Cryo-EM structure of human rhinovirus 14 in complex with its receptor ICAM-1
Human rhinovirus 14 (HRV14) belongs to the major group of human rhinoviruses, which utilize intercellular adhesion molecule 1 (ICAM-1) as their receptor. It was shown before that the binding site for ICAM-1 is located at so called ‘canyon’ region of the HRV14 in a vicinity of the five-fold symmetry axis. However, precise binding interface between HRV14 and ICAM-1 is not known. Here we present cryo-EM structure of HRV14-ICAM-1 complex at 2.8 Å resolution. We show that the interaction causes conformational changes in BC and FG loops of D1 domain of ICAM-1 and loop 151-161 in VP1 of HRV14. We describe extensive ionic and hydrogen bonds between the virus and the receptor. This information will provide a guide for development of small molecule inhibitors interfering with the cell entry of HRV14. Blocking of attachment of virus to its receptor is in scope of many drug development trials since it disrupts the viral life cycle in its very beginning.