Sequence of the Spike Srotein of the Porcine Epidemic Diarrhoea Virus

Abstract

The complete sequence of the spike (S) gene of the Brl/87 isolate of porcine epidemic diarrhoea virus (PEDV) was determined from cDNA clones. The predicted polypeptide was 1383 amino acids long, contained 29 potential N-linked glycosylation sites and showed structural features similar to those of the coronavirus spike protein. The PEDV S protein, like that of the members of the transmissible gastroenteritis virus (TGEV)-related subset, lacks a proteolytic site to yield cleaved amino and carboxy subunits S1 and $2. Viral polypeptide species of the expected Mr, i.e. 170K/190K, were observed in PEDV-infected cells. Sequence comparison confirmed that, within the subset, PEDV was most closely related to the human respiratory coronavirus HCV 229E. However, PEDV S protein has an additional 250 residue N-terminal domain which is absent from HCV 229E and porcine respiratory coronavirus, the respiratory variant of TGEV. Alignment of the S1 regions revealed a second domain of about 90 residues with increased sequence divergence which might possibly express virus-specific determinants.

Identification and analysis of gp116 and gp64 structural glycoproteins of yellow head nidovirus of Penaeus monodon shrimp

“…The size of the YHV polyprotein is similar to those of the glycoproteins of vertebrates coronaviruses including avian infectious bronchitis virus (1160 amino acids) (Binns et al, 1985), feline infectious peritonitis virus (1452 amino acids) (de Groot et al, 1987a), murine hepatitis virus (1376 amino acids) (Spann et al, 1988), porcine epidemic diarrhoea virus (Duarte & Laude, 1994) (1383 amino acids) and human respiratory coronavirus (1353 amino acids) (Mounir & Talbot, 1993). However, the predicted structure of the ORF3 polyprotein is more complex, comprising six putative transmembrane regions generating three ectodomains and two intra-virion endodomains.…”

Molecular characterization and phylogenetic analysis of membrane protein genes of porcine epidemic diarrhea virus isolates in China

“…PEDV is an enveloped, single-stranded, positivesense RNA virus. The genome of it is approximately 28 kb in length and encodes four mainly structural proteins, which are the spike (S) protein, the membrane (M) protein, the envelope (E) protein, and the nucleocapsid (N) protein [6][7][8].…”

Optimization of expression and purification of recombinant S1 domain of the porcine epidemic diarrhea virus spike (PEDV- S1) protein inEscherichia coli

“…It contains a putative signal peptide (aa , a large extracellular region, a single transmembrane domain (aa 1334-1356), and a short cytoplasmic tail. Although PEDV has an uncleaved S protein because it lacks a furin cleavage site, the S protein can be divided into S1 (aa 1-735) and S2 (736-the last aa) domains based on homology with S proteins of other coronaviruses [14][15][16][17]. Like other coronavirus S proteins, the PEDV S protein is known to play a pivotal role, interacting with the cellular receptor to mediate viral entry and inducing neutralizing antibodies in the natural host [18,19].…”