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Molecular dynamics of the α-helical epitope of a novel synthetic lipopeptide foot-and-mouth disease virus vaccine

✍ Scribed by Michael Krug; Gerd Folkers; Bernd Haas; Günter Hess; Karl-Heinz Wiesmüller; Stefan Freund; Günther Jung

Publisher: Wiley (John Wiley & Sons)
Year: 1989
Tongue: English
Weight: 727 KB
Volume: 28
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360280144

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✦ Synopsis

Institut fiir Organische Cheemie, Unioersittit Tiibingen, 0-7400 !lXbingen, Fedend Republic of Germmy synopsis A novel synthetic foot-and-mouth diseaee virua (FMDV) peptide vaccine Coneisting of a aynthetic B-cell and macrophage activator covalently linked to an amphiphilic a-helical T -d epitope waa developed. The low molecular weight vaccine of 3400 daltons is compoeed of virus VP1 antigenic detaminant and the immunologically active lipotripeptide tripalmitoyl-S glycayl-cyst&yl-smylgerine (p,csS) ae built-in adjuvant. The vaccine, tripalmitoyl43-glyceryIhomologous Challenge and aaotypespecific virus neutralizing antibodiee in guinea pigs after single adminiahtion without further adjuvants or cnrriera A P3CSS conjugate with the FMDVchallenge with 0 , K virus. The antigenic determinant VPl(135-154) ie an amphiphilic a-helix, aa ahown by CD. Molecular dynamics simulatione (MDS) carried out using the highly homologous a-helical alcohol dehydm g e n e (ADH) segment H3 as starting conformation for VPl(138-149) suggest that the FMDV segment 138-149 may adopt a-helical conformation during binding to its T-cell receptor, and that the development of the systan during MDS may be considered aa the dissodation step of the complex. ~t e i n y l ~l ~l -F M D V -V P l (VP1-OIK 136-154) induces pr~tection VPl8egmelt 135-154 of atrain 0 wuppertal produced only poor croskprotection against

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