CORRELATIONS BETWEEN THE CONFORMATIONS ELUCIDATED BY CD SPECTROSCOPY AND THE ANTIGENIC PROPERTIES OF 4 PEPTIDES OF THE FOOT-AND-MOUTH-DISEASE VIRUS

被引：33

作者：

SILIGARDI, G

DRAKE, AF

MASCAGNI, P

ROWLANDS, D

BROWN, F

GIBBONS, WA

机构：

[1] UNIV LONDON BIRKBECK COLL,DEPT CHEM,20 GORDON ST,LONDON WC1H 0AJ,ENGLAND

[2] UNIV LONDON,DEPT PHARMACEUT CHEM,LONDON,ENGLAND

[3] WELLCOME BIOTECH LTD,DEPT VIROL,BECKENHAM,KENT,ENGLAND

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1991年 / 199卷 / 03期

基金：

英国惠康基金;

关键词：

D O I：

10.1111/j.1432-1033.1991.tb16153.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The conformational features of four related antigenic peptides (A, B, C and USA) from the foot-and-mouth disease virus (FMDV) (VP1; 141 - 160 of serotype A, subtype 12), assessed by CD, were found to correlate with the serological properties of these peptides. The CD spectra of the four peptides, obtained under cryogenic and solvent titration conditions, were consistent with three conformational components (a left-handed extended helix, an alpha-helix and a 3(10) helix) for peptides A and C and four components (a beta-turn of type II, an alpha-helix, a gamma-turn and a 3(10) helix) for peptides B and USA. The amino acid substitutions at positions 148 and 153, which distinguish the peptides, are therefore responsible for both their conformational and antigenic differences.

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页码：545 / 551

页数：7

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