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. 2011 Oct 7;286(48):41402–41412. doi: 10.1074/jbc.M111.237784

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© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 5. — Binding of BNLF2a to TAP is mutually exclusive from HCMV-US6. A, interaction of BNLF2a with TAP. Membranes isolated from Sf9 insect cells coexpressing TAP1/2 and BNLF2a^C8-NST were solubilized with 2% digitonin. Solubilized proteins were immunoprecipitated using TAP2-specific antibodies (IP). As a negative control, HC10-antibody was used (mock). Aliquots of the anti-TAP2 immunoprecipitate were treated with EndoH. Samples were analyzed by SDS-PAGE (10%) and subsequent immunoblotting with the corresponding antibodies. Aliquots (1/20) of solubilized input (S) and unbound proteins after immunoprecipitation (FT) are shown. B, BNLF2a and US6 are mutually exclusive in their interaction with TAP. Membranes isolated from Sf9 cells coexpressing TAP1/2, BNLF2a^C8-NST and US6^myc were subjected to coimmunoprecipitation experiments (IP) as described above using anti-C8 and anti-myc antibodies, respectively. As a negative control, HC10-antibody was used (mock). Input (S, 1/20 aliquot) and immune complexes (IP) were analyzed by immunoblotting. Asterisk, immunoglobulin heavy chain.