Fatal pulmonary disease and encephalic complication in a man with HSV-1 Infection: A case report

Astuto, Marinella; Palermo, Concetta; Costanzo, Carmela Maria; Ettorre, G; Palmucci, Stefano; Franchina, Concetta; Russo, Raffaela; Valastro, Pietro; Timpanaro, Valentina; Scalia, Guido

doi:10.1016/j.jcv.2013.11.006

Cited by 7 publications

(8 citation statements)

References 13 publications

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“…We identified 122 novel O-glycosylation sites on 28 HCMV proteins, including gB, gH, gL, gN, and gO (Table 2 and supplemental Data Sets S1 and S4). Most of the identified glycoproteins had a relatively small number of sites (1)(2)(3)(4)(5)(6)(7)(8), with the exception of RL12 and UL22A, in which we found 18 and 14 sites, respectively. Five HCMV envelope glycoproteins are indispensable for replication: gB, gH, gL, gM, and gN (57).…”

Section: Mapping O-glycosites In Human Herpesvirusesmentioning

confidence: 56%

Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus

Bagdonaite

Nordén

Joshi

et al. 2016

Journal of Biological Chemistry

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Herpesviruses are among the most complex and widespread viruses, infection and propagation of which depend on envelope proteins. These proteins serve as mediators of cell entry as well as modulators of the immune response and are attractive vaccine targets. Although envelope proteins are known to carry glycans, little is known about the distribution, nature, and functions of these modifications. This is particularly true for O-glycans; thus we have recently developed a "bottom up" mass spectrometry-based technique for mapping O-glycosylation sites on herpes simplex virus type 1. We found wide distribution of O-glycans on herpes simplex virus type 1 glycoproteins and demonstrated that elongated O-glycans were essential for the propagation of the virus. Here, we applied our proteome-wide discovery platform for mapping O-glycosites on representative and clinically significant members of the herpesvirus family: varicella zoster virus, human cytomegalovirus, and Epstein-Barr virus. We identified a large number of O-glycosites distributed on most envelope proteins in all viruses and further demonstrated conserved patterns of O-glycans on distinct homologous proteins. Because glycosylation is highly dependent on the host cell, we tested varicella zoster virus-infected cell lysates and clinically isolated virus and found evidence of consistent O-glycosites. These results present a comprehensive view of herpesvirus O-glycosylation and point to the widespread occurrence of O-glycans in regions of envelope proteins important for virus entry, formation, and recognition by the host immune system. This knowledge enables dissection of specific functional roles of individual glycosites and, moreover, provides a framework for design of glycoprotein vaccines with representative glycosylation.

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Section: Mapping O-glycosites In Human Herpesvirusesmentioning

confidence: 56%

Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus

Bagdonaite

Nordén

Joshi

et al. 2016

Journal of Biological Chemistry

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“…Using herpesviruses as a model system, we have applied the same method for defining the O-glycoproteomes of other members of Herpesviridae family-HSV-2, VZV, HCMV and EBV Iversen et al 2016). The wide occurrence, associated complications and shortage of prophylactic measures make herpesviruses a relevant model system to analyze O-glycans and their importance in viral life cycle (Vazquez et al 2001;Cohen et al 2006;Adjei et al 2008;Kramer et al 2008;Oxman 2010;Shiley and Blumberg 2010;Lopo et al 2011;Sauerbrei et al 2011;Levine et al 2012;van Rijckevorsel et al 2012;Astuto et al 2013;Conde-Glez et al 2013;Fishman 2013;Gorfinkel et al 2013;Odland et al 2013;Pembrey et al 2013;Rowe et al 2013;Awasthi and Friedman 2014;Bradley et al 2014;Fu et al 2014;Sabugo et al 2014 Shaiegan et al 2015). In addition, the large proteomes of herpesviruses highlight the benefits of global viral O-glycoproteomics.…”

Section: Global O-glycoproteomicsmentioning

confidence: 99%

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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“…Diseases associated with herpesviruses are often easily resolved in immunocompetent individuals; however, they pose a serious health threat to those with a compromised immune system . Furthermore, in rare cases, herpesvirus infections can lead to severe life‐threatening complications . In addition, gammaherpesviruses have the potential for malignant transformation of lymphocytes and epithelia .…”

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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Fatal pulmonary disease and encephalic complication in a man with HSV-1 Infection: A case report

Cited by 7 publications

References 13 publications

Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus

Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus

Global aspects of viral glycosylation

Viral glycoproteomes: technologies for characterization and outlook for vaccine design

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