Distribution of epitopes within the amino acid sequence of the Epstein--Barr virus major envelope glycoprotein, gp340, recognized by hyperimmune rabbit sera

Pither, Richard; Nolan, Lesley A; Tarlton, John F; Walford, J.A.; Morgan, Andrew

doi:10.1099/0022-1317-73-6-1409

Cited by 9 publications

(3 citation statements)

References 35 publications

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“…These results suggest that HABPs 11382, 11389, and 11416 are capable of inducing antibodies inhibiting EBV binding of host cells in which EBV invasion is mediated by gp350/ 220. These results agree with other reports showing that monoclonal and human neutralizing antibodies recognize epitopes between gp350 residues 65-174 and 236 -327 in which HABPs 11382 and 11389, respectively, are located (5,45,49,50).…”

Section: Figure 4 the Effect Of Anti-habp Antibodies On Ebv Binding supporting

confidence: 83%

“…CR2(ϩ) HABPs 11381, 11382, 11388, 11389, and 11394 were located in the gp350/220 576-mer N-terminal fragment, containing part of the Raji-binding region, because this fragment bound to Raji cells in a similar way as to the entire gp350/gp220 (5,48). HABPs 11415 and 11416 were located in the C-terminal region, specifically in the immunodominant region recognized by anti-EBV human neutralizing antibodies (49,50). The CR2(ϩ) HABPs showed saturable binding, having a finite number of HABP-binding sites per Raji cell, thus supporting the idea of specific binding receptors.…”

Section: Discussionmentioning

confidence: 70%

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Identification of Three gp350/220 Regions Involved in Epstein-Barr Virus Invasion of Host Cells

Urquiza

López

Patino

et al. 2005

Journal of Biological Chemistry

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Epstein-Barr virus (EBV) invasion of B-lymphocytes involves Epstein-Barr virus (EBV)2 invades B-lymphocytes through molecular interactions involving the EBV gp350/220 protein. It is known that gp350 binds to B-lymphocyte CR2 (known as C3d receptor) with a 3.2 nM affinity constant (12 nM affinity has been determined for B-lymphocyte surface) (1, 2). This simple 1:1 interaction is involved in adsorption, capping, and EBV endocytosis and is considered to be a primary determinant of EBV tissue tropism (3-5). The CR2 region binding to gp350 overlaps the CR2 region binding to C3dg. The gp350 N-terminal region contains part of the B-lymphocyte binding domain (5).The gp350 21 EDPGFFNVE 29 peptide, having significant homology with C3d-amino acid sequences (6), binds to purified CR2 and to CR2(ϩ) but not to CR2(Ϫ) B-and T-lymphoblastoid cell lines; this peptide coupled to BSA inhibits CR2 binding to EBV and gp350 (7). This peptide inhibits C3dg binding to B-cells (as well as EBV) and also inhibits C3-induced Raji cell proliferative response (7,8).However, the 470-mer N-terminal recombinant protein and gp220, containing this peptide sequence, present single-component binding, whereas gp350/220 presents a higher affinity two-component binding to CR2 (5, 9) and inhibits only 50% of EBV binding and EBV infection of Raji cells (5) (5). On the other hand, the C3dg region (homologous to this gp350 peptide) is not in contact with CR2 in the reported complex structure (10). It is thus very likely that other gp350/220 regions are involved in EBV binding to B-lymphocytes.The gp350/220 region containing the epitope recognized by neutralizing monoclonal antibody 72A1 is one of the most important regions involved in gp350/220 binding to B-lymphocyte CR2, because the mAb 72A1 Fab fragment inhibits EBV binding and invasion of host cells (5, 11). Moreover, mAb 72A1 inhibits EBV invasion of monocytes (12), neutrophils (13), and T-cells (14). Anti-gp350/220 mAb 72A1 also inhibits interleukin-6 (IL-6) protein synthesis induced in PBLs by gp350/220 binding to CR2 (15); it also inhibits EBV invasion of B-lymphocytes (5). It is known that the gp350/220 region involved in EBV invasion of host cells is recognized by this monoclonal antibody; however, its precise localization remains unknown. The purpose of this work was thus to identify B-lymphocyte binding sequences that are involved in EBV virus infection of B-lymphocytes. MATERIALS AND METHODSPeptide Synthesis-Forty-six peptides, covering the total length of EBV gp350-reported sequence (16), were synthesized by the solid phase method (17) with N-terminal t-Boc-protected amino acids. Peptides were cleaved by a low-high hydrogen fluoride protocol (18). These peptides were analyzed by mass spectrometry and reverse-phase high performance liquid chromatography. Synthesized peptide sequences are shown in Fig. 1. Tyrosine (Y) was C-terminally added, allowing those peptides not containing this amino acid to be radiolabeled.Lymphoblastoid Cell Line Cultures-The cloned Raji (19), Ramos (20), and P3HR-1 ...

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Section: Figure 4 the Effect Of Anti-habp Antibodies On Ebv Binding supporting

confidence: 83%

Section: Discussionmentioning

confidence: 70%

Identification of Three gp350/220 Regions Involved in Epstein-Barr Virus Invasion of Host Cells

Urquiza

López

Patino

et al. 2005

Journal of Biological Chemistry

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“…modified vaccinia virus Ankara, MVA), mammalian DNA plasmids or plant-based plastids (32,36,37). In the context of these new formulations, debates continue concerning (i) the most appropriate protein target for an EBV vaccine, (ii) the focus of vaccines on B-cell and/or Tcell responses, and (iii) the relative importance of representing lytic or latent stages of infection in EBV vaccines (21,28,(33)(34)(35)(36)(38)(39)(40).…”

Section: Past and Current Endeavors To Develop An Ebv Vaccinementioning

confidence: 99%

Epstein-Barr virus vaccine development: a lytic and latent protein cocktail

et al. 2008

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Epstein-Barr Virus (EBV) is the causative agent of acute infectious mononucleosis and associates with malignancies such as Burkitt lymphoma, nasopharyngeal carcinoma, and non-Hodgkin's lymphoma. Additionally, EBV is responsible for B-lymphoproliferative disease in the context of HIV-infection, genetic immunodeficiencies and organ/stem-cell transplantation. Here we discuss past and current efforts to design an EBV vaccine. We further describe preliminary studies of a novel cocktail vaccine expressing both lytic and latent EBV proteins. Specifically, a tetrameric vaccinia virus (VV) -based vaccine was formulated to express the EBV lytic proteins gp350 and gp110, and the latent proteins EBNA-2 and EBNA-3C. In a proof-of-concept study, mice were vaccinated with the individual or mixed VV. Each of the passenger genes was expressed in vivo at levels sufficient to elicit binding antibody responses. Neutralizing gp350-specific antibodies were also elicited, as were EBV-specific T-cell responses, following inoculation of mice with the single or mixed VV. Results encourage further development of the cocktail vaccine strategy as a potentially powerful weapon against EBV infection and disease in humans.

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Progress in the Development of Epstein-Barr Virus Vaccines

Morgan

1993

New Generation Vaccines

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Distribution of epitopes within the amino acid sequence of the Epstein--Barr virus major envelope glycoprotein, gp340, recognized by hyperimmune rabbit sera

Cited by 9 publications

References 35 publications

Identification of Three gp350/220 Regions Involved in Epstein-Barr Virus Invasion of Host Cells

Identification of Three gp350/220 Regions Involved in Epstein-Barr Virus Invasion of Host Cells

Epstein-Barr virus vaccine development: a lytic and latent protein cocktail

Progress in the Development of Epstein-Barr Virus Vaccines

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