Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 402378
Title Characterization of foot- and mouth disease virus antigen by surface-enhanced laser desorption ionization-time of flight-mass spectrometry in aqueous and oil-emulsion formulations
Author(s) Harmsen, M.M.; Jansen, J.; Westra, D.F.; Coco-Martin, J.M.
Source Vaccine 28 (2010)19. - ISSN 0264-410X - p. 3363 - 3370.
Department(s) CVI Virology
ASG ProductenProducten
Publication type Refereed Article in a scientific journal
Publication year 2010
Keyword(s) domain antibody fragments - aluminum salt adjuvants - international bank - stability - vaccine - protein - adsorption
Abstract We have used a novel method, surface-enhanced laser desorption ionization-time of flight-mass spectrometry (SELDI-TOF-MS), to characterize foot-and-mouth disease virus (FMDV) vaccine antigens. Using specific capture with FMDV binding recombinant antibody fragments and tryptic digestion of FMDV antigens the spectral peaks representing the FMDV structural proteins VP1, VP2, VP3 and VP4 were identified. VP1 existed as 2 variants differing by 0.2 kDa and VP4 as 8 variants differing by 14–17 Da. Such heterogeneities have not been reported earlier. They could represent oxidation of VP4 and N-glycation of VP1. We also detected FMDV proteolysis upon incubation at elevated temperatures and impurities in FMDV antigen preparations. Finally, we could also characterize FMDV antigen present in emulsions with oil adjuvant by SELDI-TOF-MS. Such FMDV antigen retained the VP4 protein which is known to be specifically present in intact (146S) FMDV particles but absent from specific (12S) degradation products. This indicates that virions do not dissociate upon emulsification
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