Epstein-Barr virus uses HLA class II as a cofactor for infection of B lymphocytes

Li, Qingxue; Spriggs, Melanie K.; Kovats, Susan; Turk, Susan M.; Comeau, Michael R.; Nepom, Barbara S.; Hutt-Fletcher, Lindsey

doi:10.1128/jvi.71.6.4657-4662.1997

Cited by 274 publications

(103 citation statements)

References 61 publications

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“…Second, gp42 is generated through proteolytic cleavage in the ER and matures into a secreted form that binds class II MHC molecules at the cell surface. gp42 bound to class II MHC molecules at the cell surface prevents TCR-(peptide-loaded class II MHC) interactions and CD4 þ T cell activation (Li et al, 1997;Ressing et al, 2003Ressing et al, , 2005Spriggs et al, 1996).…”

Section: Inhibition Of Recognition At the Surface Of The Apcmentioning

confidence: 99%

Antigen Presentation and the Ubiquitin‐Proteasome System in Host–Pathogen Interactions

Loureiro

Ploegh

2006

Advances in Immunology

160

122

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Relatively small genomes and high replication rates allow viruses and bacteria to accumulate mutations. This continuously presents the host immune system with new challenges. On the other side of the trenches, an increasingly well-adjusted host immune response, shaped by coevolutionary history, makes a pathogen's life a rather complicated endeavor. It is, therefore, no surprise that pathogens either escape detection or modulate the host immune response, often by redirecting normal cellular pathways to their advantage. For the purpose of this chapter, we focus mainly on the manipulation of the class I and class II major histocompatibility complex (MHC) antigen presentation pathways and the ubiquitin (Ub)-proteasome system by both viral and bacterial pathogens. First, we describe the general features of antigen presentation pathways and the Ub-proteasome system and then address how they are manipulated by pathogens. We discuss the many human cytomegalovirus (HCMV)-encoded immunomodulatory genes that interfere with antigen presentation (immunoevasins) and focus on the HCMV immunoevasins US2 and US11, which induce the degradation of class I MHC heavy chains by the proteasome by catalyzing their export from the endoplasmic reticulum (ER)-membrane into the cytosol, a process termed ER dislocation. US2- and US11-mediated subversion of ER dislocation ensures proteasomal degradation of class I MHC molecules and presumably allows HCMV to avoid recognition by cytotoxic T cells, whilst providing insight into general aspects of ER-associated degradation (ERAD) which is used by eukaryotic cells to purge their ER of defective proteins. We discuss the similarities and differences between the distinct pathways co-opted by US2 and US11 for dislocation and degradation of human class I MHC molecules and also a putatively distinct pathway utilized by the murine herpes virus (MHV)-68 mK3 immunoevasin for ER dislocation of murine class I MHC. We speculate on the implications of the three pathogen-exploited dislocation pathways to cellular ER quality control. Moreover, we discuss the ubiquitin (Ub)-proteasome system and its position at the core of antigen presentation as proteolysis and intracellular trafficking rely heavily on Ub-dependent processes. We add a few examples of manipulation of the Ub-proteasome system by pathogens in the context of the immune system and such diverse aspects of the host-pathogen relationship as virus budding, bacterial chromosome integration, and programmed cell death, to name a few. Finally, we speculate on newly found pathogen-encoded deubiquitinating enzymes (DUBs) and their putative roles in modulation of host-pathogen interactions.

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Section: Inhibition Of Recognition At the Surface Of The Apcmentioning

confidence: 99%

Antigen Presentation and the Ubiquitin‐Proteasome System in Host–Pathogen Interactions

Loureiro

Ploegh

2006

Advances in Immunology

160

122

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“…Epstein-Barr virus (EBV) establishes a latent infection in B cells. The product of the BZLF2 gene, gp42, facilitates infection of class II MHC + cells by binding to the class II MHC product HLA-DR, which serves as a co-receptor for infection (53). Interfering with the display of peptides in the context of class II MHC products may be a strategy beneficial to EBV.…”

Section: Blocking Recognition Of Class II Mhc Productsmentioning

confidence: 99%

Viral modulation of antigen presentation: manipulation of cellular targets in the ER and beyond

