The peptide-binding and ATPase domains of recombinant hsc70 are required to interact with rotavirus and reduce its infectivity

Journal of Virology
Jimena Pérez-VargasCarlos F Arias

Abstract

The heat shock cognate protein hsc70 has been implicated as a postattachment cell receptor for rotaviruses. Here we show that hsc70 interacts specifically with rotaviruses through its peptide-binding domain, since a recombinant full-length hsc70 protein and its peptide-binding domain, but not its ATPase domain, bound triple-layered particles in a solid-phase assay, and known ligands of hsc70 competed this binding. The peptide ligands of hsc70 were also shown to block rotavirus infectivity when added to cells before virus infection, suggesting that hsc70 on the surface of MA104 cells also interacts with the virus through its peptide-binding domain and that this interaction is important for virus entry. When purified infectious virus was incubated with soluble hsc70 in the presence of the cochaperone hsp40 and ATP and then pelleted through a sucrose cushion, the recovered virus had lost 60% of its infectivity, even though hsc70 was not detected in the pellet fraction. The hsc70-treated virus showed slightly different reactivities with monoclonal antibodies and was more susceptible to heat and basic pHs than the untreated virus, suggesting that hsc70 induces a subtle conformational change in the virus that results in a reduction o...Continue Reading

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Citations

May 13, 2010·Archives of Virology·Allen XiaoHonglin Luo
Feb 24, 2010·Antimicrobial Agents and Chemotherapy·Yu-Ping WangJian-Dong Jiang
Nov 20, 2012·Virology Journal·Zhongqi BianZhaoxin Zheng
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May 14, 2016·World Journal of Virology·Carlos A Guerrero, Orlando Acosta
Mar 13, 2019·Cold Spring Harbor Perspectives in Biology·Ranen Aviner, Judith Frydman
Feb 8, 2007·The Journal of Biological Chemistry·Tijana IvanovicMax L Nibert
Aug 28, 2020·Frontiers in Microbiology·Zeng WangJianke Wang

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