Analysis of the fusion protein gene of the porcine rubulavirus LPMV: comparative analysis of paramyxovirus F proteins

Autor:	M, Berg, A C, Bergvall, M, Svenda, A, Sundqvist, J, Moreno-López, T, Linné
Rok vydání:	1997
Předmět:	Binding Sites DNA Complementary Base Sequence Genes Viral Sequence Homology Amino Acid Swine Molecular Sequence Data Open Reading Frames Rubulavirus Mumps virus DNA Viral Animals Humans Paramyxovirinae Amino Acid Sequence Cloning Molecular Viral Fusion Proteins Phylogeny
Zdroj:	Virus genes. 14(1)
ISSN:	0920-8569
Popis:	Complementary DNA clones representing the fusion (F) protein gene of the porcine rubulavirus LPMV were isolated and sequenced. The F gene was found to be 1,845 nucleotides long containing one long open reading frame capable of encoding a protein of 541 amino acids. The cleavage motif for F0 into F1 and F2 is His-Arg-Lys-Lys-Arg. A sequence comparison and a phylogenetic analysis was performed in order to identify possible functional domains of paramyxovirus fusion proteins and also to classify the porcine rubulavirus. The F gene of LPMV is most closely related to the human mumps virus and simian virus type 5 F genes, and is therefore classified into the rubulavirus genus. A coding region for a small hydrophobic protein was however not found between the F and hemagglutinin-neuraminidase (HN) genes as previously found in both SV5 and mumps.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::fd5c6b5921aba71f6ef96495101245cd https://pubmed.ncbi.nlm.nih.gov/9208455 Zobrazit plný text záznamu Full text from SpringerLink