These studies suggest that neural progenitor populations can contribute to the reservoir for HIV in the brain and undergo changes as a consequence of HIV persistence.

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Extended BiFC Bimolecular fluorescence complementation (BiFC) is a powerful tool for detecting protein-protein interactions in living cells. Proteins of interest are tagged at the N (YN) or C terminus (YC) with complementary fragments of yellow fluorescence protein (YFP); when an interaction occurs, the complementary fragments come together, producing a yellow fluorescent signal. However, this approach does not provide information on expression or localization of the individual protein partners, which would require additional analysis (e.g., FRET). Wolff et al. have modified the BiFC assay to provide expression and localization data in addition to interaction data. Proteins of interest, in this case the HIV Rev proteina key regulator in HIV replicationand known Rev interaction partners were tagged with YN or YC, each fused to a second constitutively fluorescing domainCFP (blue signal) or mRFP1 (red signal), respectively. Co-expression of pairs of interacting proteins in HeLa cells yielded blue, red, and yellow signals, identifying the free proteins and the interacting pairs; co-expression of non-interactors yielded only blue and red signals, despite colocalization of the proteins within the cell. This new approach, which the authors dub extended BiFC (exBiFC), adds an additional layer of information to BiFC analysis by normalizing the protein interaction to the expression levels of the individual interacting proteins and will surely extend the capabilities of BiFC. -Page 688

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