Authors: Shun Xu Jianqiang Zhou Kang Liu Qiliang Liu Chunyi Xue Xiaoming Li Jing Zheng Dongyu Luo Yongchang Cao
Publish Date: 2013/06/08
Volume: 47, Issue: 1, Pages: 20-26
Abstract
Influenza A H3N2 virus caused 1968 Hong Kong influenza pandemic and has since been one of the most prevalent seasonal influenza viruses in global populations representing a credible pandemic candidate in future Previous studies have established that the hemagglutinin HA protein is the predominant antigen and executes receptor binding and membrane fusion Homologous sequence analysis of all HA subtypes of influenza viruses revealed that two cysteine residues 540 and 544 are uniquely present in the transmembrane domain TM of HA proteins from all influenza A H3N2 viruses However the functions of these two cysteines have not been fully studied Here we generated three mutants C540S C544L and 2C/SL to investigate the effects of the two TM cysteines on the biological functions of H3 HA We herein presented evidences that the mutations of one or two of the cysteines did not affect the proper expressions of HA proteins in cells and more importantly all mutant H3 HAs showed decreased thermal stability but increased fusion activity in comparison with wildtype HA Our results taken together demonstrated that the two TM cysteines are important for the biological functions of H3 HA proteins
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