Zhaoyang Ji,Da Shi,Hongyan Shi,Xiaobo Wang,Jianfei Chen,Jianbo Liu,Dandan Ye,Zhaoyang Jing,Qiuge Liu,Qianjin Fan,Mingwei Li,Guangyi Cong,Jiyu Zhang,Yuru Han,Xin Zhang,Li Feng

Vet Microbiol.2020 Dec 13;253:108955.doi: 10.1016/j.vetmic.2020.108955. Online ahead of print.

Abstract

In recent years, a novel, highly virulent variant of porcine epidemic diarrhea virus (PEDV) has emerged, causing substantial economic losses to the pork industry worldwide. In this study, a PEDV strain named LNsy was successfully isolated in China. Phylogenetic analysis based on the whole genome revealed that PEDV LNsy belonged to the G2 subtype. For the first time, a unique four amino acids (4-aa) insertion was identified in the COE region of the spike (S) protein (residues 499-640), resulting in an extra alpha helix in the spatial structure of the COE region. To determine changes in virus-neutralization (VN) antibody reactivity of the virus, polyclonal antibodies (PAbs) against the S protein of different subtypes were used in a VN test. Both PAbs against the S protein of the G1 and G2 subtype showed reduced VN reactivity to PEDV LNsy. Further, recombination analyses revealed that PEDV LNsy was the result of recombination between PEDV GDS13 and GDS46 strains at the genomic breakpoints (nt 17,959-20,594 in the alignment) in the ORF1b gene of the genomes. Pathological examination showed gross morphological pathological changes in the gut, including significant villus atrophy and shedding of the infected piglets. These results indicated that a 4-aa insertion in the COE region of the S protein may have partly altered the profiles of VN antibodies and thus it will be important to develop vaccine candidates to resist wild virus infection and to monitor the genetic diversity of PEDV.

Keywords: Alpha helix; Natural recombinant; Pathogenic; Porcine epidemic diarrhea virus; Virus-Neutralization reactivity.

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