Home > Publications database > Biophysical and Dynamic Characterization of Fine-Tuned Binding of the Human Respiratory Syncytial Virus M2-1 Core Domain to Long RNAs > print

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024 7 _ |a 10.1128/JVI.01505-20
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100 1 _ |a Caruso, Icaro P.
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245 _ _ |a Biophysical and Dynamic Characterization of Fine-Tuned Binding of the Human Respiratory Syncytial Virus M2-1 Core Domain to Long RNAs
260 _ _ |a Baltimore, Md.
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520 _ _ |a The human respiratory syncytial virus (hRSV) M2-1 protein functions as a processivity and antitermination factor of the viral polymerase complex. Here, the first evidence that the hRSV M2-1 core domain (cdM2-1) alone has an unfolding activity for long RNAs is presented and the biophysical and dynamic characterization of the cdM2-1/RNA complex is provided. The main contact region of cdM2-1 with RNA was the α1-α2-α5-α6 helix bundle, which suffered local conformational changes and promoted the RNA unfolding activity. This activity may be triggered by base-pairing recognition. RNA molecules wrap around the whole cdM2-1, protruding their termini over the domain. The α2-α3 and α3-α4 loops of cdM2-1 were marked by an increase in picosecond internal motions upon RNA binding, even though they are not directly involved in the interaction. The results revealed that the cdM2-1/RNA complex originates from a fine-tuned binding, contributing to the unraveling interaction aspects necessary for M2-1 activity.
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700 1 _ |a Guimarães, Giovana C.
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700 1 _ |a Machado, Vitor B.
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700 1 _ |a Fossey, Marcelo A.
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700 1 _ |a Willbold, Dieter
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700 1 _ |a Almeida, Fabio C. L.
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700 1 _ |a Souza, Fátima P.
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773 _ _ |a 10.1128/JVI.01505-20
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856 4 _ |y Published on 2020-11-09. Available in OpenAccess from 2021-05-09.
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856 4 _ |u https://juser.fz-juelich.de/record/889873/files/JVI.01505-20.pdf
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