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Anna Jakubiak-Augustyn

Anna Jakubiak-Augustyn

Department of Lipids and Liposomes, Faculty of Biotechnology, University of WroclawWrocław, Poland
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Jakubiak-Augustyn, Anna
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Paweł Majewski

Paweł Majewski

Department of Animal Physiology, Institute of Functional Biology and Ecology, University of WarsawWarszawa, Poland
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Majewski, Paweł
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Agnieszka Wyszyńska

Agnieszka Wyszyńska

Department of Bacterial Genetics, Institute of MicrobiologyWarszawa, Poland
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Wyszyńska, Agnieszka
  
06 lis 2024
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Data publikacji: 06 lis 2024
Zakres stron: 487 - 496
Otrzymano: 02 cze 2024
Przyjęty: 28 paź 2024
DOI: https://doi.org/10.2478/jvetres-2024-0062
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© 2024 Anna Łasica et al., published by Sciendo
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Fig. 1.

A. RaptorX structure modelling for rCjaAEF-Tu (IA) and for rCjaCD (IIA). Modelling of the CjaA (IA) and CjaC (IIA) proteins with their native signal sequence is included for comparison. Protein epitopes (Ep) are shown in green (CjaA and CjaC) and black (EF-Tu and CjaD). Dashed arrows indicate elements not visible on selected orientation of protein molecule. B. The amino acid sequence of the rCjaAEF-Tu (IB) and rCjaCD (IIB) hybrid proteins. Lowercase letters denote the signal sequence at the amino terminus of the protein and the fragment at the carboxyl terminus covering the histidine tag. Epitopes of the CjaA (IB) and CjaC (IIB) proteins are indicated by underlining, epitopes of the EF-Tu (IB) and CjaD (IIB) proteins are marked in red, and insertion sites are highlighted in green
A. RaptorX structure modelling for rCjaAEF-Tu (IA) and for rCjaCD (IIA). Modelling of the CjaA (IA) and CjaC (IIA) proteins with their native signal sequence is included for comparison. Protein epitopes (Ep) are shown in green (CjaA and CjaC) and black (EF-Tu and CjaD). Dashed arrows indicate elements not visible on selected orientation of protein molecule. B. The amino acid sequence of the rCjaAEF-Tu (IB) and rCjaCD (IIB) hybrid proteins. Lowercase letters denote the signal sequence at the amino terminus of the protein and the fragment at the carboxyl terminus covering the histidine tag. Epitopes of the CjaA (IB) and CjaC (IIB) proteins are indicated by underlining, epitopes of the EF-Tu (IB) and CjaD (IIB) proteins are marked in red, and insertion sites are highlighted in green

Fig. 2.

Immunoreactivity and immunogenicity of hybrid rCjaAEF-Tu and rCjaCD proteins analysed by Western blot. A – Immunoreactivity of rCjaAEF-Tu with specific single antigen sera. Lane 1 – marker; lane 2 – purified rCjaAEF-Tu protein; B – Immunoreactivity of rCjaCD with specific single-antigen sera. Lane 1 – marker; lane 2 – purified rCjaCD protein; C – Immunogenicity of rCjaAEF-Tu detected with rabbit serum raised against whole hybrid protein. Lane 1 – marker; lane 2 – protein lysate from whole C. jejuni cells; D – Immunogenicity of rCjaCD detected with rabbit serum raised against whole hybrid protein. Lane 1 – marker; lane 2 – protein lysate from whole C. jejuni cells
Immunoreactivity and immunogenicity of hybrid rCjaAEF-Tu and rCjaCD proteins analysed by Western blot. A – Immunoreactivity of rCjaAEF-Tu with specific single antigen sera. Lane 1 – marker; lane 2 – purified rCjaAEF-Tu protein; B – Immunoreactivity of rCjaCD with specific single-antigen sera. Lane 1 – marker; lane 2 – purified rCjaCD protein; C – Immunogenicity of rCjaAEF-Tu detected with rabbit serum raised against whole hybrid protein. Lane 1 – marker; lane 2 – protein lysate from whole C. jejuni cells; D – Immunogenicity of rCjaCD detected with rabbit serum raised against whole hybrid protein. Lane 1 – marker; lane 2 – protein lysate from whole C. jejuni cells

Fig. 3.

Colonisation of chickens vaccinated with neutral or anionic liposomes containing hybrid proteins, rCjaCD and rCjaAEF-Tu, and of unvaccinated chickens challenged with strain 12/2 of Campylobacter jejuni. Viable C. jejuni cells recovered from the caeca of chickens were assessed on the specified days after the challenge. No significant differences (P-value < 0.05) were observed between groups. PBS – phosphate-buffered saline
Colonisation of chickens vaccinated with neutral or anionic liposomes containing hybrid proteins, rCjaCD and rCjaAEF-Tu, and of unvaccinated chickens challenged with strain 12/2 of Campylobacter jejuni. Viable C. jejuni cells recovered from the caeca of chickens were assessed on the specified days after the challenge. No significant differences (P-value < 0.05) were observed between groups. PBS – phosphate-buffered saline
Język:
Angielski
Częstotliwość wydawania:
4 razy w roku
Dziedziny czasopisma:
Nauki biologiczne, Biologia molekularna, Mikrobiologia i wirusologia, Nauki biologiczne, inne, Medycyna, Weterynaria
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