RT info:eu-repo/semantics/article
T1 A Single Amino Acid Substitution in the Novel H7N9 Influenza A Virus NS1 Protein Increases CPSF30 Binding and Virulence
A1 Ayllón Barasoain, Juan
A1 Domingues, Patricia
A1 Rajsbaum, Ricardo
A1 Miorin, Lisa
A1 Schmolke, Mirco
A1 Hale, Benjamin G.
A1 García Sastre, Adolfo
K1 Medicina
K1 Medicine
K1 Microbiología
K1 Microbiology
K1 Salud
K1 Health
K1 Enfermedades infecciosas
K1 Communicable diseases
AB Although an effective interferon antagonist in human and avian cells, the novel H7N9 influenza virus NS1 protein is defective at inhibiting CPSF30. An I106M substitution in H7N9 NS1 can restore CPSF30 binding together with the ability to block host gene expression. Furthermore, a recombinant virus expressing H7N9 NS1-I106M replicates to higher titers in vivo, and is subtly more virulent, than the parental virus. Natural polymorphisms in H7N9 NS1 that enhance CPSF30 binding may be cause for concern.
PB American Society for Microbiology
SN 0022-538X
YR 2014
FD 2014
LK http://hdl.handle.net/10259/7995
UL http://hdl.handle.net/10259/7995
LA eng
NO This work was partially supported by U.S. NIH funding to A.G.-S. (under grants R01AI046954 and U19AI083025 and CRIP [Center for Research on Influenza Pathogenesis, an NIAID Center of Excellence for Influenza Research and Surveillance {CEIRS}] contract HHSN266200700010C) and funding from the Medical Research Council, United Kingdom, and the European Commission (FP7 Marie Curie CIG 321703: UBIFLU) (both to B.G.H.). B.G.H. is a Sir Henry Dale Fellow jointly funded by the Wellcome Trust and the Royal Society (grant number 100034/Z/12/Z).
DS Repositorio Institucional de la Universidad de Burgos
RD 11-may-2024