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Unique Tropism and Entry Mechanism of Mumps Virus

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Unique Tropism and Entry Mechanism of Mumps Virus viruses Review Unique Tropism and Entry Mechanism of Mumps Virus Marie Kubota 1,*,† and Takao Hashiguchi 2,* 1 Department of Otorhinolaryngology, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan 2 Laboratory of Medical Virology, Institute for Frontier Life and Medical Sciences, Kyoto University, Kyoto 606-8507, Japan * Correspondence: [email protected] (M.K.); [email protected] (T.H.) † Current address: Department of Otolaryngology-Head & Neck Surgery, Stanford University School of Medicine, Stanford, CA 94305, USA. 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 popula- tions. 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. Keywords: mumps virus; tropism; entry; glycan receptors; attachment protein; structure Citation: Kubota, M.; Hashiguchi, T. Unique Tropism and Entry Mechanism of Mumps Virus. Viruses 2021, 13, 1746. https://doi.org/ 1. Introduction 10.3390/v13091746 Mumps is a well-known infectious disease caused by the mumps virus (MuV). It Academic Editor: Hironori Sato occurs worldwide, with an average of 500,000 cases reported annually. After an incubation period of 2–4 weeks, mild symptoms of the infection appear, including low fever, headache, Received: 7 August 2021 and malaise, typically followed by bilateral swelling of the parotid glands. Following the Accepted: 30 August 2021 initial viral infection in the upper respiratory mucosa and regional lymph nodes, MuV Published: 1 September 2021 spreads systemically throughout the body [1–3]. MuV shows tropism to glandular and neural tissues, to organs, such as the kidney and heart, and to joint tissues. Parotitis occurs Publisher’s Note: MDPI stays neutral in 60–70% of infections. Infrequently, other salivary glands, such as the submandibular with regard to jurisdictional claims in and sublingual glands, may also be affected. Orchitis is found in 20–30% of infected published maps and institutional affil- adult males, mostly in conjunction with epididymitis. Approximately 15% of orchitis iations. cases may progress to testicular atrophy, leading to decreased fertility [2,4]. Oophoritis is observed in 5% of infected adult females. Pancreatitis has been reported in 4% of cases. Central nervous system (CNS) involvement is another common manifestation of MuV infection. The most common neurological symptom is aseptic meningitis, which occurs Copyright: © 2021 by the authors. in 1–10% of cases. Cerebrospinal fluid (CSF) pleocytosis has been reported in up to 50% Licensee MDPI, Basel, Switzerland. of infected cases, with increased cytokine levels reflecting meningeal inflammation [2,5,6]. This article is an open access article Encephalitis is another manifestation that is observed less commonly. Sensorineural distributed under the terms and hearing loss is a well-known complication, previously estimated to occur in 1/15,000 conditions of the Creative Commons to 1/20,000 cases; however, more recent studies have suggested that the frequency could Attribution (CC BY) license (https:// be 1/1000 [3,7]. In the majority of cases, mumps-related hearing loss is profound and creativecommons.org/licenses/by/ resistant to therapeutics [8]. Live attenuated mumps vaccines, for example, the measles– 4.0/). Viruses 2021, 13, 1746. https://doi.org/10.3390/v13091746 https://www.mdpi.com/journal/viruses Viruses 2021, 13, x FOR PEER REVIEW 2 of 14 mumps–rubella (MMR) vaccines, can prevent MuV infections in childhood and serious complications in young individuals [3]. Despite its unique tropism to glandular and neural tissues, the mechanisms underly- Viruses 2021, 13, 1746 ing tropism are still poorly understood. Tropism is affected at multiple stages of the viral 2 of 14 life cycle in response to interactions with host cells. 