Figure 9From: Identification of two distinct structural regions in a human porcine endogenous retrovirus receptor, HuPAR2, contributing to function for viral entryLocation of HuPAR2 residues and regions that determine HuPAR2 function identified to date. HuPAR2 (no shading) has two regions involved in its function as a PERV-A receptor. The first N-terminal 135 amino acids contain the absolute requirements for viral receptor function. The role of L109 (open white diamond) as a determinant of PERV-A SU binding was confirmed. Residues T5, D40, P73, Q82, H110, L119 and T127 (black circles), identified by MuPAR/HuPAR2 chimeras, contribute to the efficiency of HuPAR2 function and are found in multiple structural elements. The second region (a.a. 152–285), identified by HuPAR1/HuPAR2 chimeras, determines the enhanced efficiency of HuPAR2 function for PERV-A infection. This region spans the third extracellular loop, sixth transmembrane domain, third intracellular loop and seventh transmembrane domain.Back to article page