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Chapter 4 : Molecular Biology of Epstein-Barr Virus

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Abstract:

This chapter discusses the pathologies associated with Epstein-Barr virus (EBV) infection. Infection with EBV usually occurs early in childhood and results in an asymptomatic infection. The majority of EBV isolates in Western communities are type 1, while type 2 EBV isolates appear to be largely restricted to equatorial Africa and Papua New Guinea. EBV, in contrast to herpes simplex virus (HSV), has a limited host range. This restriction is at least partially due to absence of the cellular receptor CD21 for EBV, which is also the receptor for the C3d component of complement. In addition to the essential components, EBV DNA encodes two genes that augment viral DNA replication. It is likely that the role of BHRF1 in EBV is to protect latently infected cells in vivo when they switch from latent infection to lytic infection when there is an absence of or very low Bcl2 expression, thus delaying apoptosis induced by lytic replication and ensuring productive lytic replication. EBV-transformed and latently infected lymphoblastoid cell lines (LCLs) express nine proteins and two small RNAs when grown in tissue culture. The proteins are expressed either in the nucleus (Epstein-Barr nuclear antigen [EBNA]) or in the plasma membrane (latent membrane protein [LMP]), and recent work has elucidated many of their functions. EBNA1 binds the 20-bp sequence as a homodimer. The structure of EBNA1 bound to DNA has been solved. Key elements in that structure determination are discussed in the chapter.

Citation: Longnecker R. 1998. Molecular Biology of Epstein-Barr Virus, p 135-174. In McCance D (ed), Human Tumor Viruses. ASM Press, Washington, DC. doi: 10.1128/9781555818289.ch4

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Figure 1

Viral genes expressed in cells latently infected with EBV. The four forms of latent gene expression that have been demonstrated in EBV-infected cell lines, tumor biopsies, and in vivo in normal humans latently infected are shown. The four different programs are under the control of two transcriptional units which vary the expression of the six EBNAs or three LMPs. (A) HI restriction enzyme map for the B95-8 sequence used to designate promoters and exons in each latent gene transcript. (B) The four different identified EBV latency programs. In latency I, EBNA 1 is expressed. In latency in immune-competent human hosts (In Vivo), the same EBNA1 transcript is expressed as well as LMP2A. In latency II, the previous proteins are expressed with the addition of LMP1 and LMP2B. Finally, in latency III all EBNAs and LMPs are expressed. The EBERs and BARFs ( ) are expressed in all types of EBV latencies. Solid boxes indicate exons, and arrows indicate sites of promoters. Letters indicate relevant HI restriction fragment.

Citation: Longnecker R. 1998. Molecular Biology of Epstein-Barr Virus, p 135-174. In McCance D (ed), Human Tumor Viruses. ASM Press, Washington, DC. doi: 10.1128/9781555818289.ch4
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Image of Figure 2
Figure 2

Structure of the region from the EBV viral genome. Shown are the 30-bp family of repeats, the 65-bp dyad symmetry, and the B95-8 consensus binding site for EBNA1 within the 30-bp family of repeats. Open boxes indicate EBNA1 binding regions.

Citation: Longnecker R. 1998. Molecular Biology of Epstein-Barr Virus, p 135-174. In McCance D (ed), Human Tumor Viruses. ASM Press, Washington, DC. doi: 10.1128/9781555818289.ch4
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Image of Figure 3
Figure 3

EBNA2 transactivation and EBNA3S modulation of RBPJ (CBF1) in EBV infection. EBNA2, an acidic transcriptional transactivator, is directed to EBNA2 response elements by interaction with sequence-specific host DNA binding proteins such as RBPJ. Once bound, EBNA2 stimulates transcription through interaction with components of TFIID. TFIID is a tightly associated protein complex of TBP (TATA binding protein) and eight or more TAFs (TBP-associated factors) ( ). EBNA2 interacts with TAF40, TFIIB, the p62 and p80 subunits of TFIIH, and p100. p100 associates with the p56 and p34 subunits of TFIIE ( ). The EBNA3S bind to RBPJ to modulate the expression of EBNA2-responsive promoters by preventing the interaction of RBPJ with DNA ( ).

Citation: Longnecker R. 1998. Molecular Biology of Epstein-Barr Virus, p 135-174. In McCance D (ed), Human Tumor Viruses. ASM Press, Washington, DC. doi: 10.1128/9781555818289.ch4
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Figure 4

LMP1 activation of EBV-infected B cells. Signal transduction through TNF family receptors such as CD40 is initiated by clustering of the receptor by the binding of ligand. Receptor-associated proteins called TRAFs are then activated, leading to NK-B activation ( ). In EBV-immortalized B cells, LMP1 mimics a clustered TNF family receptor, thereby constitutively associating with the TRAFs and TRADD and activating the TNF signal transduction pathway, resulting in NF-B activation ( ). TRAF3 may interfere with LMP1 binding of TRAF1 and TRAF3, which may block LMP1 activation of NF-B ( ). The relevance of TRAF association with other cellular proteins such as A20, NIK, c-IAP, and RIP needs to be determined ( ).

Citation: Longnecker R. 1998. Molecular Biology of Epstein-Barr Virus, p 135-174. In McCance D (ed), Human Tumor Viruses. ASM Press, Washington, DC. doi: 10.1128/9781555818289.ch4
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Figure 5

LMP2 effects on signal transduction through the B-cell antigen receptor complex (BCR). Ligation of the BCR induces the activation of the Src family and Syk PTKs, followed by activation of other transducing molecules (see reference for a detailed review). In latently infected B cells, LMP2A is expressed and the multiple hydrophobic domains of LMP2A mediate aggregation in the plasma membrane, where the ammo-terminal domains of LMP2A resemble cross-linked receptor tails and become tyrosine phosphorylated. The Src family PTKs and the Syk PTK bind. Other SH2-containing proteins may also bind. This complex then blocks signal transduction through the BCR, preventing activation of lytic replication following BCR ligation. The LMP2A complex does not block chemical inducers of gene transcription such as phorbol esters (PMA) or calcium ionophores (A23187). Activation to lytic replication may be mediated by an as yet unidentified pathway such as an interleukin cytokine pathway (IL-x and IL-xR) that is not blocked by LMP2A. LMP2B may aggregate in the plasma membrane with LMP2A. Lacking the ammo-terminal domain of LMP2A, LMP2B may increase the spacing between LMP2A amino-terminal domains, resulting in release of the Src family and Syk PTKs from LMP2A and restoring normal signal transduction through the BCR.

Citation: Longnecker R. 1998. Molecular Biology of Epstein-Barr Virus, p 135-174. In McCance D (ed), Human Tumor Viruses. ASM Press, Washington, DC. doi: 10.1128/9781555818289.ch4
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