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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein.

Spontaneous proteolysis of influenza virus M1 protein during crystallisation has defined an N-terminal domain of amino acids 1--164. Full-length M1, the N-terminal domain, and the C-terminal part of M1 (residues 165--252) were produced in Escherichia coli. In vitro tests showed that only full-length M1 and its N-terminal domain bind to negatively charged liposomes and that only full-length M1 and its C-terminal part bind to RNP. However, only full-length M1 had transcription inhibition activity. Several independent experimental approaches indicate that in vitro transcription inhibition occurs through polymerisation/aggregation of M1 onto RNP, or of M1 onto M1 already bound to RNP, rather than by binding to a specific active site on the nucleoprotein or the polymerase. The structure/function of influenza virus M1 will be compared with that of the Ebola virus matrix protein, VP40.[1]


  1. In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein. Baudin, F., Petit, I., Weissenhorn, W., Ruigrok, R.W. Virology (2001) [Pubmed]
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