Open AccessAmino acid determinants conferring stable sialidase activity at low pH for H5N1 influenza A virus neuraminidase
Author(s) -
Takahashi Tadanobu,
Nidom Chairul A.,
Quynh Le Mai thi,
Suzuki Takashi,
Kawaoka Yoshihiro
Publication year - 2012
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1016/j.fob.2012.08.007
Subject(s) - neuraminidase , sialidase , influenza a virus subtype h5n1 , virology , virus , influenza a virus , h5n1 genetic structure , amino acid , chemistry , microbiology and biotechnology , biology , biochemistry , medicine , covid-19 , disease , infectious disease (medical specialty)
Avian influenza A viruses (IAVs) and human 1918, 1957, and 1968 pandemic IAVs all have neuraminidases (NAs) that are stable at low pH sialidase activity, yet most human epidemic IAVs do not. We examined the pH stability of H5N1 highly pathogenic avian IAV (HPAI) NAs and identified amino acids responsible for conferring stability at low pH. We found that, unlike other avian viruses, most H5N1 IAVs isolated since 2003 had NAs that were unstable at low pH, similar to human epidemic IAVs. These H5N1 viruses are thus already human virus‐like and, therefore, have the frequent infections of humans.