Papain solubilization of the Epstein-Barr virus-induced membrane antigen.

1978 ◽  
Vol 28 (1) ◽  
pp. 344-351 ◽  
Author(s):  
G R Pearson ◽  
L F Qualtiere
Keyword(s):  
Epstein Barr Virus ◽  
Induced Membrane ◽  
Barr Virus ◽  
Epstein Barr

scholarly journals Modulation of Epstein-Barr Virus Glycoprotein B (gB) Fusion Activity by the gB Cytoplasmic Tail Domain

mBio ◽  
2013 ◽  
Vol 4 (1) ◽  
Author(s):  
Nicholas J. Garcia ◽  
Jia Chen ◽  
Richard Longnecker
Keyword(s):  
Membrane Fusion ◽  
Epstein Barr Virus ◽  
Cytoplasmic Tail ◽  
Host Cells ◽  
Glycoprotein B ◽  
Tail Domain ◽  
Induced Membrane ◽  
Barr Virus ◽  
Cellular Expression ◽  
Epstein Barr

ABSTRACTEpstein-Barr virus (EBV), along with other members of the herpesvirus family, requires a set of viral glycoproteins to mediate host cell attachment and entry. Viral glycoprotein B (gB), a highly conserved glycoprotein within the herpesvirus family, is thought to be the viral fusogen based on structural comparison of EBV gB and herpes simplex virus (HSV) gB with the postfusion crystal structure of vesicular stomatitis virus fusion protein glycoprotein G (VSV-G). In addition, mutational studies indicate that gB plays an important role in fusion function. In the current study, we constructed a comprehensive library of mutants with truncations of the C-terminal cytoplasmic tail domain (CTD) of EBV gB. Our studies indicate that the gB CTD is important in the cellular localization, expression, and fusion function of EBV gB. However, in line with observations from other studies, we conclude that the degree of cell surface expression of gB is not directly proportional to observed fusion phenotypes. Rather, we conclude that other biochemical or biophysical properties of EBV gB must be altered to explain the different fusion phenotypes observed.IMPORTANCEEpstein-Barr virus (EBV), like all enveloped viruses, fuses the virion envelope to a cellular membrane to allow release of the capsid, resulting in virus infection. To further characterize the function of EBV glycoprotein B (gB) in fusion, a comprehensive library of mutants with truncations in the gB C-terminal cytoplasmic tail domain (CTD) were made. These studies indicate that the CTD of gB is important for the cellular expression and localization of gB, as well as for the function of gB in fusion. These studies will lead to a better understanding of the mechanism of EBV-induced membrane fusion and herpesvirus-induced membrane fusion in general, which will ultimately lead to focused therapies guided at preventing viral entry into host cells.

Immunoglobulin a Antibody to Epstein-Barr Viral Antigens and Prognosis in Nasopharyngeal Carcinoma

1980 ◽  
Vol 88 (1) ◽  
pp. 52-57 ◽  
Author(s):  
Gregory D. Mathew ◽  
Louis F. Qualtiere ◽  
H. Bryan Neel ◽  
Gary R. Pearson
Keyword(s):  
Nasopharyngeal Carcinoma ◽  
Epstein Barr Virus ◽  
Immunoglobulin A ◽  
Antibody Dependent Cellular Cytotoxicity ◽  
Induced Membrane ◽  
Barr Virus ◽  
Iga Antibodies ◽  
Adcc Assay ◽  
Membrane Antigens ◽  
Epstein Barr

IgA immunoglobulin fractions containing antibodies to Epstein-Barr virus (EBV)-induced membrane antigens were isolated from the sera of two patients with nasopharyngeal carcinoma (NPC), from one non-NPC patient, and from three persons with sera negative for IgA antibodies. IgA antibodies were not cytotoxic against cells expressing EBV-induced membrane antigens in the antibody-dependent cellular cytotoxicity (ADCC) assay. However, IgA antibodies blocked IgG-mediated ADCC, which indicated that these antibodies could serve as a blocking “factor” in patients with disease and, therefore, were potentially detrimental to the host.

scholarly journals A soluble form of Epstein-Barr virus gH/gL inhibits EBV-induced membrane fusion and does not function in fusion

Virology ◽  
2013 ◽  
Vol 436 (1) ◽  
pp. 118-126 ◽  
Author(s):  
Cynthia L. Rowe ◽  
Sarah A. Connolly ◽  
Jia Chen ◽  
Theodore S. Jardetzky ◽  
Richard Longnecker
Keyword(s):  
Membrane Fusion ◽  
Epstein Barr Virus ◽  
Soluble Form ◽  
Induced Membrane ◽  
Barr Virus ◽  
Epstein Barr

scholarly journals Mutational Analyses of Epstein-Barr Virus Glycoprotein 42 Reveal Functional Domains Not Involved in Receptor Binding but Required for Membrane Fusion

2004 ◽  
Vol 78 (11) ◽  
pp. 5946-5956 ◽  
Author(s):  
Amanda L. Silva ◽  
Jasmina Omerović ◽  
Theodore S. Jardetzky ◽  
Richard Longnecker
Keyword(s):  
Membrane Fusion ◽  
Epstein Barr Virus ◽  
Mutational Analysis ◽  
Class Ii ◽  
Hla Class Ii ◽  
Hydrophobic Pocket ◽  
Induced Membrane ◽  
Lectin Domain ◽  
Barr Virus ◽  
Epstein Barr

