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Schematic representation of the measles virus particle and mechanism of membrane fusion

Sibylle Schneider-Schaulies and Volker ter Meulen
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Figure 1. Schematic representation of the measles virus particle and mechanism of membrane fusion. (a) The core structure of the measles virus (MV) is a pleomorphic ribonucleoprotein particle (RNP), consisting of the RNA genome tightly encapsidated by nucleocapsid proteins and the viral polymerase complex [the latter consisting of the large protein (L) and the phosphoprotein (P)]. Whether the RNA is inside the RNP as depicted schematically here, or, as recently shown for vesicular stomatitis virus (Ref. 108), at least partially exposed to the viral lumen, has not been clearly resolved as yet for MV. The matrix (M) protein links the RNP to the lipid envelope, from which the two viral glycoproteins – the fusion (F) and the haemagglutinin (H) proteins – project. The M protein is also thought to interact with the cytoplasmic domains of the viral glycoproteins (Ref. 109). (b) Model of MV-induced membrane fusion and conformational changes within the F protein. The H protein mediates attachment of virions to cellular surface proteins and also provides a helper function for membrane fusion (Refs 15, 16). Fusion requires the MV glycoprotein complex, consisting of an H protein tetramer and a trimer of the proteolytically activated F protein (F1–F2). [The F protein is synthesised as a precursor protein (F0), and is proteolytically cleaved and activated into the disulphide-bonded F1–F2 heterodimer in the trans-Golgi compartment (Ref. 17)]. Interaction of the MV H protein with its cellular receptor (CD150 is shown here), triggers a conformational change within the F1–F2 heterodimer that leads to insertion of the hydrophobic fusion domain (the N-terminus of the F1 subunit; represented by the arrowheads) into the target cell membrane. Intramolecular rearrangements leading to the formation of a coiled-coil structure within this subunit then occur, brought about by the interaction of two a-helical domains (Ref. 19). In this way, the membranes to be fused are brought into close proximity, which is a prerequisite for the mixing of the outer leaflets (hemifusion), and subsequent fusion (fig001ssw).

References cited in Figure 1

15 Nussbaum, O. et al. (1995) Functional and structural interactions between measles virus hemagglutinin and CD46. J Virol 69, 3341-3349, PubMed

16 Plemper, R.K., Hammond, A.L. and Cattaneo, R. (2001) Measles virus envelope glycoproteins hetero-oligomerize in the endoplasmic reticulum. J Biol Chem 276, 44239-44246, PubMed

17 Bolt, G. and Pedersen, I.R. (1998) The role of subtilisin-like proprotein convertases for cleavage of the measles virus fusion glycoprotein in different cell types. Virology 252, 387-398, PubMed

19 Baker, K.A. et al. (1999) Structural basis for paramyxovirus-mediated membrane fusion. Mol Cell 3, 309-319, PubMed

108 Iseni, F. et al. (2000) Structure of the RNA inside the vesicular stomatitis virus nucleocapsid. Rna 6, 270-281, PubMed

109 Griffin, D.E. and Bellini, W.J. (1996) Measles virus. In Virology (Fields, B.N. et al., eds), pp. 1267-1311, Lippincott-Raven, Philadelphia

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