Influenza A virus H6N1 hemagglutinin (H6N1 HA)

The Influenza A H6N1 hemagglutinin (HA) is a critical surface glycoprotein responsible for the virus's ability to infect host cells by binding to sialic acid receptors via its receptor-binding site (RBS) (Tzarum et al., 2015; Skehel & Wiley, 2000). The RBS is located in the head domain of the HA1 subunit and consists of three conserved secondary structural elements: the 130-loop, 220-loop, and 190-helix (Tzarum et al., 2015). While H6N1 is primarily an avian pathogen, the first human infection was reported in Taiwan in 2013, highlighting its zoonotic potential and the risk of pandemic emergence (Shi et al., 2013). Mutations such as G228S, P186L, and G225D within the RBS have been identified as key factors that can alter receptor preference from avian-like (alpha 2,3-linked) to human-like (alpha 2,6-linked) sialic acids (Wang et al., 2015; de Vries et al., 2017). As the primary target for neutralizing antibodies and vaccines, the H6N1 HA is central to influenza prevention and therapeutic development (Skehel & Wiley, 2000). Current therapeutic strategies include the development of broadly neutralizing antibodies, such as MEDI8852 and VIS410, which aim to block the RBS or inhibit the conformational changes required for membrane fusion (Zhang et al., 2021).

Other names

H6 hemagglutininHAHemagglutinin proteinH6N1 surface glycoproteinH6N1 HA

Neutralization of viral entry by blocking the receptor-binding site or preventing the conformational change required for membrane fusion.