Human Lectins and Their Roles in Viral Infections

Mason, Christopher P.; Tarr, Alexander W.

doi:10.3390/molecules20022229

Cited by 85 publications

(66 citation statements)

References 258 publications

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“…Importantly, CLRs are also involved in cross-presentation, thus linking the endocytosis of viral pathogens with the presentation of viral peptides on MHC-I molecules to activate CD8 + T cells. In addition, signaling cascades triggered by CLR/virus interactions induce the expression of co-stimulatory molecules and the production of cytokines, therefore contributing to the fate determination of naïve T cells upon activation [40,41]. Thus, CLRs are at the frontline of innate and adaptive antiviral immune responses.…”

Section: Myeloid C-type Lectins Receptors—pattern Recognition Recementioning

confidence: 99%

“…As DC-SIGN, L-SIGN is a type II transmembrane protein with a short cytoplasmic tail involved in signaling and internalization, a transmembrane region, a neck domain consisting of eight repeat regions of 23 amino acids, and a Ca 2+ -dependent CRD [63]. Oppositely to DC-SIGN, L-SIGN presents a highly variable and polymorphic neck region, which impacts ligand-binding affinity and specificity for viral pathogens [40,44]. The neck region of L-SIGN is essential for tetramerization, thus increasing the binding avidity to multivalent ligands displayed on pathogen surfaces [44].…”

Section: Myeloid C-type Lectins Receptors—pattern Recognition Recementioning

confidence: 99%

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Myeloid C-Type Lectin Receptors in Viral Recognition and Antiviral Immunity

Monteiro

Lepenies

2017

Viruses

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Recognition of viral glycans by pattern recognition receptors (PRRs) in innate immunity contributes to antiviral immune responses. C-type lectin receptors (CLRs) are PRRs capable of sensing glycans present in viral pathogens to activate antiviral immune responses such as phagocytosis, antigen processing and presentation, and subsequent T cell activation. The ability of CLRs to elicit and shape adaptive immunity plays a critical role in the inhibition of viral spread within the host. However, certain viruses exploit CLRs for viral entry into host cells to avoid immune recognition. To block CLR interactions with viral glycoproteins, antiviral strategies may involve the use of multivalent glycan carrier systems. In this review, we describe the role of CLRs in antiviral immunity and we highlight their dual function in viral clearance and exploitation by viral pathogens.

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Section: Myeloid C-type Lectins Receptors—pattern Recognition Recementioning

confidence: 99%

Section: Myeloid C-type Lectins Receptors—pattern Recognition Recementioning

confidence: 99%

Myeloid C-Type Lectin Receptors in Viral Recognition and Antiviral Immunity

Monteiro

Lepenies

2017

Viruses

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“…Ficolins form complexes with MASPs (MBL-associated serine proteases or MASPs) and activate complement through the lectin pathway, leading to opsonization and phagocytosis of pathogens, and stimulating the production of inflammatory cytokines and nitric oxide [9]. Most active ficolins are composed of four trimeric subunits.…”

Section: Introductionmentioning

confidence: 99%

Association of a new FCN3 haplotype with high ficolin-3 levels in leprosy

et al. 2017

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Leprosy is a chronic inflammatory disease caused by Mycobacterium leprae that mainly affects the skin and peripheral nervous system, leading to a high disability rate and social stigma. Previous studies have shown a contribution of genes encoding products of the lectin pathway of complement in the modulation of the susceptibility to leprosy; however, the ficolin-3/FCN3 gene impact on leprosy is currently unknown. The aim of the present study was to investigate if FCN3 polymorphisms (rs532781899: g.1637delC, rs28362807: g.3524_3532insTATTTGGCC and rs4494157: g.4473C>A) and ficolin-3 serum levels play a role in the susceptibility to leprosy. We genotyped up to 190 leprosy patients (being 114 (60%) lepromatous), and up to 245 controls with sequence-specific PCR. We also measured protein levels using ELISA in 61 leprosy and 73 controls. FCN3 polymorphisms were not associated with disease, but ficolin-3 levels were higher in patients with FCN3 *2B1 (CinsA) haplotype (p = 0.032). Median concentration of ficolin-3 was higher in leprosy per se (26034 ng/mL, p = 0.005) and lepromatous patients (28295 ng/mL, p = 0.016) than controls (18231 ng/mL). In addition, high ficolin-3 levels (>33362 ng/mL) were more common in leprosy per se (34.4%) and in lepromatous patients (35.5%) than controls (19.2%; p = 0.045 and p = 0.047, respectively). Our results lead us to suggest that polymorphisms in the FCN3 gene cooperate to increase ficolin-3 concentration and that it might contribute to leprosy susceptibility by favoring M. leprae infection.

