Abstract:
Influenza remains a serious global health threat and further characterization of key
viral proteins is necessary in order to develop novel drugs and vaccines. Matrix protein 1
(M 1) and matrix protein 2 (M2) of Influenza A Virus play key roles in the assembly and
release of new infectious viral particles. The cytoplasmic tail of M2 has been shown to be
critical for inducing membrane curvature in order to facilitate budding. M 1 has multiple
roles, including packaging viral RN A and recruiting it to the budozone through interactions
with M2 and other viral membrane proteins. In this role as an adaptor protein , Ml
participates in interactions with the membrane, viral genome elements and other viral
proteins and it is important to use a full-length M 1 construct that is capable of recapitulating
these many interactions. In this study, we present an optimized expression and purification
protocol for full-length Ml. We also present preliminary data showing characterization of
full-length M 1 using circular dichroism spectroscopy as well as isothermal titration
calorimetry and biolayer interferometry to study Ml-M2 binding.
