N-Glycans on the Rift Valley Fever Virus Envelope Glycoproteins Gn and Gc Redundantly Support Viral Infection via DC-SIGN

Phoenix, Inaia; Nishiyama, Shoko; Lokugamage, Nandadeva; Hill, Terence E.; Huante, Matthew B.; Slack, Olga A. L.; Carpio, Victor H.; Freiberg, Alexander N.; Ikegami, Tetsuro

doi:10.3390/v8050149

Cited by 31 publications

(30 citation statements)

References 44 publications

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“…Most importantly, N-and Olinked glycans shield immunodominant epitopes from immune recognition (Francica et al 2010;Helle et al 2011;Sommerstein et al 2015;Behrens et al 2016;Gram et al 2016;Walls et al 2016). In addition to general functions, specific types of glycans on viral glycoproteins often affect receptor binding and cell fusion (Lin et al 2003;Lozach et al 2003;Gramberg et al 2005;Davis et al 2006;Miller et al 2008;Chen et al 2014;Phoenix et al 2016;Wang et al 2016). Moreover, it is becoming increasingly clear that distinct glycans play separate roles in various stages of the viral cycle (Goffard et al 2005;Falkowska et al 2007;Helle et al 2010;Wang et al 2013Wang et al , 2017Lennemann et al 2014;Bradel-Tretheway et al 2015;Luo et al 2015;Orlova et al 2015;Wu et al 2017).…”

Section: Roles Of Glycosylation In Virus Biologymentioning

confidence: 99%

“…A number of viruses, such as HCV, Dengue virus, Ebola virus, SARS coronavirus, West Nile virus, Rift Valley fever virus and Japanese encephalitis virus use N-linked glycans as attachment and entry receptors by interacting with cellular lectins DC-SIGN, L-SIGN, LSECtin, ASGP-R or mannose receptor (Becker et al 1995;Lin et al 2003;Lozach et al 2003;Gramberg et al 2005;Davis et al 2006;Miller et al 2008;Chen et al 2014;Phoenix et al 2016;Wang et al 2016). Mature N-glycans have been suggested to influence Lassa virus binding to cell entry receptor α-dystroglycan (Shrivastava-Ranjan et al 2016).…”

Section: Attachment and Entrymentioning

confidence: 99%

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Global aspects of viral glycosylation

2018

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Enveloped viruses encompass some of the most common human pathogens causing infections of different severity, ranging from no or very few symptoms to lethal disease as seen with the viral hemorrhagic fevers. All enveloped viruses possess an envelope membrane derived from the host cell, modified with often heavily glycosylated virally encoded glycoproteins important for infectivity, viral particle formation and immune evasion. While N-linked glycosylation of viral envelope proteins is well characterized with respect to location, structure and site occupancy, information on mucin-type O-glycosylation of these proteins is less comprehensive. Studies on viral glycosylation are often limited to analysis of recombinant proteins that in most cases are produced in cell lines with a glycosylation capacity different from the capacity of the host cells. The glycosylation pattern of the produced recombinant glycoproteins might therefore be different from the pattern on native viral proteins. In this review, we provide a historical perspective on analysis of viral glycosylation, and summarize known roles of glycans in the biology of enveloped human viruses. In addition, we describe how to overcome the analytical limitations by using a global approach based on mass spectrometry to identify viral O-glycosylation in virus-infected cell lysates using the complex enveloped virus herpes simplex virus type 1 as a model. We underscore that glycans often pay important contributions to overall protein structure, function and immune recognition, and that glycans represent a crucial determinant for vaccine design. High throughput analysis of glycosylation on relevant glycoprotein formulations, as well as data compilation and sharing is therefore important to identify consensus glycosylation patterns for translational applications.

