Interaction of influenza A virus NS2/NEP protein with the amino-terminal part of Nup214

Autor: Kadir Turan, Atsushi Kawaguchi, Burçak Şenbaş Akyazi, Kyosuke Nagata, Ayşegül Pirinçal
Přispěvatelé: Senbas Akyazi, Burcak, Pirincal, Aysegul, Kawaguchi, Atsushi, Nagata, Kyosuke, Turan, Kadir
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Nup214
Physiology
viruses
0206 medical engineering
NUCLEAR-PORE COMPLEX
02 engineering and technology
Biology
medicine.disease_cause
Microbiology
Article
03 medical and health sciences
Influenza A viruses
NS2/NEP
Nup214
nuclear pore complex
nuclear export

0302 clinical medicine
DOMAIN
nuclear pore complex
Genetics
Influenza A virus
medicine
Nuclear pore
Nuclear export signal
Molecular Biology
Nucleoporin 214
M1 PROTEIN
Influenza A viruses
FUNCTIONAL-ANALYSIS
IMPORT
NUCLEOCYTOPLASMIC TRANSPORT
POLYMERASE
virus diseases
RNA
Cell Biology
biochemical phenomena
metabolism
and nutrition

020601 biomedical engineering
Cell biology
Nucleoprotein
Viral replication
030220 oncology & carcinogenesis
Nucleoporin
nuclear export
OVEREXPRESSION
NUCLEOPORIN NUP214
EXPORT PROTEIN
General Agricultural and Biological Sciences
NS2/NEP
Zdroj: Volume: 44, Issue: 2 82-92
Turkish Journal of Biology
ISSN: 1300-0152
1303-6092
Popis: Influenza A viruses have a single-stranded RNA genome consisting of 8 segments. Each RNA segment associates with the nucleoprotein NP and viral RNA polymerase to and from a viral ribonucleoprotein vRNP particle. The viral mRNA synthesis is dependent on a capped primer derived from nascent host RNA transcripts. For these processes to take place, vRNPs must pass through the cell nuclear pore complex NPC to the nucleus. The influenza A virus NS2 protein, also called the nuclear export protein NES , has an important role in the nucleocytoplasmic transport of vRNPs. This protein interacts with the host cellular nucleoporins during the nuclear export of vRNPs. In this study, the human nucleoporin 214 Nup214 was identified as an NS2-binding protein by using a yeast two-hybrid assay. The interaction between NS2 and human Nup214 was confirmed in both yeast and mammalian cells. It has been shown that the NS2 protein interacts with the amino terminal FG domain of the Nup214 protein. The influenza viral replication was suppressed in knockdown cells for the Nup214 protein. It was concluded that the FG domains of nucleoporins have an important role in the interaction of the influenza NS2 protein with host NPC for vRNA export.
Databáze: OpenAIRE