Porcine circovirus type 2 protective epitope densely carried by chimeric papaya ringspot virus-like particles expressed in Escherichia coli as a cost-effective vaccine manufacture alternative.

Authors:
Dr. Mauricio Carrillo-Tripp, PhD
Dr. Mauricio Carrillo-Tripp, PhD
Biomolecular Diversity Laboratory, Cinvestav
Associate Profesor
Computational Biophysics
Irapuato, Guanajuato | México
Laura Silva-Rosales
Laura Silva-Rosales
Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional
Mexico
Rodolfo Hernandez-Gutierrez
Rodolfo Hernandez-Gutierrez
Centro de Investigación y Estudios Avanzados del IPN

Biotechnol Appl Biochem 2017 May 20;64(3):406-414. Epub 2016 Apr 20.

Unidad de Biotecnología Médica y Farmacéutica, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Normalistas 800, Colinas de la Normal, Guadalajara, Jalisco 44270, México.

Porcine circovirus type 2 (PCV2) still represents a major problem to the swine industry worldwide, causing high mortality rates in infected animals. Virus-like particles (VLPs) have gained attention for vaccine development, serving both as scaffolds for epitope expression and immune response enhancers. The commercial subunit vaccines against PCV2 consist of VLPs formed by the self-assembly of PCV2 capsid protein (CP) expressed in the baculovirus vector system. In this work, a PCV2 protective epitope was inserted into three different regions of papaya ringspot virus (PRSV) CP, namely, the N- and C-termini and a predicted antigenic region located near the N-terminus. Wild-type and chimeric CPs were modeled in silico, expressed in Escherichia coli, purified, and visualized by transmission electron microscopy. This is the first report that shows the formation of chimeric VLPs using PRSV as epitope-presentation scaffold. Moreover, it was found that PCV2 epitope localization strongly influences VLP length. Also, the estimated yields of the chimeric VLPs at a small-scale level ranged between 65 and 80 mg/L of culture medium. Finally, the three chimeric VLPs induced high levels of immunoglobulin G against the PCV2 epitope in immunized BALB/c mice, suggesting that these chimeric VLPs can be used for swine immunoprophylaxis against PCV2.

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May 2017
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References

(Supplied by CrossRef)
Article in Arch. Virol.
Tischer et al.
Arch. Virol. 1986
Article in Vet. Microbiol.
Allan et al.
Vet. Microbiol. 1999
Article in Vet. Q.
Segalés et al.
Vet. Q. 2002
Article in J. Vet. Intern. Med.
Gillespie et al.
J. Vet. Intern. Med. 2009
Article in J. Gen. Virol.
Mahé et al.
J. Gen. Virol. 2000
Article in J. Virol.
Lekcharoensuk et al.
J. Virol. 2004
Article in Clin. Vaccine Immunol.
Trible et al.
Clin. Vaccine Immunol. 2011
Article in Arch. Virol.
Truong et al.
Arch. Virol. 2001
Article in Mol. Immunol.
Shang et al.
Mol. Immunol. 2009
Article in J. Vet. Sci.
Kim et al.
J. Vet. Sci. 2002
Article in Vet. Res. Commun.
Fan et al.
Vet. Res. Commun. 2007

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