Epstein-Barr Virus Recombinant Lacking Expression of Glycoprotein gp150 Infects B Cells Normally but Is Enhanced for Infection of Epithelial Cells

Borza, Corina M.; Hutt-Fletcher, Lindsey

doi:10.1128/jvi.72.9.7577-7582.1998

Cited by 42 publications

(17 citation statements)

References 33 publications

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“…Furthermore, the HSV-2 and VZV orthologs were also found to be O-glycosylated (Zezulak and Spear 1983;Bagdonaite et al 2016). Similarly, other mucin-like region-containing proteins such as HSV-1 gI, HSV-2 gG, EBV gp150 and gp350 have been shown to accommodate high density of O-glycosylation, and the types of O-glycan structures were identified for some of these proteins Nolan and Morgan 1995;Borza and Hutt-Fletcher 1998;Norberg et al 2007). The conserved viral fusion effector gB has been shown or predicted to be O-glycosylated in all herpesvirus subfamilies (Serafini-Cessi, Dall'Olio, Scannavini, Costanzo et al 1983;Gong et al 1987;Montalvo and Grose 1987;Britt and Vugler 1989).…”

Section: Global O-glycoproteomicsmentioning

confidence: 91%

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: Global O-glycoproteomicsmentioning

confidence: 91%

Global aspects of viral glycosylation

2018

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“…However, low-efficiency CR2-independent EBV infection of established human epithelial cell lines, previously deemed resistant, has been convincingly demonstrated by infecting with a viral genome carrying a selective marker (Yoshiyama et al, 1997;Imai et al, 1998). Using recombinant EBV in which a neomyocin-resistance cassette was inserted into the BDLF3 open reading frame (Borza and Hutt-Fletcher, 1998), we derived a uniformly infected MDCK-pR4 cell population from apically exposed cells selected in medium containing G418 (data not shown). Together, these results are consistent with the notion of a naturally expressed coreceptor distributed apically that functions synergistically with transfected CR2.…”

Section: Efficiency Of Infection At Apical Versus Basolateral Surfacesmentioning

confidence: 95%

“…Stock EBV preparations transformed 50% of primary lymphocyte cultures at a dilution of 10 Ϫ4 in the lymphocyte transformation assay (Moss and Pope, 1972). Recombinant Akata virus bearing the neomycin-resistant cassette (gift of L. Hutt-Fletcher, University of Missouri at Kansas City; Borza and Hutt-Fletcher, 1998) was produced as above for use in a single experiment.…”

Section: Cell Lines and Virusmentioning

confidence: 99%

Patterned Entry and Egress by Epstein–Barr Virus in Polarized CR2-Positive Epithelial Cells

et al. 2000

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In polarized epithelium direction of viral entry and release correlates with proclivity of a virus to establish local versus systemic infection. The Epstein-Barr virus (EBV), whose principal tissue reservoir is B lymphocytes, also has disease manifestations in epithelium, suggesting intertissue spread potentially influenced by epithelial cell polarity. We stably transfected the B lymphocyte EBV receptor (CR2/CD21) into Madin-Darby canine kidney (MDCK) epithelial cells used extensively to study effects of cell polarity on infection by both DNA and RNA viruses. CR2/CD21 was detected on both apical and basolateral surfaces of polarized MDCK cells, with predominant expression basolaterally. However, infectivity was up to four-fold greater apically, suggesting that endogenous cell surface molecules, sorted asymmetrically onto polarized plasma membranes, may be involved in EBV entry into MDCK cells. EBV gp350/220, a replicative cycle glycoprotein added to the virus envelope on egress through the cell membrane, was immunolocalized by confocal microscopy to basolateral cell surfaces only. Apical entry of EBV with subsequent basolateral release of newly replicated virus favors systemic infection by viral dissemination to underlying lymphocytic aggregations. Under conditions of long-term culture, latent EBV was not stably maintained in these cells, suggesting that the epithelial phase of acute EBV infection may be transient.

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“…Moreover, specific N‐glycosites in VZV and HSV‐2 have been identified, which are important for binding and entry, respectively . Quite a few attachment proteins such as HSV‐1 gC, HSV‐2 gG, EBV gp150, and gp350 contain mucin‐like regions and have been shown to accommodate high density of O‐glycosylation . For HSV‐1 gC and EBV gp350, specific glycosites have been identified by tandem MS .…”

Section: Glycosylation Analysis Of Viral Glycoproteinsmentioning

confidence: 99%

Viral glycoproteomes: technologies for characterization and outlook for vaccine design

et al. 2018

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It has long been known that surface proteins of most enveloped viruses are covered with glycans. It has furthermore been demonstrated that glycosylation is essential for propagation and immune evasion for many viruses. The recent development of high-resolution mass spectrometry techniques has enabled identification not only of the precise structures but also the positions of such post-translational modifications on viruses, revealing substantial differences in extent of glycosylation and glycan maturation for different classes of viruses. In-depth characterization of glycosylation and other post-translational modifications of viral envelope glycoproteins is essential for rational design of vaccines and antivirals. In this Review, we provide an overview of techniques used to address viral glycosylation and summarize information on glycosylation of enveloped viruses representing ongoing public health challenges. Furthermore, we discuss how knowledge on glycosylation can be translated to means to prevent and combat viral infections.

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Epstein-Barr Virus Recombinant Lacking Expression of Glycoprotein gp150 Infects B Cells Normally but Is Enhanced for Infection of Epithelial Cells

Cited by 42 publications

References 33 publications

Global aspects of viral glycosylation

Global aspects of viral glycosylation

Patterned Entry and Egress by Epstein–Barr Virus in Polarized CR2-Positive Epithelial Cells

Viral glycoproteomes: technologies for characterization and outlook for vaccine design

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