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. 2021 Sep 1;13(9):1746. doi: 10.3390/v13091746

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© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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MuV entry mechanism and host factors. Binding of MuV-HN to glycan receptors causes sequential conformational changes in the HN and F proteins, leading to membrane fusion. Multimerization of the MuV-HN head domain upon receptor binding may affect the structural change of the MuV-HN stalk domain, which in turn may trigger the structural change of the F protein. Following cellular entry, replication and transcription of the viral genome are regulated by host factors, such as heat shock protein family. LAMP family proteins support furin-mediated cleavage of the newly synthesized F protein.