CCR2 and CCR5 receptor‐binding properties of herpesvirus‐8 vMIP‐II based on sequence analysis and its solution structure

摘要: Human herpesvirus-8 (HHV-8) is the infectious agent responsible for Kaposi’s sarcoma and encodes a protein, macrophage inflammatory protein-II (vMIP-II), which shows sequence similarity to human CC chemokines. vMIP-II has broad receptor specificity that crosses chemokine subfamilies, inhibits HIV-1 viral entry mediated by numerous receptors. In this study, solution structure of chemically synthesized was determined nuclear magnetic resonance. The protein monomer possesses fold consisting flexible N-terminus, three antiparallel β strands, C-terminal α helix. Except N-terminal residues (residues 1–13) last two 73–74), well-defined, exhibiting average rmsd 0.35 0.90 A backbone heavy atoms all 14–72, respectively. Taking into account differences between various chemokines comparing their three-dimensional structures allows us implicate influence quaternary binding activation these proteins in solution. analysis indicates presence epitopes involved receptors CCR2 CCR5. We propose initially specific CCR5 acquired receptor-binding properties other