Research Article

Molecular cloning and characterization of the pseudorabies virus UL31 gene

Published: March 17, 2014
Genet. Mol. Res. 13 (1) : 1832-1847 DOI: 10.4238/2014.March.17.11

Abstract

We amplified a 816-bp sequence of the UL31 gene from the pseudorabies virus (PRV) Becker strain genome. Evidence that this was the UL31 gene was confirmed by cloning and sequencing. The PRV UL31 gene encodes a putative protein of 271-amino acid residues, which was designated the UL31 protein. Bioinformatic analysis indicated that PRV UL31 contains a conserved PHA03328 domain, closely related with the herpes virus nuclear egress lamina protein UL31 family and highly conserved among counterparts encoded by herpes UL31 genes. Nucleic acid sequence and amino acid sequence alignments demonstrated that PRV UL31 has a relatively higher homology with UL31 homologous proteins of subfamily Alphaherpesvirinae than other subfamilies. In addition, phylogenetic analysis showed that PRV UL31 has a close evolutionary relationship with members of the subfamily Alphaherpesvirinae, especially bovine herpesvirus 1 (BoHV-1), BoHV-5, equine herpesvirus 4 (EHV-4), EHV-9 and EHV-1. Antigen prediction demonstrated that several potential B-cell epitopes are located in PRV UL31. Additionally, secondary structure and three-dimension structure prediction revealed that PRV UL31 predominantly consists of α-helix. Taken together, these results provide insight on the function and mechanism of UL31 during PRV infection.

We amplified a 816-bp sequence of the UL31 gene from the pseudorabies virus (PRV) Becker strain genome. Evidence that this was the UL31 gene was confirmed by cloning and sequencing. The PRV UL31 gene encodes a putative protein of 271-amino acid residues, which was designated the UL31 protein. Bioinformatic analysis indicated that PRV UL31 contains a conserved PHA03328 domain, closely related with the herpes virus nuclear egress lamina protein UL31 family and highly conserved among counterparts encoded by herpes UL31 genes. Nucleic acid sequence and amino acid sequence alignments demonstrated that PRV UL31 has a relatively higher homology with UL31 homologous proteins of subfamily Alphaherpesvirinae than other subfamilies. In addition, phylogenetic analysis showed that PRV UL31 has a close evolutionary relationship with members of the subfamily Alphaherpesvirinae, especially bovine herpesvirus 1 (BoHV-1), BoHV-5, equine herpesvirus 4 (EHV-4), EHV-9 and EHV-1. Antigen prediction demonstrated that several potential B-cell epitopes are located in PRV UL31. Additionally, secondary structure and three-dimension structure prediction revealed that PRV UL31 predominantly consists of α-helix. Taken together, these results provide insight on the function and mechanism of UL31 during PRV infection.