Role of Envelope Proteins in Measles Virus Assembly

Maisner, Andrea

doi:10.1007/0-306-47650-9_7

Cited by 1 publication

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“…The M protein is a basic protein of 335 amino acids which is initially synthesized in the cytoplasm but rapidly associates with cellular membranes (Bellini et al, 1986;Riedl et al, 2002). In MV-infected cells, M plays the key role in the virus assembly process, because of its multiple binding capacities to different viral and cellular components (Peebles, 1991;Maisner, 2002). On the one hand, the M protein is found in perinuclear inclusions which are formed by the viral RNPs.…”

Section: Introductionmentioning

confidence: 99%

Measles virus nucleocapsid transport to the plasma membrane requires stable expression and surface accumulation of the viral matrix protein

et al. 2007

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Summary In measles virus (MV)-infected cells the matrix (M)protein plays a key role in virus assembly and budding processes at the plasma membrane because it mediates the contact between the viral surface glycoproteins and the nucleocapsids. By exchanging valine 101, a highly conserved residue among all paramyxoviral M proteins, we generated a recombinant MV (rMV) from cloned cDNA encoding for a M protein with an increased intracellular turnover. The mutant rMV was barely released from the infected cells. This assembly defect was not due to a defective M binding to other matrix-or nucleoproteins, but could rather be assigned to a reduced ability to associate with cellular membranes, and more importantly, to a defective accumulation at the plasma membrane which was accompanied by the deficient transport of nucleocapsids to the cell surface. Thus, we show for the first time that M stability and accumulation at intracellular membranes is a prerequisite for M and nucleocapsid co-transport to the plasma membrane and for subsequent virus assembly and budding processes.

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Section: Introductionmentioning

confidence: 99%