TY  - JOUR
AU  - Caruso, Icaro P.
AU  - Guimarães, Giovana C.
AU  - Machado, Vitor B.
AU  - Fossey, Marcelo A.
AU  - Willbold, Dieter
AU  - Almeida, Fabio C. L.
AU  - Souza, Fátima P.
TI  - Biophysical and Dynamic Characterization of Fine-Tuned Binding of the Human Respiratory Syncytial Virus M2-1 Core Domain to Long RNAs
JO  - Journal of virology
VL  - 94
IS  - 23
SN  - 1098-5514
CY  - Baltimore, Md.
PB  - Soc.
M1  - FZJ-2021-00481
SP  -  e01505-20
PY  - 2020
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - 32938771
UR  - <Go to ISI:>//WOS:000595866900011
DO  - DOI:10.1128/JVI.01505-20
UR  - https://juser.fz-juelich.de/record/889873
ER  -