Loading…

Development of Novel Recombinant Antigens of Nucleoprotein and Matrix Proteins of IPorcine orthorubulavirus:/I Antigenicity and Structural Prediction

Blue eye disease (BED) is a swine viral infection that affects the pork industry of Mexico. Porcine orthorubulavirus (PRV) is the etiological agent, and the hemagglutinin-neuraminidase protein (HN) is characterized as the best antigen for serological tests, although other structural proteins, includ...

Full description

Saved in:
Bibliographic Details
Published in:Viruses 2022-09, Vol.14 (9)
Main Authors: Lara-Romero, Rocío, Cerriteño-Sánchez, José Luis, Mendoza-Elvira, Susana, García-Cambrón, José Bryan, Castañeda-Montes, María Azucena, Pérez-Aguilar, José Manuel, Cuevas-Romero, Julieta Sandra
Format: Article
Language:English
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Blue eye disease (BED) is a swine viral infection that affects the pork industry of Mexico. Porcine orthorubulavirus (PRV) is the etiological agent, and the hemagglutinin-neuraminidase protein (HN) is characterized as the best antigen for serological tests, although other structural proteins, including the nucleoprotein (NP) and the matrix (M) protein, have been investigated during the infection of members of the Paramyxoviridae family, generating promising results. Herein, for the first time, we successfully produced and characterized both the NP and M proteins of PRV by using a recombinant strategy in the E. coli heterologous system. The ORF of the NP and M genes were cloned in-frame with the pET-SUMO expression vector. Recombinant proteins proved to be a sensitive target to detect seroconversion at 7 days until 28 days in vaccinated mice (BALB/c) by indirect ELISAs. Immunoreactivity was also tested using porcine serum samples, in which antibodies were recognized from early stages to a persistence of PRV infection, which is indicative that these proteins contain properties similar to native antigens. The predicted tertiary structure showed that both proteins have a conserved structure that resembles those found in others Paramyxovirus. Our results pave the way for developing biotechnological tools based on these proteins for the control and prevention of BED.
ISSN:1999-4915
1999-4915
DOI:10.3390/v14091946