Crystallization of a nonreplicating rotavirus vaccine candidate.

Hong, MS; Kaur, K; Sawant, N; Joshi, SB; Volkin, DB; Braatz, RD

Crystallization of a nonreplicating rotavirus vaccine candidate.

Hong, MS Kaur, K Sawant, N Joshi, SB Volkin, DB Braatz, RD

Permalink

Publisher:: WILEY
Publication Type:: Journal Article
Citation:: Biotechnol Bioeng, 2021, 118, (4), pp. 1750-1756
Issue Date:: 2021-04

Open Access

Copyright Clearance Process

Recently Added
In Progress
Open Access

This item is open access.

Adobe PDF

Download Published versionAdobe PDF (1.08 MB)

View on publisher's site

View statistics

Full metadata record

Field	Value	Language
dc.contributor.author	Hong, MS
dc.contributor.author	Kaur, K
dc.contributor.author	Sawant, N
dc.contributor.author	Joshi, SB
dc.contributor.author	Volkin, DB
dc.contributor.author	Braatz, RD
dc.date.accessioned	2022-04-10T20:10:41Z
dc.date.available	2021-01-19
dc.date.available	2022-04-10T20:10:41Z
dc.date.issued	2021-04
dc.identifier.citation	Biotechnol Bioeng, 2021, 118, (4), pp. 1750-1756
dc.identifier.issn	0006-3592
dc.identifier.issn	1097-0290
dc.identifier.uri	http://hdl.handle.net/10453/156035
dc.description.abstract	Nonreplicating rotavirus vaccine (NRRV) candidates are being developed with the aim of serving the needs of developing countries. A significant proportion of the cost of manufacturing such vaccines is the purification in multiple chromatography steps. Crystallization has the potential to reduce purification costs and provide new product storage modality, improved operational flexibility, and reduced facility footprints. This communication describes a systematic approach for the design of the crystallization of an NRRV candidate, VP8 subunit proteins fused to the P2 epitope of tetanus toxin, using first-principles models and preliminary experimental data. The first-principles models are applied to literature data to obtain feasible crystallization conditions and lower bounds for nucleation and growth rates. Crystallization is then performed in a hanging-drop vapor diffusion system, resulting in the nucleation and growth of NRRV crystals. The crystals obtained in a scaled-up evaporative crystallization contain proteins truncated in the P2 region, but have no significant differences with the original samples in terms of antibody binding and overall conformational stability. These results demonstrate the promise of evaporative crystallization of the NRRV.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	WILEY
dc.relation.ispartof	Biotechnol Bioeng
dc.relation.isbasedon	10.1002/bit.27699
dc.rights	info:eu-repo/semantics/openAccess
dc.subject.classification	Biotechnology
dc.subject.mesh	Crystallization
dc.subject.mesh	Rotavirus
dc.subject.mesh	Rotavirus Vaccines
dc.subject.mesh	Rotavirus
dc.subject.mesh	Rotavirus Vaccines
dc.subject.mesh	Crystallization
dc.title	Crystallization of a nonreplicating rotavirus vaccine candidate.
dc.type	Journal Article
utslib.citation.volume	118
utslib.location.activity	United States
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology/School of Computer Science
utslib.copyright.status	open_access	*
dc.date.updated	2022-04-10T20:10:37Z
pubs.issue	4
pubs.publication-status	Published
pubs.volume	118
utslib.citation.issue	4

Abstract:

Nonreplicating rotavirus vaccine (NRRV) candidates are being developed with the aim of serving the needs of developing countries. A significant proportion of the cost of manufacturing such vaccines is the purification in multiple chromatography steps. Crystallization has the potential to reduce purification costs and provide new product storage modality, improved operational flexibility, and reduced facility footprints. This communication describes a systematic approach for the design of the crystallization of an NRRV candidate, VP8 subunit proteins fused to the P2 epitope of tetanus toxin, using first-principles models and preliminary experimental data. The first-principles models are applied to literature data to obtain feasible crystallization conditions and lower bounds for nucleation and growth rates. Crystallization is then performed in a hanging-drop vapor diffusion system, resulting in the nucleation and growth of NRRV crystals. The crystals obtained in a scaled-up evaporative crystallization contain proteins truncated in the P2 region, but have no significant differences with the original samples in terms of antibody binding and overall conformational stability. These results demonstrate the promise of evaporative crystallization of the NRRV.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/156035