Difference between revisions of "Part:BBa K1621001"
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This part contains the coding sequence of the N-terminal part of glycoprotein E derived form Varicella Zoster Virus. | This part contains the coding sequence of the N-terminal part of glycoprotein E derived form Varicella Zoster Virus. | ||
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| + | [[File:2015_freiburg_varicella.jpg|300px|thumb|centre|Schematic view of the Varicella Zoster Virus with glycoprotein spykes]] | ||
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Thomssona ''et al.'' (2011) generated this sequence for the development of next generation vaccines against Varicella Zoster Virus. Amino acids 1 – 539 were used to mimic the N-terminal domain which is located in the extracellular space. It exposes several linear as well as conformational B cell epitopes (Fowler ''et al.'', 2995). Therefore, is has been suggested as a vaccine component by Haumont ''et al.'' (1996). Besides its use for vaccination strategies, its antibody binding properties can be used for diagnostic applications. | Thomssona ''et al.'' (2011) generated this sequence for the development of next generation vaccines against Varicella Zoster Virus. Amino acids 1 – 539 were used to mimic the N-terminal domain which is located in the extracellular space. It exposes several linear as well as conformational B cell epitopes (Fowler ''et al.'', 2995). Therefore, is has been suggested as a vaccine component by Haumont ''et al.'' (1996). Besides its use for vaccination strategies, its antibody binding properties can be used for diagnostic applications. | ||
Revision as of 11:25, 3 September 2015
Glycoprotein E epitope derived from Varicella Zoster Virus
This part contains the coding sequence of the N-terminal part of glycoprotein E derived form Varicella Zoster Virus.
Thomssona et al. (2011) generated this sequence for the development of next generation vaccines against Varicella Zoster Virus. Amino acids 1 – 539 were used to mimic the N-terminal domain which is located in the extracellular space. It exposes several linear as well as conformational B cell epitopes (Fowler et al., 2995). Therefore, is has been suggested as a vaccine component by Haumont et al. (1996). Besides its use for vaccination strategies, its antibody binding properties can be used for diagnostic applications.
There are different types of epitopes included in this part. Some of the epitopes are linear, so recognition by an antibody depends only on the primary structure of the polypeptide. Regarding other epitopes, the glycosylation pattern is important for antibody binding. The part exhibits some N- and O-glycosylations, that cannot be added in a prokaryotic expression system. For this reason, the part’s sequence is optimized for expression in a mammalian cell line.
The part was added to the registry in the iGEM standard vector pSB1C3 beginning with a start codon (ATG). Cloning the part into the shipping backbone was performed by Gibson Assembly and the sequence was verified afterwards.