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[1] [2] [3] Hemagglutinins are responsible for binding to receptors, sialic acid residues, on host cell membranes to initiate virus docking and infection. [ 4 ] [ 5 ] Specifically, they recognize cell-surface glycoconjugates containing sialic acid on the surface of host red blood cells with a low affinity and use them to enter the endosome of ...
Hemagglutinin is a class I fusion protein, [1] [2] having multifunctional activity as both an attachment factor and membrane fusion protein. Therefore, HA is responsible for binding influenza viruses to sialic acid on the surface of target cells, such as cells in the upper respiratory tract or erythrocytes , [ 3 ] resulting in the ...
HA and HAI apply the process of hemagglutination, in which sialic acid receptors on the surface of red blood cells (RBCs) bind to the hemagglutinin glycoprotein found on the surface of influenza virus (and several other viruses) and create a network, or lattice structure, of interconnected RBCs and virus particles. [2]
Blood type can be determined by using antibodies that bind to the A or B blood group antigens in a sample of blood.. For example, if antibodies that bind the A blood group are added and agglutination occurs, the blood is either type A or type AB.
The HA-tag is a protein tag derived from the human influenza hemagglutinin (HA) protein, which allows the virus to target and enter host cells. An HA-tag is composed of a peptide derived from the HA-molecule corresponding to amino acids 98-106, which can be recognized and selectively bound by commercially available antibodies .
Kawaoka and his colleagues combined the H5 hemagglutinin gene from the bird flu virus with genes from the 2009 H1N1 swine flu virus. Then they coaxed their hybrid to evolve in a way that allowed ...
This Pfam entry also matches measles hemagglutinin (cd15467), which has a "dead" neuraminidase part repurposed as a receptor binding site. [4] Hemagglutinin-neuraminidase allows the virus to stick to a potential host cell, and cut itself loose if necessary.
The structure of hemagglutinin-esterase contributes to the intracellular transport. The hemagglutinin-esterase (HE) glycoprotein of influenza C virus is composed of three domains: a stem domain active in membrane fusion (F), an acetylesterase domain (E), and a receptor-binding domain (R). [6]