Difference in viral binding between two epstein‐barr virus substrains to a spectrum of receptor‐positive target cells

Wells, Alan; Koide, Naoki; Klein, George

doi:10.1002/ijc.2910270308

Cited by 11 publications

(10 citation statements)

References 28 publications

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“…HABPs 11402, 11403, and 11404 contain this reported epitope (underlined in the following: SAVTTPTPNATSPTLGKTSPT); HABPs 11401 and 11405 contain only part of this epitope (AVTTPTPNATSPT). The differences in cell binding tropism between B95-8 EBV (containing the repeat region) and P3HR-1 EBV (which does not contain this region) could be due to this binding region (46,47).…”

Section: Discussionmentioning

confidence: 99%

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: Discussionmentioning

confidence: 99%

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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“…The transforming prototype B9.5-8 and P3HR-1 viruses were shown to bind to the same receptors on lymphoma cell lines [28]. When resting B cells were exposed to P3HR-1 virus first and thereafter to B95-8 virus the transformation was abrogated [32].…”

Section: Discussionmentioning

confidence: 99%

“…Virus binding and uptake assays were performed as described [28]. One million tonsillar B cells were incubated for 2 h at 37°C in the presence of 5000 cpm [3H]thymidine ([3H]dThd)labeled virus in a total volume of 1 ml medium with 10% fetal calf serum (FCS).…”

Section: Virus Binding and Uptakementioning

confidence: 99%

B cell activation by the nontransforming P3HR‐1 substrain of the Epstein‐Barr virus (EBV)

Hu¹,

Åman²,

Masucci³

et al. 1986

Eur J Immunol

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The P3HR-1 substrain of Epstein-Barr virus does not transform B cells. This defect is known to be determined by the loss of the coding sequence for the nuclear antigen EBNA-2. The virus can attach to and enter resting B cells. The initial events after EBV infection are reminiscent of those induced by polyclonal B cell activators. Similar to the effect of these, P3HR-1 virus lowers membrane IgD expression on B cells and abrogates the transient elevation of activation markers BB-1 and LB-1 induced by the culture conditions. An important event of B cell activation is the acquisition of competence to respond to specific growth factors produced by T cells. This was induced by the P3HR-1 virus. The infected B cells had elevated [3H]thymidine incorporation when exposed to the supernatant of PHA-treated T cells. The EBV receptor is identical with the complement receptor CR2. Ligand binding to CR2 has been shown both with mouse and human B cells to deliver certain activation signals. Therefore, it is possible that the early step of activation by EBV is initiated through the binding to the receptor and is thus a cell surface event.

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confidence: 99%

The Epstein-Barr Virus Receptor is Distinct from the C3 Receptor

Koide

Stein

Gerdes

et al. 1983

Journal of General Virology

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SUMMARYPolyvalent serum directed against C3 receptors was employed in an attempt to block Epstein-Barr virus (EBV) binding to virus receptor-containing cell lines. The serum eliminated 90 ~ of virus binding to Daudi and B JAB, lines which express only the C3d receptor. Raji and Ramos cells, which express the C3d, C3b and C3bi receptors, still adsorbed 70 ~ of their virus capacity in the presence of excess antiserum. These effects were independent of the virus strain. In the light of previous reports, these data imply that, although the two receptors, EBV and C3d, are closely associated, the binding sites of EBV and complement are distinct. Additionally, an unusual EBV substrain-specific receptor found on U698 and P3HR-1/ASNP lines was shown to be independent of complement receptors.

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Difference in viral binding between two epstein‐barr virus substrains to a spectrum of receptor‐positive target cells

Cited by 11 publications

References 28 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

B cell activation by the nontransforming P3HR‐1 substrain of the Epstein‐Barr virus (EBV)

The Epstein-Barr Virus Receptor is Distinct from the C3 Receptor

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