. 2018 Feb 12;92(5):e01541-17. doi: 10.1128/JVI.01541-17

TABLE 1.

Overview of dissociation constants measured by MST and 2fFCS for the interaction of TRIM B30.2 domains and CypA with the different HIV-1 capsid surrogates normalized to monomeric capsid equivalents

Capsid surrogate or negative control	K_d^a
Capsid surrogate or negative control	rhTRIM5α	hsTRIM5α	hsTRIM20	CypA
Capsid monomer	1.6 ± 0.1 mM^b	1.1 ± 0.1 mM^b	2.2 ± 0.1 mM^b	ND
Capsid dimer	0.61 ± 0.04 mM^d	0.49 ± 0.06 mM^b	1.8 ± 0.1 mM^b	26.5 ± 5 μM^c
Capsid trimer	0.44 ± 0.04 mM^c	0.84 ± 0.09 mM^c	ND	17.8 ± 2 μM^c
Capsid hexamer	0.60 ± 0.09 mM^c	0.54 ± 0.1 mM^c	ND	28.9 ± 3 μM^c
Lysozyme	2.6 ± 0.3 mM^c	ND	ND	ND

The K_ds for the interactions of TRIM B30.2 domains with the different HIV-1 capsid surrogates, as well as lysozyme, are indicated relative to the concentrations of the monomeric capsid equivalents. The K_ds of the rhTRIM5α and hsTRIM5α B30.2 domains for the capsid trimer, which has the strongest binding affinity for the B30.2 domain of rhTRIM5α as well as the greatest increase in affinity compared to the K_d for the B30.2 domain of hsTRIM5α, are highlighted in bold. ND, not determined.

K_d determined by MST.

K_d determined by 2fFCS.

Average of K_ds determined by MST and 2fFCS.