Dataset Information


Atomic model of an infectious rotavirus particle.

ABSTRACT: Non-enveloped viruses of different types have evolved distinct mechanisms for penetrating a cellular membrane during infection. Rotavirus penetration appears to occur by a process resembling enveloped-virus fusion: membrane distortion linked to conformational changes in a viral protein. Evidence for such a mechanism comes from crystallographic analyses of fragments of VP4, the rotavirus-penetration protein, and infectivity analyses of structure-based VP4 mutants. We describe here the structure of an infectious rotavirus particle determined by electron cryomicroscopy (cryoEM) and single-particle analysis at about 4.3 Å resolution. The cryoEM image reconstruction permits a nearly complete trace of the VP4 polypeptide chain, including the positions of most side chains. It shows how the two subfragments of VP4 (VP8(*) and VP5(*)) retain their association after proteolytic cleavage, reveals multiple structural roles for the ?-barrel domain of VP5(*), and specifies interactions of VP4 with other capsid proteins. The virion model allows us to integrate structural and functional information into a coherent mechanism for rotavirus entry.

PROVIDER: S-EPMC3025467 | BioStudies |

REPOSITORIES: biostudies

Similar Datasets

| S-EPMC114969 | BioStudies
| S-EPMC2772785 | BioStudies
| S-EPMC2330132 | BioStudies
| S-EPMC8297411 | BioStudies
1993-01-01 | S-EPMC237872 | BioStudies
| S-EPMC114321 | BioStudies
| S-EPMC2812363 | BioStudies
| S-EPMC136269 | BioStudies
| S-EPMC2496849 | BioStudies
2003-01-01 | S-EPMC164779 | BioStudies