Mutations in the Stalk Region of the Measles Virus Hemagglutinin Inhibit Syncytium Formation but Not Virus Entry
Matthew K. Ennis, Chunling Hu, Shruthi Naik, Louay K. Hallak, Kah Whye Peng, Stephen J. Russell, David Dingli
Abstract
Matthew K. Ennis, Chunling Hu, Shruthi Naik, Louay K. Hallak, Kah Whye Peng, Stephen J. Russell, David Dingli
Abstract
Measles virus (MV) entry requires at least 2 viral proteins, the hemagglutinin (H) and fusion (F) proteins. We describe the rescue and characterization of a measles virus with a specific mutation in the stalk region of H (I98A) that is able to bind normally to cells but infects at a lower rate than the wild type due to a reduction in fusion triggering. The mutant H protein binds to F more avidly than the parent H protein does, and the corresponding virus is more sensitive to inhibition by fusion-inhibitory peptide. We show that after binding of MV to its receptor, H-F dissociation is required for productive infection.
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Measles virus (MV) entry requires at least 2 viral proteins, the hemagglutinin (H) and fusion (F) proteins. We describe the rescue and characterization of a measles virus with a specific mutation in the stalk region of H (I98A) that is able to bind normally to cells but infects at a lower rate than the wild type due to a reduction in fusion triggering. The mutant H protein binds to F more avidly than the parent H protein does, and the corresponding virus is more sensitive to inhibition by fusion-inhibitory peptide. We show that after binding of MV to its receptor, H-F dissociation is required for productive infection.
Key concepts: Biology, Syncytium, Measles virus, Virology, Hemagglutinin (influenza), Virus, Morbillivirus, Mononegavirales