Paramyxovirus Glycoprotein Incorporation, Assembly and Budding: A Three Way Dance for Infectious Particle Production

Viruses

Farah El Najjar¹  Anthony P. Schmitt² 

[1] Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, KY 40536, USA; E-Mail:;Department of Veterinary and Biomedical Sciences, The Pennsylvania State University, University Park, PA 16802, USA; E-Mail:

关键词: paramyxovirus;    matrix protein;    glycoproteins;    virus assembly;    viral trafficking;    membrane rafts;    virus budding;   

DOI  :  10.3390/v6083019

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland.