The Crystal Structure of the Fifth Scavenger Receptor Cysteine-Rich Domain of Porcine CD163 Reveals an Important Residue Involved in Porcine Reproductive and Respiratory Syndrome Virus Infection

• DOI: 10.1128/jvi.01897-16
• Publication Date: 2016-11-24T03:00:48Z
• Authors: Hongfang Ma; Longguang Jiang; Songlin Qiao; Yubao Zhi; Xin-Xin Chen; Yanyan Yang; Xiaojing Huang; Mingdong Huang; Rui Li; Gai-Ping Zhang
• Keywords: Scavenger Receptor; Arterivirus

Porcine reproductive and respiratory syndrome (PRRS) has become an economically critical factor in swine industry since its worldwide spread the 1990s. Infection by causative agent, PRRS virus (PRRSV), was proven to be mediated indispensable receptor, porcine CD163 (pCD163), fifth scavenger receptor cysteine-rich domain (SRCR5) is essential for infection. However, structural details specific residues of pCD163 SRCR5 involved infection have not been defined yet. In this study, we prepared recombinant Drosophila melanogaster Schneider 2 (S2) cells determined crystal structure at a high resolution 2.0 Å. This includes markedly long loop region shows special electrostatic potential, these are significantly different from those other members superfamily (SRCR-SF). Subsequently, carried out structure-based mutational studies identify that arginine residue position 561 (Arg561) important PRRSV Further, showed Arg561 probably takes effect on binding during invasion. Altogether current work provides first view SRCR domain, expands our knowledge invasion mechanism PRRSV, supports molecular basis prevention control virus.PRRS caused huge economic losses pig farming. The shown host cell surface receptors. One them, pCD163, especially indispensable, further demonstrated play significant role unknown. then site-directed based elucidate which important. Our only information time but also indicates lays foundation future applications PRRS.