Structural Insights into Rotavirus Entry.

  title={Structural Insights into Rotavirus Entry.},
  author={Javier M Rodr{\'i}guez and Daniel Luque},
  journal={Advances in experimental medicine and biology},
To initiate infection, non-enveloped viruses must recognize a target cell and penetrate the cell membrane by pore formation or membrane lysis. Rotaviruses are non-enveloped dsRNA viruses that infect the mature intestinal epithelium. They are major etiologic agents of diarrheal disease in human infants, as well as in young individuals of various avian and mammalian species. Rotavirus entry into the cell is a complex multistep process initiated by the interaction of the tip of the viral spike… 

Rotavirus cell entry: not so simple after all.

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Penetration of non-enveloped viruses.



Early steps in rotavirus cell entry.

Recent molecules found to be associated with rotavirus cell entry include integrins, alphavbeta3, and alphaxbeta2, and a heat shock protein, which could explain the cell and tissue tropism of these viruses.

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This review focuses on the current understanding of the structural basis of the molecular processes that govern the replication of rotavirus.

Rotavirus cell entry.

These studies only begin to capture the basic cellular, molecular, and structural mechanisms of cell entry, but the unusual features they have uncovered and many intriguing questions they have raised undoubtedly will prompt further investigations.

New Insights into Rotavirus Entry Machinery: Stabilization of Rotavirus Spike Conformation Is Independent of Trypsin Cleavage

Cryo-EM three-dimensional reconstruction of uncleaved virions showed spikes with a structure compatible with the atomic model of the cleaved spike, and indistinguishable from that of digested particles, suggesting that the spike precursor protein must be proteolytically processed not to achieve a rigid conformation, but to allow the conformational changes that drive virus entry.

Structural rearrangements in the membrane penetration protein of a non-enveloped virus

The crystal structure of the main part of VP4, a principal component in the entry apparatus of rotavirus, is determined and it is shown that VP4 also undergoes a second rearrangement, which resembles the conformational transitions of membrane fusion proteins of enveloped viruses.

Substantial Receptor‐induced Structural Rearrangement of Rotavirus VP8*: Potential Implications for Cross‐Species Infection

The first observation of significant structural rearrangement of VP8* from human and animal rotavirus strains upon glycan receptor binding is reported, which delivers important insights into how human andAnimal rotaviruses utilize the wider range of cellular glycans identified asVP8* binding partners.

A Rotavirus Spike Protein Conformational Intermediate Binds Lipid Bilayers

It is proposed that VP5*, the rotavirus protein believed to interact with the membrane bilayer, binds lipid bilayers in an intermediate conformational state, analogous to the extended intermediate conformation of enveloped-virus fusion proteins.

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The viral and cellular factors involved in the different stages of a productive virus cell entry are reviewed and the journey that the author has taken into the cell to learn about virus entry is shared.

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Comparing the entry characteristics of four rotavirus strains known to have different receptor requirements found that even though all the strains share their requirements for hsc70, dynamin, and cholesterol, three of them differ from the simian strain RRV in the endocytic pathway used.