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Virologica Sinica, 18 (5) : 446-450, 2003
Research Article
Expression,Purification and Biological Activity Study of Viral Chemokine VM IP2
1 中国科学院武汉病毒研究所,湖北武汉,43007l:2.武汉市疾病预防控制中心,湖北武汉,430000
 Correspondence:
(247.46KB)  
Abstract
Abstract:ChemokiRe receptor CCR5 and CXCR4 are principal coreceptors for HIV Blockage of
Human immunodeficiecy virus(HIV)infection can be achieved by engaging CCR5 and CXCR4 with their
natural ligands. man herpesvirus 8 encodes three chemokines: vM IP1.vMIP2 and vM IP3.vM Ⅱ’2
has been shown to bind a range of receptors including CCR5 and CXCR4.In this study,we report the
expression and purification of recombinant vM IP2 from Escherichia coli.vM IP2 gene was cloned into
pET-32a(+)expression vector,which allows production of the desired protein along with a thioredoxin
fusion tag.The vector containing the sequence encoding the mature form of vM IP2 was transform ed
into AD494(DE3).After induction.TrxA—VMIP2 fusion protein was purified using Ni chelating column.
Cleavage of the thioredoxin fusion tag was subsequently carried out with enterokinase.The cleaved
protein was further purified by cation exchange column.W estern blotting indicated that purified V~皿2
had specific immunological activity with vM IP2 antibody./n vitro infection demonstrated that vM Ⅱ’2
potently inhibited the replication of R5 and X4 HIV in human peripheral blood mononuclear cell
(PBMC).This study provides basis for development of efective prevention strategies against HIV
Further investigation may help to define the role of vM IP2 ifl HHV8 pathogenesis.
  Published online: 5 Oct 2003
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