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Summary  The matrix protein 1 ( M 1) is the most abundant structural protein in influenza  A  virus particles. It oligomerizes to form the matrix layer under the lipid membrane, sustaining stabilization of the morphology of the virion. The present study indicates that  M 1 forms oligomers based on a fourfold symmetrical oligomerization pattern. Further analysis revealed that the oligomerization pattern of  M 1 was controlled by a highly conserved region within the  C ‐terminal domain. Two polar residues of this region, serine‐183 ( S 183) and threonine‐185 ( T 185), were identified to be critical for the oligomerization pattern of  M 1.  M 1 point mutants suggest that single  S183A  or  T185A  substitution could result in the production of morphologically filamentous particles, while double substitutions,  M1 ‐ S183A / T185A , totally disrupted the fourfold symmetry and resulted in the failure of virus production. These data indicate that the polar groups in these residues are essential to control the oligomerization pattern of  M 1. Thus, the present study will aid in determining the mechanisms of influenza  A  virus matrix layer formation during virus morphogenesis.

Two polar residues within C ‐terminal domain of M 1 are critical for the formation of influenza A Virions