Structure and sequence analysis of influenza A virus nucleoprotein

  title={Structure and sequence analysis of influenza A virus nucleoprotein},
  author={Andy Ka-Leung Ng and Jia-huai Wang and Pang-Chui Shaw},
  journal={Science in China Series C: Life Sciences},
Influenza A virus nucleoprotein (NP) forms homo-oligomers and multiple copies of NP wrap around genomic RNA, along with a trimeric polymerase making up ribonucleoprotein (RNP) complex. Sequence comparison of more than 2500 influenza A NP showed that this protein contains 30.1 % of polymorphic residues. NP is composed of a head and a body domain and a tail loop/ linker region. The head domain is more conserved than the body domain, as revealed from the structure-based sequence alignment. NP… 
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NP contains both positive and negative sequence elements involved in oligomerization and is consistent with the importance of NP-NP contacts for the formation of a transcriptionally active RNP.
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Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design
  • A. Ng, Hongmin Zhang, P. Shaw
  • Biology
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2008
The 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.
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NP, purified from virions and devoid of RNA, bound synthetic RNAs in vitro and interacted with the ribonucleotide homopolymers poly(A, poly(G), poly(U), and poly(C) in a salt-dependent manner, showing higher binding affinity for polypyrimidine homopolymer.
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