@misc{10481/68346,
year = {2021},
month = {4},
url = {http://hdl.handle.net/10481/68346},
abstract = {Viruses interact extensively with the host molecular machinery, but the underlying
mechanisms are poorly understood. Bacteriophage T7 recruits the small protein
thioredoxin of the Escherichia coli host as an essential processivity factor for
the viral DNA polymerase. We challenged the phage to propagate in a host in
which thioredoxin had been extensively modified to hamper its recruitment.
The virus adapted to the engineered host without losing the capability to propagate
in the original host, but no genetic mutations were fixed in the thioredoxin
binding domain of the viral DNA polymerase. Virus adaptation correlated with
mutations in the viral RNA polymerase, supporting that promiscuous thioredoxin
recruitmentwas enabled by phenotypicmutations caused by transcription errors.
These results point to a mechanism of virus adaptation that may play a role in
cross-species transmission.We propose that phenotypicmutations may generally
contribute to the capability of viruses to evade antiviral strategies},
organization = {Spanish Ministry of Economy and Competitiveness/FEDER Funds Grant
RTI2018-097142-B-100},
organization = {Human Frontier Science Program Grant RGP0041/2017},
publisher = {Elsevier},
title = {Evidence for a role of phenotypic mutations in virus adaptation},
doi = {10.1016/j.isci.2021.102257},
author = {Luzón Hidalgo, Raquel and Risso, Valeria Alejandra and Delgado Delgado, Asunción and Andrés-León, Eduardo and Ibarra Molero, Beatriz and Sánchez Ruiz, José Manuel},
}