Abstract

Mumps virus (MuV) is an important human pathogen that causes parotitis, orchitis, oophoritis, meningitis, encephalitis, and sensorineural hearing loss. Although mumps is a vaccine-preventable disease, sporadic outbreaks have occurred worldwide, even in highly vaccinated populations. MuV not only causes systemic infection but also has a unique tropism to glandular tissues and the central nervous system. In general, tropism can be defined by multiple factors in the viral life cycle, including its entry, interaction with host factors, and host-cell immune responses. Although the underlying mechanisms of MuV tropism remain to be fully understood, recent studies on virus–host interactions have provided insights into viral pathogenesis. This review was aimed at summarizing the entry process of MuV by focusing on the glycan receptors, particularly the recently identified receptors with a trisaccharide core motif, and their interactions with the viral attachment proteins. Here, we describe the receptor structures, their distribution in the human body, and the recently identified host factors for MuV and analyze their relationship with MuV tropism.

Highlights

  • Mumps is a well-known infectious disease caused by the mumps virus (MuV)

  • This analysis confirmed that the trisaccharide structure is the core-receptor unit and that elongation of the glycan does not affect its binding with MuV-HN

  • The amino acid residues involved in the interaction with glycan of all genotypes except Phe370, which forms a stacking interaction with Tyr369 and is receptors were conserved in the MuV-HN of all genotypes except Phe370, which forms a replaced with leucine in genotype K, suggesting that MuVs of all 12 genotypes utilize them as receptors

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Summary

Introduction

Mumps is a well-known infectious disease caused by the mumps virus (MuV) It occurs worldwide, with an average of 500,000 cases reported annually. Binding to cellular receptors during the initial stages of viral entry is known to be one of the determinants that plays a key role in regulating tropism and virulence of the virus. N protein together initial stages of viral entry is known to be one of the determinants that plays a key role in with the RNA-dependent. Cellular entry an of essential paramyxoviruses relies on the ribonucleoprotein (RNP) complex, which plays role in viral replication two envelope glycoproteins: attachment proteins in thein majority of paramyxoviruses, and transcription. The general of MuV entry envelope glycoproteins: attachment proteins

Glycans and Viruses
Glycan Receptors with the Trisaccharide
Distribution of Glycan Receptors for MuV in the Human Body
Envelope Glycoproteins and Entry Models of Paramyxoviruses
Lysosome-Associated Membrane Proteins
Heat Shock Proteins
Findings
Future Investigations
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