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A new common mutation in the hemagglutinin of the 2009 (H1N1) influenza A virus

2010; Public Library of Science; Volume: 2; Linguagem: Inglês

10.1371/currents.rrn1162

2157-3999

Sebastian Maurer‐Stroh, Raphael Tze Chuen Lee, Frank Eisenhaber, Lin Cui, Shiau Pheng Phuah, Raymond T. P. Lin,

Protein Structure and Dynamics

As the 2009 (H1N1) influenza A virus continues evolving, most mutations appear geographically and temporally confined. However, the latest surveillance data suggests emergence of a new prominent mutation, E391K, in the hemagglutinin (HA) that is globally on the rise. Interestingly, when modelled in the context of the available HA crystal structure, this mutation could alter salt bridge patterns and stability in a region of the HA oligomerization interface that is important for membrane fusion and also a known antigenic site. We discuss occurrence of HA-E391K in global surveillance data and associated clinical phenotypes from Singapore ranging from mostly mild to few severe symptoms, including sporadic vaccine failure. More clinical and experimental data are needed to determine if this mutation could alter the biology and fitness of the virus or if its increased occurrence is due to founder effects.