title: Morbillivirus and henipavirus attachment protein cytoplasmic domains differently affect protein expression, fusion support and particle assembly.
abstract: The amino-terminal cytoplasmic domains of paramyxovirus attachment glycoproteins include trafficking signals that influence protein processing and cell surface expression. To characterize the role of the cytoplasmic domain in protein expression, fusion support and particle assembly in more detail, we constructed chimeric Nipah virus (NiV) glycoprotein (G) and canine distemper virus (CDV) haemagglutinin (H) proteins carrying the respective heterologous cytoplasmic domain, as well as a series of mutants with progressive deletions in this domain. CDV H retained fusion function and was normally expressed on the cell surface with a heterologous cytoplasmic domain, while the expression and fusion support of NiV G was dramatically decreased when its cytoplasmic domain was replaced with that of CDV H. The cell surface expression and fusion support functions of CDV H were relatively insensitive to cytoplasmic domain deletions, while short deletions in the corresponding region of NiV G dramatically decreased both. In addition, the first 10 residues of the CDV H cytoplasmic domain strongly influence its incorporation into virus-like particles formed by the CDV matrix (M) protein, while the co-expression of NiV M with NiV G had no significant effect on incorporation of G into particles. The cytoplasmic domains of both the CDV H and NiV G proteins thus contribute differently to the virus life cycle.
authors.affiliation: Galveston National Laboratory, University of Texas Medical Branch, Galveston, Texas, USA.|INRS-Institut Armand-Frappier, University of Quebec, Laval, Quebec, Canada.|Veterinary Medicine Division, Paul-Ehrlich-Institute, Langen, Germany.|Department of Microbiology & Immunology, University of Texas Medical Branch, Galveston, Texas, USA.
authors.forename: Bevan
authors.initials: B
authors.lastname: Sawatsky
authors.affiliation: Department of Microbiology & Immunology, University of Texas Medical Branch, Galveston, Texas, USA.|Galveston National Laboratory, University of Texas Medical Branch, Galveston, Texas, USA.
authors.forename: Dennis A
authors.initials: DA
authors.lastname: Bente
authors.affiliation: Faculty of Veterinary Medicine, University of Calgary, Calgary, Alberta, Canada.
authors.forename: Markus
authors.initials: M
authors.lastname: Czub
authors.affiliation: INRS-Institut Armand-Frappier, University of Quebec, Laval, Quebec, Canada.|Veterinary Medicine Division, Paul-Ehrlich-Institute, Langen, Germany.
authors.forename: Veronika
authors.initials: V
authors.lastname: von Messling
mesh_terms: D000595:Amino Acid Sequence; D015967:Gene Expression Regulation, Viral / Q000502:physiology*; D045403:Henipavirus / Q000235:genetics / Q000378:metabolism*; D018103:Morbillivirus / Q000235:genetics / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism*; D019065:Virus Assembly / Q000502:physiology*; D053586:Virus Internalization
chemical_list: D014759:Viral Envelope Proteins
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