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Fig. 4 | Retrovirology

Fig. 4

From: Functional analysis of the secondary HIV-1 capsid binding site in the host protein cyclophilin A

Fig. 4

CypA A25D binds with the same affinity as wild-type CypA to authentic HIV-1 capsids. a Schematic diagram of the TIRF assay for measuring CypA binding to the intact capsid. b Representative equilibrium binding curves obtained for wild type (top) and A25D (bottom) by plotting the mean number of CypA molecules bound per capsid at equilibrium as a function of CypA concentration. The fit of an equilibrium binding model (black line) gave estimates for KD and number of molecules bound at saturation; wild type: KD = 11.6 μM, number of molecules = 1381; A25D: KD = 11.2 μM, number of molecules = 688. c KD (top graph) and mean number of CypA molecules bound per capsid at saturation (corresponding to the number of CypA loops that can be occupied simultaneously) (bottom graph) for the interaction of wild type CypA and CypA A25D with the capsid determined in independent experiments using different virus preparations; each symbol represents an independent experiment. The error bars represent standard deviations

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