Abstract
In this article we report the initial biochemical, genetic, and electron microscopic analysis of a previously uncharacterized, 8.9-kDa, predicted thiol-redox protein. The name A2.5L was assigned to the corresponding vaccinia virus gene, which is conserved in all sequenced poxviruses. Multiple alignment analysis and secondary structure prediction indicated that the A2.5L gene product is an all-α-helical protein with a conserved Cxx(x)C motif in the N-terminal α-helix. The DNA replication requirement and kinetics of A2.5L protein accumulation in virus-infected cells were typical of a late gene product, in agreement with the predicted promoter sequence. The A2.5L protein was a monomer under reducing conditions, but was mostly associated with the vaccinia virus E10R redox protein as a heterodimer under nonreducing conditions. The A2.5L protein was detected in virus particles at various stages of assembly, suggesting that it is an integral component of intracellular virions. An inducer-dependent A2.5L null mutant was constructed: in the absence of inducer, infectious virus formation was abolished and electron microscopy revealed an assembly block with an accumulation of crescent membranes and immature virions. This stage of assembly block was similar to that occurring when the E10R and G4L redox proteins were repressed, which is compatible with the involvement of E10R, A2.5L, and G4L in the same redox pathway.
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