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Marlene Bouvier
Department of Microbiology and Immunology, University of Illinois at Chicago, 909 S Wolcott Avenue, Chicago, IL 60612, USA

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Communication
Published: 01 July 2021 in Viruses
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The enteric human adenoviruses of species F (HAdVs-F), which comprise HAdV-F40 and HAdV-F41, are significant pathogens that cause acute gastroenteritis in children worldwide. The early transcription unit 3 (E3) of HAdVs-F is markedly different from that of all other HAdV species. To date, the E3 proteins unique to HAdVs-F have not been characterized and the mechanism by which HAdVs-F evade immune defenses in the gastrointestinal (GI) tract is poorly understood. Here, we show that HAdV-F41 infection of human intestinal HCT116 cells upregulated the expression of MHC class I-related chain A (MIC A) and MIC B relative to uninfected cells. Our results also showed that, for MIC B, this response did not however result in a significant increase of MIC B on the cell surface. Instead, MIC B was largely sequestered intracellularly. Thus, although HAdV-F41 infection of HCT116 cells upregulated MIC B expression, the ligand remained inside infected cells. A similar observation could not be made for MIC A in these cells. Our preliminary findings represent a novel function of HAdVs-F that may enable these viruses to evade immune surveillance by natural killer (NK) cells in the infected gut, thereby paving the way for the future investigation of their unique E3 proteins.

ACS Style

Edson Oliveira; Lenong Li; Marlene Bouvier. Intracellular Sequestration of the NKG2D Ligand MIC B by Species F Adenovirus. Viruses 2021, 13, 1289 .

AMA Style

Edson Oliveira, Lenong Li, Marlene Bouvier. Intracellular Sequestration of the NKG2D Ligand MIC B by Species F Adenovirus. Viruses. 2021; 13 (7):1289.

Chicago/Turabian Style

Edson Oliveira; Lenong Li; Marlene Bouvier. 2021. "Intracellular Sequestration of the NKG2D Ligand MIC B by Species F Adenovirus." Viruses 13, no. 7: 1289.

Journal article
Published: 01 December 2019 in Journal of Biological Chemistry
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Endoplasmic reticulum aminopeptidase 1 (ERAP1) and ERAP2 critically shape the major histocompatibility complex I (MHC I) immunopeptidome. The ERAPs remove N-terminal residues from antigenic precursor peptides and generate optimal-length peptides (i.e. 8–10-mers) to fit into the MHC class I groove. It is therefore intriguing that MHC class I molecules can present N-terminally extended peptides on the cell surface that can elicit CD8+ T-cell responses. This observation likely reflects gaps in our understanding of how antigens are processed by the ERAP enzymes. To better understand ERAPs' function in antigen processing, here we generated a nested set of N-terminally extended 10–20-mer peptides (RA)nAAKKKYCL covalently bound to the human leukocyte antigen (HLA)-B*0801. We used X-ray crystallography, thermostability assessments, and an ERAP1-trimming assay to characterize these complexes. The X-ray structures determined at 1.40–1.65 Å resolutions revealed that the residue extensions (RA)n unexpectedly protrude out of the A pocket of HLA-B*0801, whereas the AAKKKYCL core of all peptides adopts similar, bound conformations. HLA-B*0801 residue 62 was critical to open the A pocket. We also show that HLA-B*0801 and antigenic precursor peptides form stable complexes. Finally, ERAP1-mediated trimming of the MHC I–bound peptides required a minimal length of 14 amino acids. We propose a mechanistic model explaining how ERAP1-mediated trimming of MHC I–bound peptides in cells can generate peptides of canonical as well as noncanonical lengths that still serve as stable MHC I ligands. Our results provide a framework to better understand how the ERAP enzymes influence the MHC I immunopeptidome.

ACS Style

Lenong Li; Mansoor Batliwala; Marlene Bouvier. ERAP1 enzyme-mediated trimming and structural analyses of MHC I–bound precursor peptides yield novel insights into antigen processing and presentation. Journal of Biological Chemistry 2019, 294, 18534 -18544.

AMA Style

Lenong Li, Mansoor Batliwala, Marlene Bouvier. ERAP1 enzyme-mediated trimming and structural analyses of MHC I–bound precursor peptides yield novel insights into antigen processing and presentation. Journal of Biological Chemistry. 2019; 294 (49):18534-18544.

Chicago/Turabian Style

Lenong Li; Mansoor Batliwala; Marlene Bouvier. 2019. "ERAP1 enzyme-mediated trimming and structural analyses of MHC I–bound precursor peptides yield novel insights into antigen processing and presentation." Journal of Biological Chemistry 294, no. 49: 18534-18544.

