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Hydrogen-deuterium exchange mass spectrometry of rotavirus NSP2/NSP5 biomolecular condensates

ABSTRACT: Biomolecular condensates selectively compartmentalise and organise biomolecules within the crowded cellular milieu, and are instrumental in some disease mechanisms, including aiding RNA virus replication. Upon infection, many RNA viruses form biomolecular condensates that are often referred to as viral factories. The assembly mechanism of these viral factories remains poorly defined, but involves transient, non-stoichiometric protein/RNA interactions, posing challenges for their characterisation. Here we present HDX-MS data of NSP2 and NSP5, in a biomolecular condensate to study the mechanism of condensate assembly.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Bovine Rotavirus Strain Rf

SUBMITTER: Antonio Calabrese

LAB HEAD: Antonio Calabrese

PROVIDER: PXD058097 | Pride | 2025-06-23

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	230308_NSP2_NSP5WT_1.DnX	Other
	230309_NSP5WT_NSP2.DnX	Other
	230815_NSP2_NSP5dC.DnX	Other
	BS16AMC_230804_09.raw.zip	Raw
	BS16AMC_230804_11.raw.zip	Raw

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Publications

Uncovering protein conformational dynamics within two-component viral biomolecular condensates.

Colyer Alice A Acker Julia J Borodavka Alexander A Calabrese Antonio N AN

Protein science : a publication of the Protein Society 20250701 7

Biomolecular condensates selectively compartmentalize and organize biomolecules within the crowded cellular milieu and are instrumental in some disease mechanisms. Upon infection, many RNA viruses form biomolecular condensates that are often referred to as viral factories. The assembly mechanism of these viral factories remains poorly defined but involves transient, non-stoichiometric protein/RNA interactions, making their structural characterization challenging. Here, we sought to investigate t ...[more]

PMID: 40521608

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