Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production

• Published in: Viruses 2014-08, Vol.6 (8), p.3019-3054
• Main Authors: El Najjar, Farah, Schmitt, Anthony P, Dutch, Rebecca Ellis
• Format: Article
• Language: English
• Subjects: Animals; glycoproteins; Glycoproteins - metabolism; Humans; matrix protein; Measles virus; membrane rafts; Mumps virus; Newcastle disease virus; Paramyxovirinae - physiology; Paramyxovirus; Respiratory syncytial virus; Review; Rinderpest virus; Viral Envelope Proteins - metabolism; Viral Matrix Proteins - metabolism; viral trafficking; Virus Assembly; virus budding; Virus Release
• ISSN: 1999-4915; 1999-4915
• DOI: 10.3390/v6083019

Paramyxoviruses are a family of negative sense RNA viruses whose members cause serious diseases in humans, such as measles virus, mumps virus and respiratory syncytial virus; and in animals, such as Newcastle disease virus and rinderpest virus. Paramyxovirus particles form by assembly of the viral matrix protein, the ribonucleoprotein complex and the surface glycoproteins at the plasma membrane of infected cells and subsequent viral budding. Two major glycoproteins expressed on the viral envelope, the attachment protein and the fusion protein, promote attachment of the virus to host cells and subsequent virus-cell membrane fusion. Incorporation of the surface glycoproteins into infectious progeny particles requires coordinated interplay between the three viral structural components, driven primarily by the matrix protein. In this review, we discuss recent progress in understanding the contributions of the matrix protein and glycoproteins in driving paramyxovirus assembly and budding while focusing on the viral protein interactions underlying this process and the intracellular trafficking pathways for targeting viral components to assembly sites. Differences in the mechanisms of particle production among the different family members will be highlighted throughout.