8ZE6

Crystal structure of MjHKU4r-CoV-1 RBD bound to MjDPP4

Summary for 8ZE6

• Entry DOI: 10.2210/pdb8ze6/pdb
• Descriptor: Dipeptidyl peptidase 4, Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: virus protein and receptor complex, viral protein
• Biological source: Manis javanica; More
• Total number of polymer chains: 4
• Total formula weight: 217568.40

Authors

Yang, M.,Li, Z.,Xu, Y.,Zhang, S. (deposition date: 2024-05-04, release date: 2024-10-30, Last modification date: 2025-05-14)

Primary citation

Yang, M.,Li, Z.,Chen, J.,Li, Y.,Xu, R.,Wang, M.,Xu, Y.,Chen, R.,Ji, W.,Li, X.,Wei, J.,Zhou, Z.,Ren, M.,Ma, K.,Guan, J.,Mo, G.,Zhou, P.,Shu, B.,Guo, J.,Yuan, Y.,Shi, Z.L.,Zhang, S.
Structural basis for human DPP4 receptor recognition by a pangolin MERS-like coronavirus.
Plos Pathog., 20:e1012695-e1012695, 2024

PubMed Abstract: Middle East respiratory syndrome coronavirus (MERS-CoV) and the pangolin MERS-like coronavirus MjHKU4r-CoV-1 employ dipeptidyl peptidase 4 (DPP4) as an entry receptor. MjHKU4r-CoV-1 could infect transgenic mice expressing human DPP4. To understand the mechanism of MjHKU4r-CoV-1 entry into cells, we determined the crystal structures of the receptor binding domain (RBD) of MjHKU4r-CoV-1 spike protein bound to human DPP4 (hDPP4) and Malayan pangolin DPP4 (MjDPP4), respectively. The overall hDPP4-binding mode of MjHKU4r-CoV-1 RBD is similar to that of MERS-CoV RBD. MjHKU4r-CoV-1 RBD shows higher binding affinity to hDPP4 compared to the bat MERS-like coronavirus Ty-BatCoV-HKU4. Via swapping residues between MjHKU4r-CoV-1 RBD and Ty-BatCoV-HKU4 RBD, we identified critical determinants on MjHKU4r-CoV-1 that are responsible for virus usage of hDPP4. Our study suggests that MjHKU4r-CoV-1 is more adapted to the human receptor compared to the bat HKU4 coronavirus and highlights the potential of virus emergence into the human population.

PubMed: 39514585
DOI: 10.1371/journal.ppat.1012695

Experimental method

X-RAY DIFFRACTION (2.7 Å)