Epstein-Barr virus tissue tropism: a major determinant of immunopathogenesis

Hutt-Fletcher, Lindsey

doi:10.1007/bf00201463

Cited by 3 publications

(2 citation statements)

References 107 publications

(83 reference statements)

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“…EBV infects greater than 90% of the human population world-wide, infection usually occurring early in childhood, but in the Western world infection is frequently delayed tmtil adolescence when there is a 50% chance of infectious mononucleosis occurring. EBV can infect only B lymphocytes and certain classes of epithelial cell by binding to the complement receptor CR2 of B lymphocytes and a similar molecule on epithelial cells (Hutt-Fletcher, 1991). The mode of infection is by horizontal transmission through an oral portal of entry leading to infection of epithelial cells in the oropharynx.…”

Section: Vaccinating Humansmentioning

confidence: 99%

New Generation Vaccines

Gregoriadis¹,

McCormack²,

Allison³

et al. 1993

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The electronic index to the NATO ASI Series provides full bibliographical references (with keywords and/or abstracts) to more than 30,000 contributions from international scientists published in aII sections of the NATO ASI Series. Access to the NATO-PCO-DATA SASE is possible in two ways:-via online FILE 128 (NATO-PCO-DATA BASE) hosted by ESRIN, PREFACEIt is widely accepted that vaccination still renains the best answer to ITDst infectious diseases. Recently, vaccine developnent has been greatly facilitated by advances in ITDlecular and cell biology which have laid the foundations of a new generation of vaccines. '!hese are exemplified by submit vaccines produced through gene cloning and synthetic peptides mimicking snall regions of proteins on the outer coat of viruses and capable of eliciting virus neutralizing antibodies. However, submit and peptide vaccines are only weakly or non-inmmogenic in the absence of immunological adjuvants. The latter are a diverse array of agents that augment specific cell-mediated immune responses to the antigens and the formation of protective antibodies.'!his book contains the proceedings of the 3rd NATO Advanced Studies Institute (ASI) "New-Generation vaccines: '!he Role of Basic Irrmmology" held at Cape Sounion Beach, Greece, during 24 June-5 July, 1992. It deals with recent developnents in the understanding of inmmity at the ITDlecular and cellular levels and the application of such knowledge in the search for novel inmmological adjuvants and the fonnulation of new-generation vaccines for experimental and clinical use. We express our appreciation to Professor K. Dalsgaard and H. Snippe for their cooperation in planning the ASI and to Mrs. Concha Perring for her excellent production of the manuscripts. '!he ASI was held tmder the sponsorship of NATO Scientific Affairs Division and generously co-sponsored by SrnithKline Beecham Pharmaceuticals (Fhiladelp,.ia).

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Section: Vaccinating Humansmentioning

confidence: 99%

New Generation Vaccines

Gregoriadis¹,

McCormack²,

Allison³

et al. 1993

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“…Herpesviruses are complex pathogens that typically encode at least 10 glycoproteins (1,2). These glycoproteins transport the virus between cells and between hosts, and help to determine its tropism.…”

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confidence: 99%

Intercellular Gamma‐Herpesvirus Dissemination Involves Co‐Ordinated Intracellular Membrane Protein Transport

May

Lima

Colaco

et al. 2005

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The murine gamma-herpesvirus-68 (MHV-68) ORF27 encodes gp48, a type 2 transmembrane glycoprotein that contributes to intercellular viral spread. Gp48 is expressed on the surface of infected cells but is retained intracellularly after transfection. In this study, we show that the multimembrane spanning ORF58 gene product is both necessary and sufficient for gp48 to reach the cell surface. ORF58-deficient MHV-68 expressed ORF27 in normal amounts, but retained it in the endoplasmic reticulum (ER). Transfected ORF27 also remained in ER, whereas green fluorescent protein-tagged ORF58 localized to the ER and trans-Golgi network. When ORF27 and ORF58 were co-transfected, they formed a protein complex and reached the cell surface. Surprisingly, ORF58 rather than ORF27 mediated cell binding via a small extracellular loop. The heavily glycosylated ORF27 component of the complex may, therefore, act mainly to protect this loop against antibody. The interdependent transport of ORF27 and ORF58 transport ensures that such protection is always present. Herpesviruses are complex pathogens that typically encode at least 10 glycoproteins (1,2). These glycoproteins transport the virus between cells and between hosts, and help to determine its tropism. Those that mediate viral membrane fusion -the gH/gL heterodimer and gB (3-5) -are conserved between the major herpesvirus subfamilies and essential for infectivity. Subfamily-specific glycoproteins, by contrast, are often dispensable for viral propagation in vitro. Nevertheless, they are likely to play important roles in vivo. The restricted species tropisms of the human gammaherpesviruses -Epstein-Barr virus (EBV) and the Kaposi's sarcoma-associated herpesvirus (KSHV) -and the difficulty of propagating them by lytic replication have limited our understanding of some gamma-herpesvirus-specific glycoproteins. Cloned glycoprotein genes can be studied in isolation, but their functions are often integral to viral replication and can be hard to appreciate outside this context. One solution is to study the homologous genes of more tractable, related viruses. The murine gamma-herpesvirus-68 (MHV-68) (6-10) behaves as a natural pathogen in conventional mice and grows to high titre in a variety of cultured cell lines. It is, therefore, useful for identifying the functions of shared gamma-herpesvirus genes. Our focus with MHV-68 has been on defining what immune evasion contributes to host colonization (11). Because viral glycoproteins must confront host antibody, their expression is inseparable from immune evasion. We (12-16) and others (17,18) have, therefore, begun to define the functions of the MHV-68 glycoproteins.We recently identified the product of the MHV-68 ORF27, which has homologues in both EBV (BDLF2) and KSHV (ORF27), as a 48-kDa type 2 transmembrane glycoprotein (gp48) that contributes to intercellular viral spread (16). Gp48 is expressed on the plasma membrane of infected cells. However, transfected ORF27 remains entirely intracellular. Thus gp48 requires other viral gene product...

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Progress in the Development of Epstein-Barr Virus Vaccines

Morgan

1993

New Generation Vaccines

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Epstein-Barr virus tissue tropism: a major determinant of immunopathogenesis

Cited by 3 publications

References 107 publications

New Generation Vaccines

New Generation Vaccines

Intercellular Gamma‐Herpesvirus Dissemination Involves Co‐Ordinated Intracellular Membrane Protein Transport

Progress in the Development of Epstein-Barr Virus Vaccines

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