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Comparative Analysis of the Biological Activities of Different NS1 Variants from H5N1 Avian Influenza Virus
Author(s) -
Zhang Chi
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.lb82
Subject(s) - influenza a virus subtype h5n1 , virulence , virus , biology , influenza a virus , virology , mutant , mutation , amino acid , gene , reverse genetics , microbiology and biotechnology , genetics
The nonstructural protein NS1 contributes significantly to the pathogenicity of H5N1 avian influenza virus. It has been reported that five amino acids missing at 80–84 sites or mutation from aspartic acid to glutamic acid at position 92 (D92E) in NS1 play a key role in the enhanced virulence of H5N1 influenza virus. In order to elucidate whether the elevated virulence of virus is associated with the changes of cytokines induction/resistance and cellular apoptotic response caused by these NS1 mutations, we constructed three mutant NS1 proteins: NS51 with 5aa deletion at position 80–84; NS51(I) with 5aa insertion at position 80–84, and NS51(IM) with 5aa insertion and D92E replacement. We observed that 5aa deletion enhanced resistance to TNF¦Á response and D92E mutation resulted in the lost of NS1 inhibition in IFN induction. Our results also revealed that all three variants interfered similarly the transcriptional activity of p53. The above findings help to understand the role of NS1 in H5N1 avian influenza virus.