Molecular recognition of a host protein by NS1 of pandemic and seasonal influenza A viruses.
Class Ia Phosphatidylinositol 3-Kinase
/ metabolism
Host-Pathogen Interactions
Humans
Influenza A Virus, H1N1 Subtype
/ pathogenicity
Influenza A Virus, H3N2 Subtype
/ pathogenicity
Influenza A virus
/ classification
Influenza, Human
/ epidemiology
Protein Binding
Protein Conformation
Protein Interaction Domains and Motifs
Species Specificity
Structure-Activity Relationship
Viral Nonstructural Proteins
/ chemistry
Virulence Factors
/ chemistry
conformational dynamics
influenza virus
nonstructural protein 1
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
24 03 2020
24 03 2020
Historique:
pubmed:
11
3
2020
medline:
11
8
2020
entrez:
11
3
2020
Statut:
ppublish
Résumé
The 1918 influenza A virus (IAV) caused the most severe flu pandemic in recorded human history. Nonstructural protein 1 (NS1) is an important virulence factor of the 1918 IAV. NS1 antagonizes host defense mechanisms through interactions with multiple host factors. One pathway by which NS1 increases virulence is through the activation of phosphoinositide 3-kinase (PI3K) by binding to its p85β subunit. Here we present the mechanism underlying the molecular recognition of the p85β subunit by 1918 NS1. Using X-ray crystallography, we determine the structure of 1918 NS1 complexed with p85β of human PI3K. We find that the 1918 NS1 effector domain (1918 NS1
Identifiants
pubmed: 32152123
pii: 1920582117
doi: 10.1073/pnas.1920582117
pmc: PMC7104383
doi:
Substances chimiques
INS1 protein, influenza virus
0
Viral Nonstructural Proteins
0
Virulence Factors
0
Class Ia Phosphatidylinositol 3-Kinase
EC 2.7.1.137
Banques de données
PDB
['6U28', '6OX7']
Types de publication
Comparative Study
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
6550-6558Subventions
Organisme : NIGMS NIH HHS
ID : P41 GM111244
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM127723
Pays : United States
Organisme : NIH HHS
ID : S10 OD012331
Pays : United States
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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