The BMJ4 p24 protein forms a dimer in solution and in budding viruses.

<p>(A) Recombinant p24 proteins encoded by different HIV CA genes representing various subtypes were subjected to non-reducing SDS-PAGE. Only BMJ4 p24 displays a dimeric form, as determined by non-reducing SDS-PAGE. (B) The c(M) profiles resulting from sedimentation velocity (SV) were used to determine the apparent MW of the various p24 proteins in solution. The BMJ4 p24 protein displays a dimeric form, which is consistent with gel electrophoresis analysis. (C) p24 proteins extracted from an HIV lysate that was infected by infectious clones, including NL 4–3, MJ4 and the MJ4 C177A mutant, were subjected to non-reducing SDS-PAGE. Dimerization associated with the disulfide bond contributed by residue 177 was validated in a native HIV virion. The p24 dimers are indicated by red stars. (D) p24 proteins extracted from HIV lysates infected by infectious clones, including NL 4–3, MJ4 and the MJ4 C177A mutant, were subjected to reducing SDS-PAGE. The p24 dimers formed by disulfide bonds were dissociated under reducing conditions.