Research Article

Bioinformatic analysis and characteristics of glycoprotein C encoded by the newly identified UL44 gene of duck plague virus

Published: June 17, 2014
Genet. Mol. Res. 13 (2) : 4505-4515 DOI: https://doi.org/10.4238/2014.June.17.2
Cite this Article:
(2014). Bioinformatic analysis and characteristics of glycoprotein C encoded by the newly identified UL44 gene of duck plague virus. Genet. Mol. Res. 13(2): gmr3038. https://doi.org/10.4238/2014.June.17.2
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Abstract

Glycoprotein C is one of the duck plague virus (DPV) glycoproteins and is encoded by the DPV UL44 gene. DPV glycoprotein C (DPV-gC) comprises 431 amino acids with a putative molecular mass of 47.35 kDa. Sequence analysis indicated that the protein possesses typical characteristics of type-I membrane glycoproteins, containing an N-terminal signal sequence, an external domain, a C-terminal membrane anchor region, and a short cytoplasmic domain. Comparisons of 22 alphaherpesvirus-gC protein sequences revealed eight conservative Cys-residue sites, which may play a crucial role in the biological functions and structural stabilization of the DPV-gC protein. Estimates of potential antigenic epitopes and secondary structure identified four B cell dominant epitopes, which are located at amino acids 68-71, 87-91, 369-352, and 372-374. A model for the structure of DPV-gC was derived by associating its predicted secondary and three-dimensional structures. In conclusion, these results will provide a basis for further functional studies of DPV-gC, establishing novel clinical diagnoses of DPV, and in the development of a new DPV vaccine.

Glycoprotein C is one of the duck plague virus (DPV) glycoproteins and is encoded by the DPV UL44 gene. DPV glycoprotein C (DPV-gC) comprises 431 amino acids with a putative molecular mass of 47.35 kDa. Sequence analysis indicated that the protein possesses typical characteristics of type-I membrane glycoproteins, containing an N-terminal signal sequence, an external domain, a C-terminal membrane anchor region, and a short cytoplasmic domain. Comparisons of 22 alphaherpesvirus-gC protein sequences revealed eight conservative Cys-residue sites, which may play a crucial role in the biological functions and structural stabilization of the DPV-gC protein. Estimates of potential antigenic epitopes and secondary structure identified four B cell dominant epitopes, which are located at amino acids 68-71, 87-91, 369-352, and 372-374. A model for the structure of DPV-gC was derived by associating its predicted secondary and three-dimensional structures. In conclusion, these results will provide a basis for further functional studies of DPV-gC, establishing novel clinical diagnoses of DPV, and in the development of a new DPV vaccine.

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