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The Predicted Primary Structure of the Peplomer Protein E2 of the Porcine Coronavirus Transmissible Gastroenteritis Virus

Institut National de la Recherche Agronomique, Station de Recherches de Virologie et d'Immunologie, F-78850 Thiverval-Grignon, France

The complete nucleotide sequence of cloned cDNAs containing the E2 glycoprotein-encoding region of the genome of transmissible gastroenteritis virus (TGEV) has been determined. A single large translatable frame of 4.3 kb starting at 8.2 kb from the 3' end of the genome was identified. Its deduced amino acid sequence contains the characteristic features of a coronavirus peplomer protein: (i) the precursor polypeptide of TGEV E2 is 1447 residues long (i.e. 285 longer than the avian infectious bronchitis coronavirus spike protein); (ii) partial N-terminal sequencing demonstrated that a putative secretory signal sequence of 16 amino acids is absent in the virion-associated protein; (iii) the predicted mol. wt. of the apoprotein is 158K; most of the 32 potential N-glycosylation sites available in the sequence are presumed to be functional to account for the difference between this and the experimentally determined value (200K to 220K); (iv) a typical hydrophobic sequence near the C terminus is likely to be responsible for anchoring the peplomer to the virion envelope.

Keywords: TGEV, peplomer protein E2, gene sequence

Received 18 December 1986; accepted 31 March 1987.

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