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Category: Clinical Microbiology
Committing the Oldest Sins in the Newest Kind of Ways—Antibodies Targeting the Influenza Virus Type A Hemagglutinin Globular Head, Page 1 of 2
< Previous page | Next page > /docserver/preview/fulltext/10.1128/9781555817411/9781555817350_Chap12-1.gif /docserver/preview/fulltext/10.1128/9781555817411/9781555817350_Chap12-2.gifAbstract:
Influenza hemagglutinin (HA) is the major glycoprotein on the surface of influenza virions. It mediates receptor binding and fusion. The surface glycoprotein neuraminidase (NA) is a receptor-destroying enzyme. Even though humoral immunity to NA and other proteins and cellular immunity to several viral proteins contribute to protection against influenza infection, neutralizing antibodies directed against influenza HA are sufficient to protect against disease. The H3 HA crystal structure was solved in 1981 at 3-Å resolution ( 1 ). Since then, the crystal structures of HA molecules from H2, H5, H7, and several different H1 strains including the pandemic 1918 H1 and the pandemic 2009 H1 ( 2 ) have been determined. In brief, HA is a trimeric type I membrane glycoprotein made of three identical subunits ( Fig. 1 ). Each subunit is synthesized as an HA0 precursor and cleaved proteolytically into an HA1 subunit that composes the membrane-distal globular head and part of the membrane-proximal stem region, and an HA2 subunit that only contributes to the stem region ( Fig. 1 ).
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Space-filling model of influenza hemagglutinin HA based on PDB 1RD8 ( 38 ). The three protomers of the HA trimer are colored white, gray, or black.
Characteristics of globular head versus stem HA antibodies
Select cross-reactive globular head HA antibodies