Characterization Of The Interaction Between Two Influenza A Proteins (M1 and M2) Involved In Viral Assembly

Document Type

Poster Session

Publication Date


Published In

Biophysical Journal


Two of the proteins required for the efficient assembly of influenza A virus particles are matrix protein 1 (M1) and membrane-bound matrix 2 protein (M2). Our work involves developing a detailed biophysical understanding of the interaction of M1 protein and M2 protein. M2 is a 97-amino acid membrane-bound protein that we have previously characterized using site-directed spin-label electron paramagnetic resonance (SDSL-EPR). M1 is a 252-amino acid protein that associates with M2 protein during viral assembly and budding. Using a multi-pronged biophysical approach, we have probed the interaction of M1 protein with membranes both with and without reconstituted M2 protein. Both M1 and M2 proteins have been previously shown to have multiple conformational states. We hypothesize that the interaction of the two proteins preferentially stabilizes a subset of accessible conformations.