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Hemagglutinin of the Victoria lineage is a major surface glycoprotein of Influenza B virus responsible for binding to sialic acid–containing receptors on host cells, initiating viral attachment and membrane fusion required for infection[6][2][3]. It is the primary target of neutralizing antibodies, making it a key antigen in seasonal influenza vaccines and a focus of therapeutic antibody development[5]. The Victoria lineage is one of two main evolutionary branches (along with Yamagata) of Influenza B virus hemagglutinin, differentiated by genetic and antigenic properties. HA functions as a trimer that undergoes proteolytic cleavage and acid-triggered conformational changes necessary for membrane fusion and viral entry into the host cell[3][2]. Antigenic drift in HA leads to regular updates in vaccine composition due to immune escape and poses ongoing challenges for influenza control.
Antibodies (from infection, vaccination, or therapy) neutralize virus by blocking HA’s binding to host receptors or inhibiting fusion mechanism[5]
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