Key result
Mutagenesis of two neighboring hydrophobic residues in the viral fusion protein cavity caused severe F-to-H binding and fusion-triggering deficiencies, suggesting sideways H binding.
Identified critical hydrophobic residues in the Canine Distemper Virus F protein cavity essential for interaction with the H protein and membrane fusion.
Hypothesis-generating for CDV fusion mechanisms; leaves open relevance to human paramyxoviruses or antiviral strategies.
Membrane fusion for morbillivirus cell entry relies on critical interactions between the viral fusion (F) and attachment (H) envelope glycoproteins. Through extensive mutagenesis of an F cavity recently proposed to contribute to F's interaction with the H protein, we identified two neighboring hydrophobic residues responsible for severe F-to-H binding and fusion-triggering deficiencies when they were mutated in combination. Since both residues reside on one side of the F cavity, the data suggest that H binds the F globular head domain sideways.
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Avila et al. (2014) studied Canine Distemper Virus infection. Mutagenesis of F cavity hydrophobic residues was evaluated on F-to-H binding and fusion-triggering. Mutagenesis of two neighboring hydrophobic residues in the viral fusion protein cavity caused severe F-to-H binding and fusion-triggering deficiencies, suggesting sideways H binding.
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