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Section: Roles Of Glycosylation In Virus Biologymentioning

confidence: 99%

Section: Attachment and Entrymentioning

confidence: 99%

Global aspects of viral glycosylation

2018

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“…Furthermore, if this region includes an epitope, the acquisition of N-linked glycosylation at helix h10 may mask the protein surface, similar to the "glycan shields" described for Old World Arenaviruses and HIV-1 (66,67). The occurrence of non-essential N-linked glycosylation sites affecting viral infectivity and replication has been previously described in BUNV (68) and RVFV (69).…”

Section: Structural Analysis Of Orov Proteins and Sites Under Selectionmentioning

confidence: 71%

The evolutionary dynamics of Oropouche Virus (OROV) in South America

Gutierrez

Wise

Pullan

et al. 2019

Preprint

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The Amazon basin is host to numerous arthropod-borne viral pathogens that cause febrile disease in humans. Among these, Oropouche orthobunyavirus (OROV) is a relatively understudied member of the Peribunyavirales that causes periodic outbreaks in human populations in Brazil and other South American countries. Although several studies have described the genetic diversity of the virus, the evolutionary processes that shape the viral genome remain poorly understood. Here we present a comprehensive study of the genomic dynamics of OROV that encompasses phylogenetic analysis, evolutionary rate estimates, inference of natural selective pressures, recombination and reassortment, and structural analysis of OROV variants. Our study includes all available published sequences, as well as a set of new OROV genomes sequences obtained from patients in Ecuador, representing the first set of viral genomes from this country. Our results show that differing evolutionary processes on the three segments that encompass the viral genome lead to variable evolutionary rates and TMRCAs that could be explained by cryptic reassortment. We also present the discovery of previously unobserved putative N-linked glycosylation sites, and codons which evolve under positive selection on the viral surface proteins, and discuss the potential role of these features in the evolution of the virus through a combined phylogenetic and structural approach.

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“…The two envelope glycoproteins Gc and Gn are responsible for viral attachment and acid-activated penetration ( 74 ). It has been reported that the entry of Germiston and LaCrosse viruses, two other Orthobunyaviruses , is promoted by DC-SIGN (Dendritic cell-specific intracellular adhesion molecule-3-grabbing non integrin) receptors, which is seen in other Bunyaviruses, like the Phleboviruses ( 75 ). These receptors are found in dermal dendritic cells and may play a role in viral entry into mammalian cells following transmission by an arthropod bite ( 62 , 74 ).…”

Section: Classification Genomic Characteristics and Replication In mentioning

confidence: 99%

A Review of Bunyamwera, Batai, and Ngari Viruses: Understudied Orthobunyaviruses With Potential One Health Implications

Dutuze

Nzayirambaho

et al. 2018

Front. Vet. Sci.

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Bunyamwera (BUNV), Batai (BATV), and Ngari (NRIV) are mosquito-borne viruses of the Bunyamwera serogroup in the Orthobunyavirus genus of the Bunyaviridae family. These three viruses have been found to cause disease in both livestock animals, avian species, and humans. Thus, these viruses pose a potential threat to human public health, animal health, and food security. This is especially the case in the developing nations, where BUNV and NRIV are found, mainly in Africa. BUNV and BATV are fairly well characterized, while NRIV is not well characterized owing to only sporadic detection in human and animal populations in Africa. Reassortment is common among bunyaviruses, but NRIV is believed to be the only natural reassortant of the Bunyamwera serogroup. It resulted from a combination of BUNV S and L segments and the BATV M segment. This indicates at least some level co-circulation of BUNV and BATV, which have no historically been reported to overlap in geographic distributions. But as these viruses are undercharacterized, there remains a gap in the understanding of how such reassortment could occur, and the consequences of such. Due to their combined wide range of hosts and vectors, geographic distributions, potential severity of associated diseases, and potential for transmissibility between vertebrate hosts, these viruses represent a significant gap in knowledge with important One Health implications. The goal of this review is to report available knowledge of and identify potential future directions for study of these viruses. As these are collectively understudied viruses, there is a relative paucity of data; however, we use available studies to discuss different perspectives in an effort to promote a better understanding of these three viruses and the public and One Health threat(s) they may pose.

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N-Glycans on the Rift Valley Fever Virus Envelope Glycoproteins Gn and Gc Redundantly Support Viral Infection via DC-SIGN

Cited by 31 publications

References 44 publications

Global aspects of viral glycosylation

Global aspects of viral glycosylation

The evolutionary dynamics of Oropouche Virus (OROV) in South America

A Review of Bunyamwera, Batai, and Ngari Viruses: Understudied Orthobunyaviruses With Potential One Health Implications

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