The Cholera Toxin B Subunit (CTB) Fused to the Porcine Arterivirus Matrix M and GP5 Envelope Proteins Fails to Enhance the GP5-Specific Antibody Response in Pigs Immunized with Adenovectors
- PMID: 25801418
- DOI: 10.1007/s12033-015-9861-6
The Cholera Toxin B Subunit (CTB) Fused to the Porcine Arterivirus Matrix M and GP5 Envelope Proteins Fails to Enhance the GP5-Specific Antibody Response in Pigs Immunized with Adenovectors
Abstract
The porcine reproductive and respiratory syndrome virus (PRRSV) is an arterivirus of the Arteriviridae family. As the current commercial vaccines are incompletely protective effective against PRRSV infection, we developed a vaccine strategy using replicating but non-disseminating adenovectors (rAdVs) expressing the PRRSV M matrix protein in fusion with the neutralizing major epitope-carrying GP5 envelope protein (Roques et al. in Vet Res 44:17, 2013). Although production of GP5-specific antibodies (Abs) was observed, no PRRSV-specific neutralizing Abs (NAbs) were induced in pigs given the rAdVs expressing M-GP5 or M-GP5m (GP5m being a mutant form of GP5). Nevertheless, partial protection was observed in the M-GP5m-rAdV-inoculated pigs experimentally infected with PRRSV. Here, we determined the impact of the cholera toxin B subunit (CTB, known for its adjuvant effect) in fusion with the C-terminus of M-GP5m on the Ab response to PRRSV. Three-week-old pigs were immunized twice both intramuscularly and intranasally at 3-week intervals with rAdV-expressing the green fluorescent protein (rAdV-GFP), rAdV-M-GP5m, or rAdV-M-GP5m-CTB. Pigs immunized with rAdV-M-GP5m showed a high level of serum GP5-specific Abs (as determined by an indirect ELISA). In contrast, CTB in fusion with M-GP5m had an unexpected severe negative impact on GP5-specific Ab production. PRRSV-specific NAbs could not be detected in any pigs of all groups.
Similar articles
-
Immunogenic and protective properties of GP5 and M structural proteins of porcine reproductive and respiratory syndrome virus expressed from replicating but nondisseminating adenovectors.Vet Res. 2013 Mar 11;44(1):17. doi: 10.1186/1297-9716-44-17. Vet Res. 2013. PMID: 23497101 Free PMC article.
-
Recombinant adenovirus expressing GP5 and M fusion proteins of porcine reproductive and respiratory syndrome virus induce both humoral and cell-mediated immune responses in mice.Vet Immunol Immunopathol. 2006 Sep 15;113(1-2):169-80. doi: 10.1016/j.vetimm.2006.05.001. Epub 2006 Jun 13. Vet Immunol Immunopathol. 2006. PMID: 16777236
-
The immunogenicity of DNA constructs co-expressing GP5 and M proteins of porcine reproductive and respiratory syndrome virus conjugated by GPGP linker in pigs.Vet Microbiol. 2010 Dec 15;146(3-4):189-99. doi: 10.1016/j.vetmic.2010.05.007. Epub 2010 May 10. Vet Microbiol. 2010. PMID: 20570063
-
Current knowledge on the structural proteins of porcine reproductive and respiratory syndrome (PRRS) virus: comparison of the North American and European isolates.Arch Virol. 2000;145(4):659-88. doi: 10.1007/s007050050662. Arch Virol. 2000. PMID: 10893147 Free PMC article. Review.
-
Membrane proteins of arterivirus particles: structure, topology, processing and function.Virus Res. 2014 Dec 19;194:16-36. doi: 10.1016/j.virusres.2014.09.010. Epub 2014 Sep 30. Virus Res. 2014. PMID: 25278143 Free PMC article. Review.
Cited by
-
Development of a Ferritin Protein Nanoparticle Vaccine with PRRSV GP5 Protein.Viruses. 2024 Jun 20;16(6):991. doi: 10.3390/v16060991. Viruses. 2024. PMID: 38932282 Free PMC article.
-
Combined Subcutaneous-Intranasal Immunization With Epitope-Based Antigens Elicits Binding and Neutralizing Antibody Responses in Serum and Mucosae Against PRRSV-2 and SARS-CoV-2.Front Immunol. 2022 Mar 31;13:848054. doi: 10.3389/fimmu.2022.848054. eCollection 2022. Front Immunol. 2022. PMID: 35432364 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials
Miscellaneous