ABSTRACT Epstein-Barr virus (EBV) is a human gammaherpesvirus associated with malignancies of both epithelial and lymphoid origin. Efficient infection of the latent host reservoir B lymphocytes involves the binding of glycoproteins gp350/220 for initial attachment, followed by the concerted action of gH, gL, gB, and gp42 for membrane fusion. The type II membrane protein gp42 is required for infection of B cells and assembles into a complex with gH and gL. The cellular host receptor for gp42, class II human leukocyte antigen (HLA), has been structurally verified by crystallization analyses of gp42 bound to HLA-DR1. Interestingly, the crystal structure revealed a hydrophobic pocket consisting of many aromatic and aliphatic residues from the predicted C-type lectin domain of gp42 that in other members of the C-type lectin family binds major histocompatibility complex class I or other diverse ligands. Although the hydrophobic pocket does not bind HLA class II, mutational analyses presented here indicate that this domain is essential for EBV-induced membrane fusion. In addition, mutational analysis of the region of gp42 contacting HLA class II in the gp42-HLA-DR1 cocrystal confirms that this region interacts with HLA class II and that this interaction is also important for EBV-induced membrane fusion.

scholarly journals The KGD Motif of Epstein-Barr Virus gH/gL Is Bifunctional, Orchestrating Infection of B Cells and Epithelial Cells

mBio ◽  
2012 ◽  
Vol 3 (1) ◽  
Author(s):  
Jia Chen ◽  
Cynthia L. Rowe ◽  
Theodore S. Jardetzky ◽  
Richard Longnecker
Keyword(s):  
Amino Acids ◽  
B Cells ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Membrane Fusion ◽  
Epstein Barr Virus ◽  
Cell Infection ◽  
Induced Membrane ◽  
Barr Virus ◽  
Epstein Barr

ABSTRACTEpstein-Barr virus (EBV), a member of the herpesvirus family, is the causative agent of common human infections and specific malignancies. EBV entry into target cells, including B cells and epithelial cells, requires the interaction of multiple virus-encoded glycoproteins. Glycoproteins H and L (gH/gL) cooperate with glycoprotein B (gB) to mediate fusion of the viral envelope with target cell membranes. Both the gH/gL complex and gB are required for fusion, whereas glycoprotein 42 (gp42) acts as a tropism switch and is required for B cell infection and inhibits epithelial cell infection. Our previous studies identified a prominent KGD motif located on the surface of gH/gL. In the current study, we found that this motif serves as a bifunctional domain on the surface of gH/gL that directs EBV fusion of B cells and epithelial cells. Mutation of the KGD motif to AAA decreased fusion with both epithelial and B cells and reduced the binding of gH/gL to epithelial cells and to gp42. We also demonstrate that deletion of amino acids 62 to 66 of gp42 selectively reduces binding to wild-type gH/gL, but not the KGD mutant, suggesting that the KGD motif of gH/gL interacts with the N-terminal amino acids 62 to 66 of gp42.IMPORTANCEEpithelial and B cells are the major targets of Epstein-Barr virus (EBV) infection in the human host. EBV utilizes different glycoprotein complexes to enter these cell types. For B cell fusion, EBV uses complexes containing gp42, gH/gL, and gB, whereas just gH/gL and gB are required for epithelial cell fusion. In the current study, a bifunctional domain consisting of a prominent KGD motif on the surface of the gH/gL structure was identified; this domain affects interactions with gp42 or epithelial receptors, ultimately dictating with which cell type virus-induced fusion can occur. These studies will lead to a better understanding of the mechanism of EBV-induced membrane fusion and herpesvirus-induced membrane fusion in general.

A Quantitative Ultrastructural Study of Peripheral Blood Lymphocytes Containing Parallel Tubular Arrays in Epstein-Barr Virus and Cytomegalo-Virus Mononucleosis

1981 ◽  
Vol 39 ◽  
pp. 454-455
Author(s):  
C. M. Payne ◽  
P. M. Tennican
Keyword(s):  
Peripheral Blood ◽  
Lymphocyte Count ◽  
Epstein Barr Virus ◽  
Absolute Lymphocyte Count ◽  
Peripheral Blood Lymphocytes ◽  
Clinical State ◽  
Barr Virus ◽  
The Absolute ◽  
Epstein Barr ◽  
Tubular Arrays

In the normal peripheral circulation there exists a sub-population of lymphocytes which is ultrastructurally distinct. This lymphocyte is identified under the electron microscope by the presence of cytoplasmic microtubular-like inclusions called parallel tubular arrays (PTA) (Figure 1), and contains Fc-receptors for cytophilic antibody. In this study, lymphocytes containing PTA (PTA-lymphocytes) were quantitated from serial peripheral blood specimens obtained from two patients with Epstein -Barr Virus mononucleosis and two patients with cytomegalovirus mononucleosis. This data was then correlated with the clinical state of the patient.It was determined that both the percentage and absolute number of PTA- lymphocytes was highest during the acute phase of the illness. In follow-up specimens, three of the four patients' absolute lymphocyte count fell to within normal limits before the absolute PTA-lymphocyte count.In one patient who was followed for almost a year, the absolute PTA- lymphocyte count was consistently elevated (Figure 2). The estimation of absolute PTA-lymphocyte counts was determined to be valid after a morphometric analysis of the cellular areas occupied by PTA during the acute and convalescent phases of the disease revealed no statistical differences.

Sign in / Sign up

Export Citation Format

Share Document