Examination of immunogenic properties of recombinant antigens based on p22 protein from African swine fever virus

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00027162%3A_____%2F22%3AN0000110" target="_blank" >RIV/00027162:_____/22:N0000110 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15310/22:73616789 RIV/62157124:16170/22:43880224 RIV/61989592:15640/22:73616789

Výsledek na webu

<a href="https://sciendo.com/article/10.2478/jvetres-2022-0043" target="_blank" >https://sciendo.com/article/10.2478/jvetres-2022-0043</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.2478/jvetres-2022-0043" target="_blank" >10.2478/jvetres-2022-0043</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Examination of immunogenic properties of recombinant antigens based on p22 protein from African swine fever virus

Popis výsledku v původním jazyce

Introduction: The single member of the Asfarviridae family is African swine fever virus (ASFV). This double-stranded DNA virus infects wild and farmed swine and loses the pig industry large sums of money. An inner envelope, capsid, and outer envelope are parts of the ASFV particle containing structural proteins playing different roles in the process of infection or host immune defence evasion. When expressed by the baculovirus system, the p22 protein from the inner envelope was found to induce partial protection against a virulent virus strain. This study aimed to express a part of this protein in a different system and evaluate its immunogenicity. Material and Methods: We designed two proteins, the extracellular (C terminal) part of the p22 protein (p22Ct) and its fusion with the heat-labile enterotoxin B subunit from Escherichia coli (LTB-p22Ct), which is supposed to be a potent enhancer of the immune response. Both proteins were produced in the E. coli expression system and subsequently used for mice immunisation to analyse their safety and immunogenicity. Results: The protein fused with LTB did not show the expected adjuvant properties and did not prove safe, because abscess formation was observed after immunisation. In contrast, immunisation with the p22Ct protein alone induced a higher antibody titre but caused no adverse symptoms. Conclusion: These results show the high potential of the p22Ct region as an immunogenic protein for ASFV serological detection purposes.

Název v anglickém jazyce

Examination of immunogenic properties of recombinant antigens based on p22 protein from African swine fever virus

Popis výsledku anglicky

Introduction: The single member of the Asfarviridae family is African swine fever virus (ASFV). This double-stranded DNA virus infects wild and farmed swine and loses the pig industry large sums of money. An inner envelope, capsid, and outer envelope are parts of the ASFV particle containing structural proteins playing different roles in the process of infection or host immune defence evasion. When expressed by the baculovirus system, the p22 protein from the inner envelope was found to induce partial protection against a virulent virus strain. This study aimed to express a part of this protein in a different system and evaluate its immunogenicity. Material and Methods: We designed two proteins, the extracellular (C terminal) part of the p22 protein (p22Ct) and its fusion with the heat-labile enterotoxin B subunit from Escherichia coli (LTB-p22Ct), which is supposed to be a potent enhancer of the immune response. Both proteins were produced in the E. coli expression system and subsequently used for mice immunisation to analyse their safety and immunogenicity. Results: The protein fused with LTB did not show the expected adjuvant properties and did not prove safe, because abscess formation was observed after immunisation. In contrast, immunisation with the p22Ct protein alone induced a higher antibody titre but caused no adverse symptoms. Conclusion: These results show the high potential of the p22Ct region as an immunogenic protein for ASFV serological detection purposes.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10607 - Virology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2022

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Veterinary Research

ISSN

2450-7393

e-ISSN

2450-8608

Svazek periodika

66

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

8

Strana od-do

297-304

Kód UT WoS článku

000846940000001

EID výsledku v databázi Scopus

2-s2.0-85137050050