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J Gen Virol 72 (1991), 75-81; DOI 10.1099/0022-1317-72-1-75
© 1991 Society for General Microbiology

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Deduced Amino Acid Sequence of the Fusion Glycoprotein of Turkey Rhinotracheitis Virus has Greater Identity with that of Human Respiratory Syncytial Virus, a Pneumovirus, than that of Paramyxoviruses and Morbilliviruses

Q. Yu1, P. J. Davis1, T. Barrett2, M. M. Binns1,{dagger}, M. E. G. Boursnell1,{ddagger}> and D. Cavanagh1

1 Institute for Animal Health, Division of Molecular Biology, Houghton Laboratory, Houghton, Huntingdon, Cambridgeshire PE17 2DA
and2 Pirbright Laboratory, Pirbright, Woking, Surrey GU24 0NF, U.K.

The sequence of the fusion (F) glycoprotein of turkey rhinotracheitis virus (TRTV) has been deduced from cDNA clones derived from oligo(dT)-selected infected cell RNA. The protein consists of 538 amino acids, the F2 and F1 subunits containing 102 (including the F2-F1 connecting peptide RRRR) and 436 residues, respectively. Each subunit has one potential N-linked glycosylation site. The protein has 38 to 39% amino acid identity with the F protein of respiratory syncytial virus (Pneumovirus genus) but only about half that with members of the other two genera (Paramyxovirus and Morbillivirus) in the Paramyxoviridae family. This is the first sequence evidence to support the view that TRTV is a pneumovirus, the first avian member of the genus to be described.

{dagger} Present address: Animal Health Trust, Lanwades Park, Kennett, Newmarket, Suffolk CB8 7PN, U.K.

{ddagger}> Present address: Immunology Limited, 184 Cambridge Science Park, Milton Road, Cambridge CB4 4GN, U.K.

Received 24 August 1990; accepted 12 October 1990.


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