5JFB

Crystal structure of the scavenger receptor cysteine-rich domain 5 (SRCR5) from porcine CD163

Summary for 5JFB

• Entry DOI: 10.2210/pdb5jfb/pdb
• Descriptor: Scavenger receptor cysteine-rich type 1 protein M130 (2 entities in total)
• Functional Keywords: cd163, srcr, prrsv, endocytosis
• Biological source: Sus scrofa (Pig)
• Cellular location: Soluble CD163: Secreted . Cell membrane ; Single-pass type I membrane protein : Q2VL90
• Total number of polymer chains: 1
• Total formula weight: 12083.34

Authors

Ma, H.,Jiang, L.,Qiao, S.,Zhang, G.,Li, R. (deposition date: 2016-04-19, release date: 2017-03-22, Last modification date: 2024-11-06)

Primary citation

Ma, H.,Jiang, L.,Qiao, S.,Zhi, Y.,Chen, X.X.,Yang, Y.,Huang, X.,Huang, M.,Li, R.,Zhang, G.P.
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
J. Virol., 91:-, 2017

PubMed Abstract: Porcine reproductive and respiratory syndrome (PRRS) has become an economically critical factor in swine industry since its worldwide spread in the 1990s. Infection by its causative agent, PRRS virus (PRRSV), was proven to be mediated by an indispensable receptor, porcine CD163 (pCD163), and the fifth scavenger receptor cysteine-rich domain (SRCR5) is essential for virus infection. However, the structural details and specific residues of pCD163 SRCR5 involved in infection have not been defined yet. In this study, we prepared recombinant pCD163 SRCR5 in Drosophila melanogaster Schneider 2 (S2) cells and determined its crystal structure at a high resolution of 2.0 Å. This structure includes a markedly long loop region and shows a special electrostatic potential, and these are significantly different from those of other members of the scavenger receptor cysteine-rich superfamily (SRCR-SF). Subsequently, we carried out structure-based mutational studies to identify that the arginine residue at position 561 (Arg561) in the long loop region is important for PRRSV infection. Further, we showed Arg561 probably takes effect on the binding of pCD163 to PRRSV during virus invasion. Altogether the current work provides the first view of the CD163 SRCR domain, expands our knowledge of the invasion mechanism of PRRSV, and supports a molecular basis for prevention and control of the virus.

PubMed: 27881657
DOI: 10.1128/JVI.01897-16

Experimental method

X-RAY DIFFRACTION (2 Å)