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Structural modeling of the Influenza virus Hemagglutinin protein in complex with a broadly neutralizing antibody
Author(s) -
Ramirez Robert,
Johnson Brendon,
Nguyen Tina,
Kwan James,
Chowdhury Parag,
Bhabha Gira,
Ekiert Damian
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.lb169
Subject(s) - hemagglutinin (influenza) , virology , antibody , virus , biology , viral envelope , influenza a virus , neutralizing antibody , immunology
The 1918 Spanish Influenza (H1N1) is considered one of the most disastrous pandemics in human history. It is estimated to have killed over 50 million people worldwide. The recent outbreak of H1N1 has renewed interest in this virus and the envelope proteins that allow it to enter mammalian cells. Hemagglutinin (HA) is a trimeric protein found on the surface of the influenza virus, and mediates viral attachment and entry into host cells. This protein has been the subject of intense research, as it may serve as an ideal target for the attachment of antibodies, that could prevent pathogenesis. Broadly neutralizing antibodies have the ability to bind and inhibit several subtypes of Hemagglutinin, and therefore hold much promise for therapies against influenza. CR8020 is one such broadly neutralising antibody. In a current study we look at how this antibody interacts with the stem region of the HA trimer. CR8020 binds in the stem region of HA and prevents viral fusion with the endocytic vesicle thus inhibiting the release of viral RNA into the cell. This work is important for the development of a “durable universal cross‐protective vaccine.” Supported by a grant from the HHMI Pre‐College Program.