Lilley

Ploegh

2005

Immunological Reviews

118

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Viruses that establish long-term infections in their hosts have evolved a number of methods to interfere with the activities of the innate and adaptive immune systems. Control of viral infections is achieved in part through the action of cytotoxic T lymphocytes (CTLs) that recognize cytosolically derived antigenic peptides in the context of class I major histocompatibility complex (MHC) molecules. Viral replication within host cells produces abundant proteinaceous fodder for proteasomal digestion and display by class I MHC products. Tactics that disrupt antigen-presentation pathways and prevent the display of peptides to CD8(+) CTLs have been favored during the course of host-virus co-evolution. Viral immunoevasins exploit diverse cellular processes to interfere with host antiviral functions. The study of such viral factors has uncovered novel host proteins that assist these viral factors in their task and that themselves perform important cellular functions. Here, we focus on viral immunoevasins that, together with their cellular targets, interfere with antigen-presentation pathways. In particular, we emphasize the intersection of the cellular quality-control machinery in the endoplasmic reticulum with the herpesvirus proteins that have co-opted it.

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“…PrV HS-GAG (Mettenleiter et al, 1990); nectin-1 alpha/Prr1/HveC ; nectin-2 alpha/Prr2/HveB (Warner et al, 1998); murine HveB (Shukla et al, 1999b); porcine HveC (Milne et al, 2001); murine HveC ; PVR/CD155 Herpesviridae, betaherpesvirinae HCMV/HHV-5 HS-GAG (Compton et al, 1993); APN/CD13 (Soderberg et al, 1993); MHC class I via 2 -microglobulin (Grundy et al, 1987) HHV-6 CD46 (Santoro et al, 1999) HHV-7 HS-GAG (Secchiero et al, 1997;Skrincosky et al, 2000); CD4 (Lusso et al, 1994) KSHV/HHV-8 HS-GAG Birkmann et al, 2001;Wang et al, 2001); integrin 3 1 (Akula et al, 2002) MCMV MHC class I (H-2Dd and Kb) (Wykes et al, 1993) Herpesviridae, gammaherpesvirinae EBV/HHV-4 CD21/CR2 (Fingeroth et al, 1984;Frade et al, 1985;Nemerow et al, 1985); MHC class II (HLA-DR, -DP, -DQ) (Reisert et al, 1985;Li et al, 1997; BHV-4 HS-GAG (Vanderplasschen et al, 1993) Papovaviridae Papillomavirus 6 integrins (Evander et al, 1997;McMillan et al, 1999); HS-GAG (Giroglou et al, 2001) Murine polyomavirus Sialic acid (N-acetyl neuraminic acid) (Stehle et al, 1994;Stehle and Harrison, 1996);integrin 41 (Caruso et al, 2003) SV40 MHC class I (Atwood and Norkin, 1989;Breau et al, 1992) Poxviridae Vaccinia virus HS-GAG and CS-GAG (Chung et al, 1998;Hsiao et al, 1999) Myxoma virus CCR1, CCR5, CXCR4 (Lalani et al, 1999) Single-stranded DNA viruses Parvoviridae AAV2 HS-GAG (Summerford and Samulski, 199...…”

Section: Nature Of Viral Receptorsmentioning

confidence: 99%

Evolution of Cell Recognition by Viruses: A Source of Biological Novelty with Medical Implications

Baranowski

Ruiz-Jarabo

Pariente

et al. 2003

Advances in Virus Research

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Receptor classCellular structure a Extracellular matrix components, sugar derivatives and lipids GalactosylceramideGangliosides Glycosaminoglycans (heparan and chondroitin sulfates) Phospholipids Sialic acid (N-acetylneuraminic acid, N-acetyl-9-O-acetylneuraminic acid and N-glycolylneuraminic acid 3-O-sulfated heparan sulfate Cell adhesion and cell-cell contact proteins -Dystroglycan Coxsackievirus-adenovirus receptor (CAR; Ig superfamily) CD4 (Ig superfamily) CEACAMs (including Bgp1a, Bgp2, and pregnancy-specific glycoprotein) Intercellular adhesion molecule type 1 (ICAM-1; Ig superfamily) Integrins Junction adhesion molecule (JAM) Laminin receptor (high affinity) MHC class I and 2 -microglobulin Neural cell adhesion molecule (NCAM) Signaling lymphocyte activation molecule

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Epstein-Barr virus uses HLA class II as a cofactor for infection of B lymphocytes

Cited by 274 publications

References 61 publications

Antigen Presentation and the Ubiquitin‐Proteasome System in Host–Pathogen Interactions

Antigen Presentation and the Ubiquitin‐Proteasome System in Host–Pathogen Interactions

Viral modulation of antigen presentation: manipulation of cellular targets in the ER and beyond

Evolution of Cell Recognition by Viruses: A Source of Biological Novelty with Medical Implications

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