STRUCTURE OF A MAJOR IMMUNOGENIC SITE ON FOOT-AND-MOUTH-DISEASE VIRUS

被引:320
作者
LOGAN, D
ABUGHAZALEH, R
BLAKEMORE, W
CURRY, S
JACKSON, T
KING, A
LEA, S
LEWIS, R
NEWMAN, J
PARRY, N
ROWLANDS, D
STUART, D
FRY, E
机构
[1] UNIV OXFORD,MOLEC BIOPHYS LAB,REX RICHARDS BLDG,OXFORD OX1 3QU,ENGLAND
[2] AFRC,INST ANIM HLTH,WOKING GU24 0NF,ENGLAND
[3] WELLCOME RES LABS,DEPT MOLEC SCI,BECKENHAM BR3 3BS,KENT,ENGLAND
关键词
D O I
10.1038/362566a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
ATTACHMENT of foot-and-mouth disease virus (FMDV) to its cellular receptor involves a long and highly antigenic loop containing the conserved sequence, Arg-Gly-Asp, a motif known to be a recognition element in many integrin-dependent cell adhesion processes1-7. In our original crystal structure of FMDV the Arg-Gly-Asp-containing loop ('the loop'), located between beta-strands G and H of capsid protein VP1, was disordered and hence essentially invisible. We previously surmised that its disorder is enhanced by a disulphide bond linking the base of the loop (Cys 134) to Cys 130 of VP2 (ref. 8). We report here the crystal structure of the virus in which this disulphide is reduced. Reduced virus retains infectivity and serological experiments suggest that some of the loop's internal structure is conserved8. But here its structure has become sufficiently ordered to allow us to describe an unambiguous conformation, which we relate to some key biological properties of the virus.
引用
收藏
页码:566 / 568
页数:3
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