Key result
Hsc70 outcompetes NS2 for influenza M1 binding, suggesting a key role in vRNP nuclear export.
Hsc70-M1 competition may modulate vRNP export; leaves open therapeutic targeting pending infection-model validation.
The influenza virus replicates in the host cell nucleus, and the progeny viral ribonucleoprotein complex (vRNP) is exported to the cytoplasm prior to maturation. NS2 has a nuclear export signal that mediates the nuclear export of vRNP by the vRNP-M1-NS2 complex. We previously reported that the heat shock cognate 70 (Hsc70) protein binds to M1 protein and mediates vRNP export. However, the interactions among M1, NS2, and Hsc70 are poorly understood. In the present study, we demonstrate that Hsc70 interacts with M1 more strongly than with NS2 and competes with NS2 for M1 binding, suggesting an important role of Hsc70 in the nuclear export of vRNP.
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Watanabe et al. (2014) studied Influenza virus infection. Hsc70 was evaluated on Protein interactions among M1, NS2, and Hsc70. Hsc70 interacts with influenza virus M1 protein more strongly than with NS2 and competes with NS2 for M1 binding, suggesting an important role in the nuclear export of vRNP.
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