Sequence alignment and in silico protein structure prediction of the receptor-binding domain (RBD) from human and other primate erythroparvoviruses (simian, rhesus, and pig-tailed) revealed a similar structure characterized by a fold of three or four α-helices.
Functional studies confirmed the presence of a conserved RBD mediating virus entry in human erythroid cells. The presence of an analogous RBD in non-human primate erythroparvoviruses emphasizes their parallel evolutionary trait and zoonotic potential.

This work was carried out in the group of PD Dr. Carlos Ros.

References:

• C. Bircher, J. Bieri, R. Assaraf, R. Leisi, C. Ros;
  "A Conserved Receptor-Binding Domain in the VP1u of Primate Erythroparvoviruses Determines the Marked Tropism for Erythroid Cells"
  Viruses, 2022, 14(2), 420/1-16; doi:10.3390/v14020420.