Molecular cloning and sequence analysis of the human parainfluenza 3 virus mRNA encoding the P and C proteins |
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Authors: | M S Galinski M A Mink D M Lambert S L Wechsler M W Pons |
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Affiliation: | 1. Duke Global Health Institute, Duke University, Durham, NC, USA;2. Division of Infectious Diseases, Duke University School of Medicine, Durham, NC, USA;3. Duke University Infection Prevention and Hospital Epidemiology, Duke Hospital, Durham, NC, USA;4. Duke University Hospital Hematological Oncology Unit, Duke Hospital, Durham, NC, USA;5. Department of Pathology, School of Medicine, Duke University, Durham, NC, USA;6. Global Health Research Center, Duke–Kunshan University, Kunshan, Jiangsu, China;7. Emerging Infectious Diseases Program, Duke–NUS Medical School, Singapore;1. State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, LuoJia Hill, Wuhan 430072, China |
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Abstract: | The sequence of the mRNA encoding the phosphoprotein (P protein) of the human parainfluenza virus 3 (PF3) was determined by molecular cloning. In other Parmyxoviridae the P protein mRNA is functionally bicistronic and encodes an additional smaller nonstructural protein termed C. In this report three open reading frames (ORF) are described. These consist of a single long ORF encoding the P protein, and two shorter ORFs encoding the structural Vp18 protein (analogous to the Sendai C protein) and a putative polypeptide termed D protein. The encoded phosphoprotein consists of 603 amino acids and has a predicted molecular weight of 67,683. The C protein consists of 199 amino acids and has a predicted molecular weight of 23,288. The D protein consists of 140 amino acids and has a predicted molecular weight of 16,270. Although the D protein has not yet been demonstrated in vivo its synthesis could be demonstrated in vitro using a rabbit reticulocyte lysate system. Thus it appears that unlike the other paramyxoviruses, the PF3 P protein mRNA may be functionally tricistronic. |
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