期刊文献+

RDD基序对口蹄疫Asia1型毒株感染力的影响 被引量:5

Infectivity of Asia1 type foot-and-mouth disease virus was increased via an alternative RDD motif
原文传递
导出
摘要 不同型口蹄疫病毒1D蛋白的βG和βH链之间都含有一个高度保守的RGD基序,其结合细胞受体,起始病毒感染.但本文通过对Asia1型FMDV的1D序列分析证实,田间毒株含有RGD和RDD基序(RGD中的G突变为D)的两种类型毒株.通过反向遗传技术制备了分别含有RGD和RDD基序的两种病毒,测定其生物学特性,并通过细胞感染力和乳鼠致病力比较这两种病毒感染力的差别.结果表明,含有RGD和RDD的毒株都具有感染性,含有RDD毒株的细胞感染力和乳鼠致病力比含RGD的高10倍左右,为进一步阐明RDD基序Asia1毒株的感染机制的分子基础奠定必要的基础. The amino acid sequence motif Arg-Gly-Asp (RGD), located in the surface-exposed βG-βH loop of the 1D protein of different serotypes and subtypes of foot-and-mouth disease virus (FMDV), is highly conserved and participates in binding of FMDV to susceptible cells. Previous sequence analyses of the 1D-encoding region of a FMDV serotype Asial field isolates from China indicated the presence of an alternative RDD motif instead of the conserved βG-βH loop RGD. The role of the RGD and RDD sequences in virus infection was investigated by recovering viruses with the βG-βH loop RGD (named rRGD-Asial) and a RDD tripeptide (named rRDD-Asial), respectively, using a genome-length infectious chimeric eDNA clone. The regults show that the infectivity of the rRDD-Asial virus for baby hamster kidney cells (BHK-21) and baby hamsters was higher as 10 times. These results also demonstrate that field isolates with RGD and an alternative RDD receptor recognition site have infectivity, and RDD motif can increase the infectivity of the viruses. The study lays a foundation for further study of the existence of other receptor molecules and alternative mechanisms for FMDV entry into cells.
出处 《科学通报》 EI CAS CSCD 北大核心 2010年第14期1370-1375,共6页 Chinese Science Bulletin
基金 国家重点基础研究发展计划(2005CB23201) 国家科技支撑计划(2006BAD06A03)资助项目
关键词 口蹄疫病毒 RGD 整联蛋白 细胞结合位点 反向遗传学 FMDV, RGD, integrin, cell binding site, reverse genetics
  • 相关文献

参考文献31

  • 1Grubman M J, Baxt B. Foot-and-mouth disease. Clin Microbiol Rev, 2004, 17:465-93.
  • 2Thomson G R, Bastos A D S. Foot-and-mouth disease. In: Coetzer J A W, Tustin R C, eds. Infectious Diseases of Livestock. Cape Town: Oxford University Press, 2004. 1323 1365.
  • 3Thomson G R, Vosloo W, Bastos A D. Foot and mouth disease in wildlife. Virus Res, 2003, 91:145 161.
  • 4Acharya R, Fry E, Stuart D, et al. The three-dimensional structure of foot-and-mouth disease virus at 2.9 A resolution. Nature, 1989, 337: 709--716.
  • 5Logan D, Abu-Ghazaleh R, Blakemore W, et al. Structure of a major immunogenic site on foot-and-mouth disease virus. Nature, 1993, 362:566--568.
  • 6Mateu M G, Camarero J A, Giralt E, et al. Direct evaluation of the immunodominance of a major antigenic site of foot-and-mouth disease virus in a natural host. Virology, 1995, 206:298--306.
  • 7D'Souza S E, Ginsberg M H, Plow E F. Arginyl-glycyl-aspartic acid (RGD): A cell adhesion motif. Trends Biochem Sci, 1991, 16: 246--250.
  • 8Fox G, Parry N R, Barnett P V, et al. The cell attachment site on foot-and-mouth disease virus includes the amino acid sequence RGD (arginine-glycine-aspartic acid). J Gen Virol, 1989, 70 : 625--637.
  • 9Mason P W, Rieder E, Baxt B. RGD sequence of foot-and-mouth disease virus is essential for infecting cells via the natural receptor but can be bypassed by an antibody-dependent enhancement pathway. Proc Natl Acad Sci USA, 1994, 91:1932--1936.
  • 10Berinstein A, Roivainen M, Hovi T, et al. Antibodies to the vitronectin receptor (integrin alpha V beta 3) inhibit binding and infection of foot-and-mouth disease virus to cultured cells. J Virol, 1995, 69:2664--2666.

同被引文献51

引证文献5

二级引证文献26

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部