Biophysical and Computational Studies of the vCCI:vMIP-II Complex.

ABSTRACT: Certain viruses have the ability to subvert the mammalian immune response, including interference in the chemokine system. Poxviruses produce the chemokine binding protein vCCI (viral CC chemokine inhibitor; also called 35K), which tightly binds to CC chemokines. To facilitate the study of vCCI, we first provide a protocol to produce folded vCCI from Escherichia coli (E. coli.) It is shown here that vCCI binds with unusually high affinity to viral Macrophage Inflammatory Protein-II (vMIP-II), a chemokine analog produced by the virus, human herpesvirus 8 (HHV-8). Fluorescence anisotropy was used to investigate the vCCI:vMIP-II complex and shows that vCCI binds to vMIP-II with a higher affinity than most other chemokines, having a K_d of 0.06 ± 0.006 nM. Nuclea

SUBMITTER: Nguyen AF 

PROVIDER: S-EPMC5578167 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature