2026-06-14T03:54:56Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/147692025-05-07T10:44:19Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609
Repisalud
author
Yang, Jinsung
author
Park, Jeongsoo
author
Koehler, Melanie
author
Simpson, Joshua
author
Luque, Daniel
author
Rodríguez, Javier M
author
Alsteens, David
funder
Unión Europea. Comisión Europea. H2020
funder
Katholieke Universiteit Leuven (Bélgica)
funder
Unión Europea. Comisión Europea. European Research Council (ERC)
funder
Ministerio de Economía y Competitividad (España)
funder
Instituto de Salud Carlos III
funder
Unión Europea. Comisión Europea. H2020
funder
National Fund for Research (Francia)
2022-07-21T08:56:53Z
2022-07-21T08:56:53Z
2021
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 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.
eng
Rotavirus Binding to Cell Surface Receptors Directly Recruiting α2 Integrin
research article
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URL
https://repisalud.isciii.es/bitstreams/bdaafe47-aed9-4288-87c2-ead181c56428/download
File
MD5
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application/pdf
RotavirusBindingToCell_2021.pdf
URL
https://repisalud.isciii.es/bitstreams/0cf9b59b-a88f-4dbc-a93e-6b81c1806988/download
File
MD5
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text/plain
RotavirusBindingToCell_2021.pdf.txt