Table 4.

Effects of mutations of MVH residues on the binding affinities (IFIE sums in units of kcal/mol) with the three receptors.

Receptor	MVH Mutation	Strand Region	IFIE (before Mutation)	IFIE (after Mutation)	ΔIFIE * (kcal/mol)	Major Cause for IFIE Change	Virological Experimental Results
SLAM	R533A	β5	−707.7	−636.7	71.0	Loss of salt bridge	+ + [28]
	D505A	β4–β5	−707.7	−608.7	98.9	Loss of salt bridge	n.r. $
	D507A	β4–β5	−707.7	−576.8	130.9	Loss of salt bridge	+ [29]
	D530A	β5	−707.7	−646.8	60.9	Loss of salt bridge	+ + [29]
	E503A	β4–β5	−707.7	−661.6	46.0	Loss of salt bridge	n.r.
	P554A	β5–β6	−707.7	−675.4	32.2	Loss of van der Waals interaction	+ [28]
	F552A	β5–β6	−707.7	−680.9	26.8	Loss of OH-π	+ [28]
	Y541A	β5	−707.7	−694.5	13.2	Loss of hydrogen bond	n.r.
	L482R	β4	−707.7	−713.8	−6.1	Increase of electrostatic interaction	n.r.
Nectin-4	Y543S	β5	−173.8	−167.3	6.5	Loss of NH-π	+ + [30]
CD46	G546S	β5	−285.7	−309.6	−23.8	Increase of electrostatic interaction	+ + [31]
	Y481A	β5	−285.7	−265.5	20.3	Loss of hydrogen bond	+ + [18]
	Y481N	β5	−285.7	−267.8	17.9	Loss of hydrogen bond	+ + [28]
	E471A #	β4	−285.7	−142.3 #	143.5 #	Loss of van der Waals interaction	n.r.
	K477A #	β4
	K488A #	β4
	E503A #	β4–β5
	R547A #	β5

Following the second column for mutation specification, the associated secondary structure of MVH, the change in IFIE value (see * below), major cause for IFIE change, and binding change result by virological experiment (+, + + with references or n.r.; see below) are shown. * IFIE(after mutation)—IFIE(before mutation). + Partial loss of the binding between the mutated MVH and the receptor has been reported in the literature shown in the parentheses. + + Loss of the binding of the mutated MVH to the receptor has been reported in the literature shown in the parentheses. ^$ n.r.: not reported. ^# Computational mutant with five multiple substitutions.