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Article: Structure of the influenza virus A H5N1 nucleoprotein: Implications for RNA binding, oligomerization, and vaccine design

TitleStructure of the influenza virus A H5N1 nucleoprotein: Implications for RNA binding, oligomerization, and vaccine design
Authors
Issue Date2008
PublisherFederation of American Societies for Experimental Biology. The Journal's web site is located at http://www.fasebj.org/
Citation
Faseb Journal, 2008, v. 22 n. 10, p. 3638-3647 How to Cite?
AbstractThe threat of a pandemic outbreak of influenza virus A H5N1 has become a major concern worldwide. The nucleoprotein (NP) of the virus binds the RNA genome and acts as a key adaptor between the virus and the host cell. It, therefore, plays an important structural and functional role and represents an attractive drug target. Here, we report the 3.3-Å crystal structure of H5N1 NP, which is composed of a head domain, a body domain, and a tail loop. Our structure resolves the important linker segments (residues 397-401, 429-437) that connect the tail loop with the remainder of the molecule and a flexible, basic loop (residues 73-91) located in an arginine-rich groove surrounding Arg150. Using surface plasmon resonance, we found the basic loop and arginine-rich groove, but mostly a protruding element containing Arg174 and Arg175, to be important in RNA binding by NP. We also used our crystal structure to build a ring-shaped assembly of nine NP subunits to model the miniribonucleoprotein particle previously visualized by electron microscopy. Our study of H5N1 NP provides insight into the oligomerization interface and the RNA-binding groove, which are attractive drug targets, and it identifies the epitopes that might be used for universal vaccine development. © FASEB.
Persistent Identifierhttp://hdl.handle.net/10722/171773
ISSN
2015 Impact Factor: 5.299
2015 SCImago Journal Rankings: 2.775
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorNg, AKLen_US
dc.contributor.authorZhang, Hen_US
dc.contributor.authorTan, Ken_US
dc.contributor.authorLi, Zen_US
dc.contributor.authorLiu, JHen_US
dc.contributor.authorChan, PKSen_US
dc.contributor.authorLi, SMen_US
dc.contributor.authorChan, WYen_US
dc.contributor.authorAu, SWNen_US
dc.contributor.authorJoachimiak, Aen_US
dc.contributor.authorWalz, Ten_US
dc.contributor.authorWang, JHen_US
dc.contributor.authorShaw, PCen_US
dc.date.accessioned2012-10-30T06:16:58Z-
dc.date.available2012-10-30T06:16:58Z-
dc.date.issued2008en_US
dc.identifier.citationFaseb Journal, 2008, v. 22 n. 10, p. 3638-3647en_US
dc.identifier.issn0892-6638en_US
dc.identifier.urihttp://hdl.handle.net/10722/171773-
dc.description.abstractThe threat of a pandemic outbreak of influenza virus A H5N1 has become a major concern worldwide. The nucleoprotein (NP) of the virus binds the RNA genome and acts as a key adaptor between the virus and the host cell. It, therefore, plays an important structural and functional role and represents an attractive drug target. Here, we report the 3.3-Å crystal structure of H5N1 NP, which is composed of a head domain, a body domain, and a tail loop. Our structure resolves the important linker segments (residues 397-401, 429-437) that connect the tail loop with the remainder of the molecule and a flexible, basic loop (residues 73-91) located in an arginine-rich groove surrounding Arg150. Using surface plasmon resonance, we found the basic loop and arginine-rich groove, but mostly a protruding element containing Arg174 and Arg175, to be important in RNA binding by NP. We also used our crystal structure to build a ring-shaped assembly of nine NP subunits to model the miniribonucleoprotein particle previously visualized by electron microscopy. Our study of H5N1 NP provides insight into the oligomerization interface and the RNA-binding groove, which are attractive drug targets, and it identifies the epitopes that might be used for universal vaccine development. © FASEB.en_US
dc.languageengen_US
dc.publisherFederation of American Societies for Experimental Biology. The Journal's web site is located at http://www.fasebj.org/en_US
dc.relation.ispartofFASEB Journalen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAntiviral Agents - Chemistry - Pharmacologyen_US
dc.subject.meshCrystallography, X-Rayen_US
dc.subject.meshDrug Designen_US
dc.subject.meshInfluenza A Virus, H5n1 Subtype - Chemistry - Drug Effects - Immunologyen_US
dc.subject.meshInfluenza Vaccines - Chemistry - Immunologyen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshNucleoproteins - Chemistry - Drug Effects - Immunologyen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshRna - Chemistryen_US
dc.subject.meshViral Core Proteins - Chemistry - Drug Effects - Immunologyen_US
dc.titleStructure of the influenza virus A H5N1 nucleoprotein: Implications for RNA binding, oligomerization, and vaccine designen_US
dc.typeArticleen_US
dc.identifier.emailZhang, H:hzhang20@hku.hken_US
dc.identifier.authorityZhang, H=rp00306en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1096/fj.08-112110en_US
dc.identifier.pmid18614582-
dc.identifier.scopuseid_2-s2.0-54049146687en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-54049146687&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume22en_US
dc.identifier.issue10en_US
dc.identifier.spage3638en_US
dc.identifier.epage3647en_US
dc.identifier.isiWOS:000259642600025-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridNg, AKL=25422458400en_US
dc.identifier.scopusauthoridZhang, H=7409196101en_US
dc.identifier.scopusauthoridTan, K=14006742200en_US
dc.identifier.scopusauthoridLi, Z=23485995500en_US
dc.identifier.scopusauthoridLiu, JH=36066228400en_US
dc.identifier.scopusauthoridChan, PKS=7403497792en_US
dc.identifier.scopusauthoridLi, SM=25422455700en_US
dc.identifier.scopusauthoridChan, WY=13310314800en_US
dc.identifier.scopusauthoridAu, SWN=7005457819en_US
dc.identifier.scopusauthoridJoachimiak, A=26540762500en_US
dc.identifier.scopusauthoridWalz, T=7005465519en_US
dc.identifier.scopusauthoridWang, JH=7701330874en_US
dc.identifier.scopusauthoridShaw, PC=35599523600en_US

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