Article ; Online: Spectroscopic analysis of the bacterially expressed head domain of rotavirus VP6.
2024 Volume 44, Issue 5
Abstract: The rotavirus capsid protein VP6 forms the middle of three protein layers and is responsible for many critical steps in the viral life cycle. VP6 as a structural protein can be used in various applications including as a subunit vaccine component. The ... ...
| Abstract | The rotavirus capsid protein VP6 forms the middle of three protein layers and is responsible for many critical steps in the viral life cycle. VP6 as a structural protein can be used in various applications including as a subunit vaccine component. The head domain of VP6 (VP6H) contains key sequences that allow the protein to trimerize and that represent epitopes that are recognized by human antibodies in the viral particle. The domain is rich in β-sheet secondary structures. Here, VP6H was solubilised from bacterial inclusion bodies and purified using a single affinity chromatography step. Spectral (far-UV circular dichroism and intrinsic tryptophan fluorescence) analysis revealed that the purified domain had native-like secondary and tertiary structures. The domain could maintain structure up to 44°C during thermal denaturation following which structural changes result in an intermediate forming and finally irreversible aggregation and denaturation. The chemical denaturation with urea and guanidinium hydrochloride produces intermediates that represent a loss in the cooperativity. The VP6H domain is stable and can fold to produce its native structure in the absence of the VP6 base domain but cannot be defined as an independent folding unit. |
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| MeSH term(s) | Capsid Proteins/chemistry ; Capsid Proteins/genetics ; Antigens, Viral/chemistry ; Antigens, Viral/genetics ; Rotavirus/chemistry ; Protein Denaturation ; Protein Domains ; Circular Dichroism ; Protein Folding ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Humans ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism | |||||
| Chemical Substances | Capsid Proteins ; VP6 protein, Rotavirus ; Antigens, Viral ; Recombinant Proteins | |||||
| Language | English | |||||
| Publishing date | 2024-03-28 | |||||
| Publishing country | England | |||||
| Document type | Journal Article ; Research Support, Non-U.S. Gov't | |||||
| ZDB-ID | 764946-0 | |||||
| ISSN | 1573-4935 ; 0144-8463 | |||||
| ISSN (online) | 1573-4935 | |||||
| ISSN | 0144-8463 | |||||
| DOI | 10.1042/BSR20232178 | |||||
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| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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