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The drug oseltamivir (Tamiflu®) inhibits flu neuraminidase, a component necessary for virus spread, in susceptible flu strains. Luckily H1N1 swine flu is susceptible (at least in early May, 2009). | The drug oseltamivir (Tamiflu®) inhibits flu neuraminidase, a component necessary for virus spread, in susceptible flu strains. Luckily H1N1 swine flu is susceptible (at least in early May, 2009). | ||
The development of oseltamivir was guided, in part, by crystallographically determined structures of flu neuraminidase. Neuraminidase is a homotetramer, shown with <font color='red'>'''oseltamivir'''</font> bound (<scene name='Avian_Influenza_Neuraminidase,_Tamiflu_and_Relenza/2hu4_tetramer/3'>restore initial scene</scene>). Here is <scene name='User:Eric_Martz/Sandbox_0/2hu4_tetramer/1'>one catalytic site</scene>. Oseltamivir was designed to fit [[Avian_Influenza_Neuraminidase%2C_Tamiflu_and_Relenza#Influenza Virus Neuraminidase|N2/N9]] (neuraminidases from other strains of flu). Serendipitously, it also fits N1, doing so by <scene name='<scene name='User:Eric_Martz/Sandbox_0/Morph_2hty_to_2hu4/4'>pulling one side of the binding site against itself (induced fit)</scene>. The most common mutation in N1 that confers resistance to oseltamivir is H274Y. The mutant tyrosine prevents oseltamivir from fitting, but still allows <scene name='User:Eric_Martz/Sandbox_6/3ckz_relenza_tyr274/2'>zanamivir (Relenza) to bind</scene>. [[Avian_Influenza_Neuraminidase%2C_Tamiflu_and_Relenza|Read more...]]. | The development of oseltamivir was guided, in part, by crystallographically determined structures of flu neuraminidase. Neuraminidase is a homotetramer, shown with <font color='red'>'''oseltamivir'''</font> bound (<scene name='Avian_Influenza_Neuraminidase,_Tamiflu_and_Relenza/2hu4_tetramer/3'>restore initial scene</scene>). Here is <scene name='User:Eric_Martz/Sandbox_0/2hu4_tetramer/1'>one catalytic site</scene>. Oseltamivir was designed to fit [[Avian_Influenza_Neuraminidase%2C_Tamiflu_and_Relenza#Influenza Virus Neuraminidase|N2/N9]] (neuraminidases from other strains of flu). Serendipitously, it also fits N1, doing so by <scene name='<scene name='User:Eric_Martz/Sandbox_0/Morph_2hty_to_2hu4/4'>pulling one side of the binding site against itself (induced fit)</scene>. The most common mutation in N1 that confers resistance to oseltamivir is H274Y. The mutant tyrosine prevents oseltamivir from fitting, but still allows <scene name='User:Eric_Martz/Sandbox_6/3ckz_relenza_tyr274/2'>zanamivir (Relenza) to bind</scene>. [[Avian_Influenza_Neuraminidase%2C_Tamiflu_and_Relenza|Read more...]]. | ||
<div align="right">[[Proteopedia:Featured article archives|Earlier featured articles...]]</div> | |||
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Revision as of 23:50, 2 May 2009
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Swine Flu, Neuraminidase & Tamiflu
H5N1 bird flu has seemed a likely pandemic threat for decades, but the first new influenza virus to emerge as an imminent pandemic threat in the 21st century is H1N1 swine flu. The drug oseltamivir (Tamiflu®) inhibits flu neuraminidase, a component necessary for virus spread, in susceptible flu strains. Luckily H1N1 swine flu is susceptible (at least in early May, 2009). The development of oseltamivir was guided, in part, by crystallographically determined structures of flu neuraminidase. Neuraminidase is a homotetramer, shown with oseltamivir bound (restore initial scene). Here is one catalytic site. Oseltamivir was designed to fit N2/N9 (neuraminidases from other strains of flu). Serendipitously, it also fits N1, doing so by pulling one side of the binding site against itself (induced fit). The most common mutation in N1 that confers resistance to oseltamivir is H274Y. The mutant tyrosine prevents oseltamivir from fitting, but still allows zanamivir (Relenza) to bind. Read more.... |
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