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Prazak, V.

Publications and source records attributed to Prazak, V..

2 recordsLinked to original sources

Form follows function: Variable microtubule architecture in the malaria parasite

The malaria parasite undergoes a series of extensive morphological changes within its human host and mosquito vector. A scaffold of microtubules beneath a peripheral double membrane establishes and maintains the distinct shapes of all infectious forms, but the underlying structural basis remains unknown. Here we applied in situ electron cryo-tomography after focused ion beam milling to follow changes in the microtubule cytoskeleton throughout the Plasmodium life cycle. This revealed an unexpected level of structural and architectural diversity so far not observed in other organisms. Microtubules in migrating mosquito forms consist of 13 protofilaments reinforced by interrupted luminal helices. Conversely, gametocyte microtubules consist of 13 to 18 protofilaments with doublets, triplets and quadruplets of varying arrangements. We show the microtubule cytoskeleton within the native cellular context, highlighting structurally diverse apical rings which act as microtubule organising centres. This provides a unique view into a relevant human pathogen with an unusual microtubule cytoskeleton.

microbiology↗

The giant Mimivirus 1.2 Mb genome is elegantly organized into a 30 nm helical protein shield

Mimivirus is the prototype of the Mimiviridae family of giant dsDNA viruses. Little is known about the organization of the 1.2 Mb genome inside the membrane-limited nucleoid filling the [~]0.5 {micro}m icosahedral capsids. Cryo-electron microscopy, cryo-electron tomography and proteomics revealed that it is encased into a [~]30 nm diameter helical protein shell surprisingly composed of two GMC-type oxidoreductases, which also form the glycosylated fibrils decorating the capsid. The genome is arranged in 5- or 6-start left-handed super-helices, with each DNA-strand lining the central channel. This luminal channel of the nucleoprotein fiber is wide enough to accommodate oxidative stress proteins and RNA polymerase subunits identified by proteomics. Such elegant supramolecular organization would represent a remarkable evolutionary strategy for packaging and protecting the genome, in a state ready for immediate transcription upon unwinding in the host cytoplasm. The parsimonious use of the same protein in two unrelated substructures of the virion is unexpected for a giant virus with thousand genes at its disposal. One-Sentence SummaryMimivirus genome organization in the icosahedral virion.

microbiology↗