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“…C-type lectins such as DC-SIGN were reported previously to be involved in cell entry of various viruses (20). SFTSVpv was recently reported to use DC-SIGN as a receptor for host cell entry (5).…”

Section: Expression and Localization Of Sftsv-gpmentioning

confidence: 99%

Characterization of Glycoprotein-Mediated Entry of Severe Fever with Thrombocytopenia Syndrome Virus

Tani

Shimojima

Fukushi

et al. 2016

J Virol

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Severe fever with thrombocytopenia syndrome (SFTS) is an emerging hemorrhagic fever with a high case fatality rate caused by SFTS virus (SFTSV). Effective vaccines and specific therapies for SFTS are urgently sought, and investigation into virus-host cell interactions is expected to contribute to the development of antiviral strategies. In this study, we have developed a pseudotype vesicular stomatitis virus (VSV) bearing the unmodified Gn/Gc glycoproteins (GPs) of SFTSV (SFTSVpv). We have analyzed the host cell entry of this pseudotype virus and native SFTSV. Both SFTSVpv and SFTSV exhibited high infectivity in various mammalian cell lines. The use of lysosomotropic agents indicated that virus entry occurred via pH-dependent endocytosis. SFTSVpv and SFTSV infectivity was neutralized by serial dilutions of convalescent-phase patient sera. Entry of SFTSVpv and growth of SFTSV were increased in Raji cells expressing not only the C-type lectin dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) but also DC-SIGN-related (DC-SIGNR) and liver and lymph node sinusoidal endothelial cell C-type lectin (LSECtin). 25-Hydroxycholesterol (25HC), a soluble oxysterol metabolite, inhibited the cell entry of SFTSVpv and the membrane fusion of SFTSV. These results indicate that pH-dependent endocytosis of SFTSVpv and SFTSV is enhanced by attachment to certain C-type lectins. SFTSVpv is an appropriate model for the investigation of SFTSV-GP-mediated cell entry and virus neutralization at lower biosafety levels. Furthermore, 25HC may represent a potential antiviral agent against SFTS. IMPORTANCESFTSV is a recently discovered bunyavirus associated with SFTS, a viral hemorrhagic fever with a high case fatality rate endemic to China, South Korea, and Japan. Because little is known about the characteristics of the envelope protein and entry mechanisms of SFTSV, further studies will be required for the development of a vaccine or effective therapies. In this study, we investigated the mechanism of SFTSV cell entry using SFTSVpv and the native virus. SFTSV can grow in nonsusceptible cell lines in the presence of certain C-type lectins. Moreover, 25HC, an oxysterol metabolite, may represent a potential therapeutic inhibitor of SFTSV infection. Severe fever with thrombocytopenia syndrome (SFTS), a newly recognized emerging viral infectious disease, is caused by a novel phlebovirus in the family Bunyaviridae, SFTS virus (SFTSV) (1-3). SFTSV can be transmitted to humans by tick bites, causing abrupt high fever, thrombocytopenia, leukopenia, and gastrointestinal symptoms, with a high case fatality rate (4). SFTSV is a single-stranded negative-sense RNA virus with three genomic segments, L, M, and S. The L segment encodes a viral RNA polymerase, while the M segment encodes the two viral envelope glycoproteins (GPs) Gn and Gc. The S segment is an ambisense RNA encoding a nucleoprotein (NP) and a nonstructural protein (NSs). The Gn and Gc proteins of bunyaviruses are usually localized in the Golgi app...

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Human Lectins and Their Roles in Viral Infections

Cited by 85 publications

References 258 publications

Myeloid C-Type Lectin Receptors in Viral Recognition and Antiviral Immunity

Myeloid C-Type Lectin Receptors in Viral Recognition and Antiviral Immunity

Association of a new FCN3 haplotype with high ficolin-3 levels in leprosy

Characterization of Glycoprotein-Mediated Entry of Severe Fever with Thrombocytopenia Syndrome Virus

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