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. 2011 Nov;85(21):11242–11254. doi: 10.1128/JVI.05340-11

Fig. 7.

Fig. 7.

Sequence alignment of the relevant region within the H proteins of various morbilliviruses. GenBank accession numbers for each virus sequence are as follows: AB016162.1 (measles virus strain ICB), AF266288.1 (measles virus strain Edmonston), AF305419.1 (canine distemper virus strain Onderstepoort), AY386316.1 (canine distemper virus strain A75/17), BAA01203.1 (canine distemper virus strain 5804P), AY386315.1 (canine distemper virus strain 5804), D85755.1 (canine distemper virus strain Yanaka), X98291.3 (rinderpest virus strain Kabete O), Y18816.1 (rinderpest virus strain K), FJ648457.1 (porpoise morbillivirus strain IRL88), FJ648456.1 (phocine distemper virus strain DK02), and NC_005283.1 (dolphin morbillivirus). Below the sequences, stars indicate identical residues, and colons indicate semiconserved residues. CDV-H residues regulating SLAM-dependent fusion (Y525, D526, and R529) are highlighted in yellow. CDV-H residues regulating KeR-dependent fusion are shown against a black (for residues shown in this study, if mutated, to fully ablate KeR-dependent fusion) or a gray (for residues shown, if mutated, to partially influence KeR-dependent fusion) background. Amino acid numbering corresponds to the CDV-H sequence. Residues shown in MeV-H to regulate EpR-dependent fusion are highlighted in red; among these five amino acids, residues 478, 479, 537, and 539 inhibit EpR/KeR-dependent fusion activity both in MeV-H and in CDV-H, whereas residue 493, if mutated, was reported to fully ablate EpR-dependent fusion only in MeV-H (this residue was not mutated in CDV-H in this study due to the low probability that it is surface exposed).