Morbillivirus and henipavirus attachment protein cytoplasmic domains differently affect protein expression, fusion support and particle assembly

The Journal of General Virology
Bevan SawatskyVeronika von Messling

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 signific...Continue Reading

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Citations

Apr 12, 2019·Journal of Virology·Birgit G Bradel-TrethewayHector C Aguilar
Oct 17, 2018·NPJ Vaccines·Rebecca SchmidtVeronika von Messling
Aug 14, 2019·Transboundary and Emerging Diseases·Kemang LiShuo Su
Mar 9, 2019·Virology Journal·Santiago Rendon-MarinJulian Ruiz-Saenz

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Datasets Mentioned

BETA
AF212302
AF017149
AY386316
AF457102

Methods Mentioned

BETA
flow cytometry
transfection
FACS
transfections
PCR
Assay

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