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

被引:10
作者
Harmsen, M. M. [1 ,2 ]
Jansen, J. [1 ]
Westra, D. F. [1 ]
Coco-Martin, J. M. [1 ]
机构
[1] Lelystad Biol BV, NL-8200 AK Lelystad, Netherlands
[2] Cent Vet Inst Wageningen UR, NL-8200 AB Lelystad, Netherlands
关键词
Foot-and-mouth disease; Single-domain antibody; SELDI-TOF-MS; Mass spectrometry; DOMAIN ANTIBODY FRAGMENTS; ALUMINUM SALT ADJUVANTS; INTERNATIONAL BANK; STABILITY; VACCINE; PROTEIN; ADSORPTION;
D O I
10.1016/j.vaccine.2010.02.084
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
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 02 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. (C) 2010 Elsevier Ltd All rights reserved
引用
收藏
页码:3363 / 3370
页数:8
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