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Here we show that mouse AKAP7 rapidly degrades 2-5A with kinetics similar to that of murine coronavirus (mouse hepatitis virus [MHV]) strain A59 ns2 and human rotavirus strain WA VP3 proteins.

To determine whether AKAP7 could substitute for a viral 2′,5′-PDE, we inserted AKAP7 c DNA into an MHV genome with an inactivated ns2 gene.

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A kinase anchoring proteins (AKAPs) bind the regulatory subunits of protein kinase A (PKA) to localize and organize cyclic AMP (c AMP) signaling during diverse physiological processes.

Among more than 43 AKAP isoforms, AKAP7 appears to be unique in its homology to viral 2′,5′-PDEs.

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The AKAP7 PDE domain or N-terminally truncated AKAP7 (both lacking a nuclear localization motif), but not full-length AKAP7 or a mutant, AKAP7, PDE domain restored the infectivity of ns2 mutant MHV in bone marrow macrophages and in livers of infected mice.

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