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Review
. 2011 Jul;1(1):13-8.
doi: 10.1016/j.coviro.2011.05.001.

Receptors and tropisms of envelope viruses

Kouki Morizono  1 , Irvin S Y Chen
Affiliations
Review

Receptors and tropisms of envelope viruses

Kouki Morizono et al. Curr Opin Virol. 2011 Jul.

Abstract

Envelope virus replication begins with receptor binding, followed by fusion of the viral envelope with the cell membrane. The binding and fusion steps are usually mediated by envelope proteins. The ability of envelope proteins of a particular virus to bind and fuse with target cells defines the host range of the virus, known as 'viral tropism'. The mechanism(s) of fusion by the viral envelope is largely categorized as either pH-dependent or pH-independent. By redirecting the binding specificities of envelope proteins to desired target molecules while maintaining fusion activity, it is possible to redirect the tropisms of virus and viral vectors, enabling specific killing and/or transduction of desired cells in vivo. Recently, a lipid, phosphatidylserine, was also shown to mediate binding of virus, which affects the tropisms of viruses and viral vectors.

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Figures

Figure 1
Figure 1
A) pH-dependent entry of influenza virus. The HA protein is shown as a monomer to simplify the entry mechanism; however, it forms trimers. B) pH-dependent entry of retargeted Sindbis virus. The heterodimer of E2 and E1 is shown as a monomer to simplify the entry mechanism; however, the heterodimer forms trimers.
Figure 2
Figure 2
A) pH-independent entry of HIV. gp160 is shown as a monomer to simplify the entry mechanism; however, it forms trimers. B) pH-dependent entry of retargeted measles virus. H and F are shown as a monomer to simplify the entry mechanism; however, H forms tetramers and F forms trimers.
Figure 3
Figure 3
Schematic representations of the mechanism by which hGas6 mediates phagocytosis of dead cells and the apoptotic mimicry pathway for virus entry.
See this image and copyright information in PMC

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