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Deduced Amino Acid Sequences Surrounding the Fusion Glycoprotein Cleavage Site and of the Carboxyl-terminus of Haemagglutinin–Neuraminidase Protein of the Avirulent Thermostable Vaccine Strain I-2 of Newcastle disease virus

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Abstract

A single-tube RT-PCR technique generated a 387 bp or 300 bp cDNA amplicon covering the F0 cleavage site or the carboxyl (C)-terminus of the HN gene, respectively, of Newcastle disease virus (NDV) strain I-2. Sequence analysis was used to deduce the amino acid sequences of the cleavage site of F protein and the C-terminus of HN protein, which were then compared with sequences for other NDV strains. The cleavage site of NDV strain I-2 had a sequence motif of 112 RKQGRLIG119, consistent with an avirulent phenotype. Nucleotide sequencing and deduction of amino acids at the C-terminus of HN revealed that strain I-2 had a 7-amino-acid extension (VEILKDGVREARSSR. This differs from the virulent viruses that caused outbreaks of Newcastle disease in Australia in the 1930s and 1990s, which have HN extensions of 0 and 9 amino acids, respectively. Amino acid sequence analyses of the F and HN genes of strain I-2 confirmed its avirulent nature and its Australian origin.

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Abbreviations

bp:

base pairs

cDNA:

complementary deoxyribose nucleic acid

F0 protein:

fusion uncleaved protein

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Authors and Affiliations

  1. School of Veterinary Science, University of Queensland, Brisbane

    P. N. Wambura, J. Meers & P. B. Spradbrow

  2. Clinical Medical Virology Centre, University of Queensland & Sir Albert Sakzewski Virus Research Centre, Herston, Australia

    J. A. Kattenbelt & A. R. Gould

Authors
  1. P. N. Wambura
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  2. J. Meers
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  3. J. A. Kattenbelt
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  4. A. R. Gould
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  5. P. B. Spradbrow
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Correspondence to P. N. Wambura.

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Wambura, P.N., Meers, J., Kattenbelt, J.A. et al. Deduced Amino Acid Sequences Surrounding the Fusion Glycoprotein Cleavage Site and of the Carboxyl-terminus of Haemagglutinin–Neuraminidase Protein of the Avirulent Thermostable Vaccine Strain I-2 of Newcastle disease virus . Vet Res Commun 31, 105–112 (2007). https://doi.org/10.1007/s11259-006-3290-8

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