6K0L

The crystal structure of simian CD163 SRCR5

Summary for 6K0L

• Entry DOI: 10.2210/pdb6k0l/pdb
• Descriptor: Scavenger receptor cysteine-rich type 1 protein M130 (2 entities in total)
• Functional Keywords: scavenger receptor, scavenger receptor cysteine-rich domain, porcine reproductive and respiratory syndrome virus, endocytosis
• Biological source: Chlorocebus aethiops (Green monkey)
• Total number of polymer chains: 2
• Total formula weight: 22789.39

Authors

Ma, H.,Li, R.,Jiang, L.,Qiao, S.,Zhang, G. (deposition date: 2019-05-07, release date: 2020-05-13, Last modification date: 2023-11-22)

Primary citation

Ma, H.,Li, R.,Jiang, L.,Qiao, S.,Chen, X.X.,Wang, A.,Zhang, G.
Structural comparison of CD163 SRCR5 from different species sheds some light on its involvement in porcine reproductive and respiratory syndrome virus-2 infection in vitro.
Vet Res, 52:97-97, 2021

PubMed Abstract: Porcine reproductive and respiratory syndrome (PRRS) is a serious disease burdening global swine industry. Infection by its etiological agent, PRRS virus (PRRSV), shows a highly restricted tropism of host cells and has been demonstrated to be mediated by an essential scavenger receptor (SR) CD163. CD163 fifth SR cysteine-rich domain (SRCR5) is further proven to play a crucial role during viral infection. Despite intense research, the involvement of CD163 SRCR5 in PRRSV infection remains to be elucidated. In the current study, we prepared recombinant monkey CD163 (moCD163) SRCR5 and human CD163-like homolog (hCD163L1) SRCR8, and determined their crystal structures. After comparison with the previously reported crystal structure of porcine CD163 (pCD163) SRCR5, these structures showed almost identical structural folds but significantly different surface electrostatic potentials. Based on these differences, we carried out mutational research to identify that the charged residue at position 534 in association with the one at position 561 were important for PRRSV-2 infection in vitro. Altogether the current work sheds some light on CD163-mediated PRRSV-2 infection and deepens our understanding of the viral pathogenesis, which will provide clues for prevention and control of PRRS.

PubMed: 34193250
DOI: 10.1186/s13567-021-00969-z

Experimental method

X-RAY DIFFRACTION (1.58 Å)