2026-06-14T02:29:30Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/147692025-05-07T10:44:19Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609

00925njm 22002777a 4500 dc Yang, Jinsung author Park, Jeongsoo author Koehler, Melanie author Simpson, Joshua author Luque, Daniel author Rodríguez, Javier M author Alsteens, David author 2021 Rotavirus interactions with endogenous cell surface receptors are of fundamental interest in virology and medicine; however, the evidence of rotavirus directly binding to the receptors and the consequent dynamic behaviors are still elusive. Force–distance curve-based atomic force microscopy allows for the extraction of biophysical properties underlying binding of single virions to receptors and clarification of the dynamics of rotavirus–receptor interactions. Unfortunately, this method is time-consuming due to the lack of automation when analyzing large data sets. Herein, rotavirus–receptor interactions and early endocytosis behaviors using automated high-throughput analysis are examined. It is demonstrated that rotavirus binds to α-linked sialic acid and α2β1 integrin. The effect of trypsinization is investigated on the capsid protein VP4 binding to the receptors. Using fluidic force microscopy, it is demonstrated that the interaction leads to α2 integrin recruitment to the cell-bound rotavirus on the plasma membrane. Further, it is illustrated that an integrin-derived peptide can impede binding and alter downstream dynamics. Taken together, these results open a new understanding of the infection mechanism of rotavirus and suggest a novel inhibitory peptide against rotavirus binding. Adv. NanoBiomed Res. 2021;1(12):2100077. 10.1002/anbr.202100077 2699-9307 2699-9307 Advanced NanoBiomed Research http://hdl.handle.net/20.500.12105/14769 Rotavirus Binding to Cell Surface Receptors Directly Recruiting α2 Integrin