Table 3.

Fusion properties of mutants in residues bridging the intermolecular EI/LI β‐sheet

Virus/mutationa	Corresponding CHAV G residuesa	Phenotype
VSV/D137Lb	D121	Fusion less efficient than WT
VSV/D137Nc	D121	Fusion poorly efficient, detected only below pH 5.5
VSV/E139Lb	E123	Fusion less efficient than WT
VHSV/Q118Rg, d	K76	Shift in the pH threshold for membrane fusion
VSV/E76Ke	K76	Compensatory mutation rescuing nonfusogenic VSV G with lethal mutation A117F
VSV/H80Af VSV/H80Ef	H80	No fusion detected
VSV D121L/E123Lf	D121/E123	No fusion detected
VSV/H80Kf	H80	Mutation rescuing nonfusogenic VSV G with lethal mutations H80E
VSV/Q112Pf	E112	Compensatory mutation rescuing nonfusogenic VSV G with lethal mutations H80A or D121L/E123L

^aNumbering of residues corresponds to that used by the authors in the original publications in the first column, to CHAV G numbering used in this work in the second column. Inconsistent numbering in places is due to the length of the signal peptide being counted in some of the original publications.

^bReferenced in Fredericksen and Whitt (1995).

^cReferenced in Zhang and Ghosh (1994).

^dReferenced in Gaudin et al (1999).

^eReferenced in Stanifer et al (2011).

^fThis work.

^gThree strains sharing only this mutation from the parental VHSV strain (07–71) all show a shift of their fusion pH (Gaudin et al, 1999).