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 regulatingmumps–rubella tropism and (MMR) virulence vaccines, of the can virus. prevent MuV infections in childhood and serious MuVcomplications is an enveloped, in young non-segmented, individuals [3]. negative-stranded RNA virus of the genus OrthorubulavirusDespite and its uniquefamily tropismParamyxoviridae to glandular. Its genome and neural contains tissues, 15,384 the mechanisms nucleotides underlying en- codingtropism nucleocapsid are still (N), poorly phosphor understood. (P), matrix Tropism (M), is affectedsmall hydrophobic at multiple stages(SH), large of the (L), viral life hemagglutinin-neuraminidasecycle in response to interactions (HN), and with fusion host (F) cells. proteins Binding [3]. to Based cellular on the receptors sequence during of the SH andinitial HN stagesgenes, ofMuV viral has entry been is classified known to in beto one 12 genotypes of the determinants [9]. The N thatprotein plays together a key role in with theregulating RNA-dependent tropism and RNA virulence polymerase of the co virus.mplex comprising L and P proteins form the ribonucleoproteinMuV is an enveloped,(RNP) complex, non-segmented, which plays negative-stranded an essential role in RNA viral virus replication of the genus and transcriptionOrthorubulavirus [1,10].and The family M proteinParamyxoviridae is involved in. Its organizing genome containsvirion assembly 15,384 nucleotidesand sup- en- portingcoding the budding nucleocapsid of viral (N), particles phosphor [1,10]. (P), In matrixsome paramyxoviruses, (M), small hydrophobic M proteins (SH), have large (L), been proposedhemagglutinin-neuraminidase to inhibit host factors (HN),to enha andnce fusion viral production (F) proteins [1 [30,11].]. Based SH onproteins the sequence are of presentSH in and Rubulavirinae HN genes, such MuV as has MuV, been parainfluenza classified into virus 12 genotypes 5 (PIV5), and [9]. TheJeilongvirus N protein [10]. together SH proteinswith the are RNA-dependent believed to facilitate RNA evasion polymerase of the host complex antiviral comprising response L by and blocking P proteins the form TNF-αthe-mediated ribonucleoprotein apoptosis pathway (RNP) complex, [1,3]. Cellul whichar playsentry anof essentialparamyxoviruses role in viral relies replication on two envelopeand transcription glycoproteins: [1,10 attachment]. The M protein proteins is (HN involved in the inmajority organizing of paramyxoviruses, virion assembly and includingsupporting MuV (Figure the budding 1A); hemagglutinin of viral particles (H) [ 1in,10 Morbillivirus]. In some paramyxoviruses, (e.g., measles virus M proteins(MeV)) have (Figurebeen 1B), proposed and glycoprotein to inhibit (G) host in factorsHenipavirus to enhance (e.g., Nipah viral production virus)), and [10 F ,protein.11]. SH proteinsWhile are the attachmentpresent in proteinsRubulavirinae (HN/H/suchG proteins) as MuV, are parainfluenza responsible virusfor receptor 5 (PIV5), recognition, and Jeilongvirus the F [10]. proteinSH plays proteins a role are in membrane believed to fusion facilitate [10]. evasion of the host antiviral response by blocking Here,the TNF- we αreview-mediated the recent apoptosis advances pathway in [the1,3]. general Cellular understanding entry of paramyxoviruses of MuV entry relies on based twoon the envelope structures glycoproteins: of MuV-HN attachment and glycan proteins receptor (HN complexes, in the majority in combination of paramyxoviruses, with the functionalincluding findings MuV (Figure of these1A); interactions. hemagglutinin We present (H) in theMorbillivirus glycan receptors(e.g., measles of MuV, virus their (MeV)) structural(Figure variations,1B), and and glycoprotein their interactions (G) in Henipavirus with the HN(e.g., protein. Nipah In virus)), addition, and we F protein. discuss While MuV tropismthe attachment based on proteins the dist (HN/H/Gribution of proteins) glycan arereceptors responsible in the for human receptor body recognition, and the the F functionalprotein roles plays of recently a role in identified membrane host fusion factors [10 ].for the tropism of MuV. Figure 1. Structures of MuV and MeV attachment proteins bound to their receptors. (A) MuV-HN Figure 1. Structures of MuV and MeV attachment proteins bound to their receptors. (A) MuV-HN (rainbow color) bound to a glycan receptor analog (cyan) α2,3-linked sialyllactose (30-SL) at the top (rainbow color) bound to a glycan receptor analog (cyan) α2,3-linked sialyllactose (3′-SL) at the top receptor-bindingreceptor-binding pocket pocketof the head of the domain; head domain; (B) MeV-H (B) MeV-H (rainbow (rainbow color) bound color)
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