The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus.
Identifieur interne : 001F91 ( Ncbi/Checkpoint ); précédent : 001F90; suivant : 001F92The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus.
Auteurs : Qingliang Shen [États-Unis] ; Jae-Hyun Cho [États-Unis]Source :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Mutant Proteins, Viral Nonstructural Proteins.
- metabolism : Influenza A virus, Viral Nonstructural Proteins.
- Influenza Pandemic, 1918-1919, Models, Molecular, Protein Conformation, Solutions.
Abstract
Nonstructural protein 1 (NS1) is a multifunctional virulence factor of influenza virus. The effector domain (ED) of influenza viruses is capable of binding to a variety of host factors, however, the molecular basis of the interactions remains to be investigated. The isolated NS1-ED exists in equilibrium between the monomer and homodimer. Although the structural diversity of the dimer interface has been well-characterized, limited information is available regarding the internal conformational heterogeneity of the monomeric NS1-ED. Here, we present the solution NMR structure of the NS1-ED W187R of the 1918 influenza A virus, which caused the "Spanish flu." Structural plasticity is an essential property to understand the molecular mechanism by which NS1-ED interacts with multiple host proteins. Structural comparison with the NS1-ED from influenza A/Udorn/1972 (Ud) strain revealed a similar overall structure but a distinct conformational variation and flexibility. Our results suggest that conformational flexibility of the NS1-ED might differ depending on the influenza strain.
DOI: 10.1016/j.bbrc.2019.08.027
PubMed: 31420169
Affiliations:
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Electronic address: jaehyuncho@tamu.edu.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843</wicri:regionArea><wicri:noRegion>77843</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Influenza A virus (metabolism)</term><term>Influenza Pandemic, 1918-1919</term><term>Models, Molecular</term><term>Mutant Proteins (chemistry)</term><term>Protein Conformation</term><term>Solutions</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines</term><term>Modèles moléculaires</term><term>Pandémie de grippe de 1918-1919</term><term>Protéines mutantes ()</term><term>Protéines virales non structurales ()</term><term>Protéines virales non structurales (métabolisme)</term><term>Solutions</term><term>Virus de la grippe A (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Mutant Proteins</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Influenza A virus</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines virales non structurales</term><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Influenza Pandemic, 1918-1919</term><term>Models, Molecular</term><term>Protein Conformation</term><term>Solutions</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Modèles moléculaires</term><term>Pandémie de grippe de 1918-1919</term><term>Protéines mutantes</term><term>Protéines virales non structurales</term><term>Solutions</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nonstructural protein 1 (NS1) is a multifunctional virulence factor of influenza virus. The effector domain (ED) of influenza viruses is capable of binding to a variety of host factors, however, the molecular basis of the interactions remains to be investigated. The isolated NS1-ED exists in equilibrium between the monomer and homodimer. Although the structural diversity of the dimer interface has been well-characterized, limited information is available regarding the internal conformational heterogeneity of the monomeric NS1-ED. Here, we present the solution NMR structure of the NS1-ED W187R of the 1918 influenza A virus, which caused the "Spanish flu." Structural plasticity is an essential property to understand the molecular mechanism by which NS1-ED interacts with multiple host proteins. Structural comparison with the NS1-ED from influenza A/Udorn/1972 (Ud) strain revealed a similar overall structure but a distinct conformational variation and flexibility. Our results suggest that conformational flexibility of the NS1-ED might differ depending on the influenza strain.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Shen, Qingliang" sort="Shen, Qingliang" uniqKey="Shen Q" first="Qingliang" last="Shen">Qingliang Shen</name></noRegion><name sortKey="Cho, Jae Hyun" sort="Cho, Jae Hyun" uniqKey="Cho J" first="Jae-Hyun" last="Cho">Jae-Hyun Cho</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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