In a nutshell
Published: 15 November 2019 in FEBS Letters
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Human adenoviruses (HAdVs) are widespread pathogens that cause a number of partially overlapping, species‐specific infections associated with respiratory, urinary, gastrointestinal, and ocular diseases. The early 3 (E3) region of adenoviruses is highly divergent between different species, and it encodes a multitude of proteins with immunomodulatory functions. The study of genetic diversity in the E3 region offers a unique opportunity to gain insight into how the various HAdVs have evolutionarily adapted in response to the selection pressures exerted by host immune defenses. The objective of this review was to discuss subversion of host antiviral immune responses by HAdVs, with a focus on suppression of MHC class I antigen presentation, as a window into host–HAdV adaptation.

ACS Style

Edson Ra Oliveira; Marlene Bouvier. Immune evasion by adenoviruses: a window into host–virus adaptation. FEBS Letters 2019, 593, 3496 -3503.

AMA Style

Edson Ra Oliveira, Marlene Bouvier. Immune evasion by adenoviruses: a window into host–virus adaptation. FEBS Letters. 2019; 593 (24):3496-3503.

Chicago/Turabian Style

Edson Ra Oliveira; Marlene Bouvier. 2019. "Immune evasion by adenoviruses: a window into host–virus adaptation." FEBS Letters 593, no. 24: 3496-3503.

Protocol
Published: 31 May 2019 in Breast Cancer
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In the endoplasmic reticulum (ER), MHC class I molecules associate with several specialized proteins, forming a large macromolecular complex referred to as the “peptide-loading complex” (PLC). In the PLC, antigenic peptides undergo a stringent selection process that determines which antigen becomes part of the repertoire presented by MHC class I molecules. This ensures that the immune system elicits robust CD8+ T-cell responses to viruses and solid tumors. The ability to reconstitute in vitro MHC class I molecules in association with key proteins of the PLC provides a mean for studying at the molecular level how antigenic peptides are selected for presentation to CD8+ T-cells. Here, we describe practical procedures for generating a cell-free system made up of MHC class I molecules and tapasin that can be used for mechanistic studies of peptide loading and exchange.

ACS Style

Marlene Bouvier. In Vitro Studies of MHC Class I Peptide Loading and Exchange. Breast Cancer 2019, 1988, 71 -81.

AMA Style

Marlene Bouvier. In Vitro Studies of MHC Class I Peptide Loading and Exchange. Breast Cancer. 2019; 1988 ():71-81.

Chicago/Turabian Style

Marlene Bouvier. 2019. "In Vitro Studies of MHC Class I Peptide Loading and Exchange." Breast Cancer 1988, no. : 71-81.

Protocol
Published: 31 May 2019 in Breast Cancer
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Studies over the last decade on characterization of the major histocompatibility complex (MHC) class I antigen presentation pathway have highlighted the importance of antigen processing, peptide transport, peptide trimming, and peptide selection as key stages for the development of optimal peptide repertoires that are presented by MHC class I molecules to cytotoxic T lymphocytes (CTLs). The study of these stages and how they are regulated, is fundamental for progress in understanding the adaptive immune system. Here we describe an in vitro assay monitoring peptide trimming by the human endoplasmic reticulum amino peptidases 1 (ERAP1) and ERAP2 (ERAPs) as a tool to characterize trimming events and gain a better understanding of the role and function of ERAPs in peptide repertoire development. Specifically, our assay allows for monitoring trimming of free but also of MHC I-bound peptides which may reflect the physiological situation best.

ACS Style

Mirjana Weimershaus; Irini Evnouchidou; Lenong Li; Peter Van Endert; Marlene Bouvier. Trimming of MHC Class I Ligands by ERAP Aminopeptidases. Breast Cancer 2019, 1988, 31 -43.

AMA Style

Mirjana Weimershaus, Irini Evnouchidou, Lenong Li, Peter Van Endert, Marlene Bouvier. Trimming of MHC Class I Ligands by ERAP Aminopeptidases. Breast Cancer. 2019; 1988 ():31-43.

Chicago/Turabian Style

Mirjana Weimershaus; Irini Evnouchidou; Lenong Li; Peter Van Endert; Marlene Bouvier. 2019. "Trimming of MHC Class I Ligands by ERAP Aminopeptidases." Breast Cancer 1988, no. : 31-43.

Journal article
Published: 12 August 2016 in Scientific Reports
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The processing of MHC class I antigenic precursor peptides by the endoplasmic reticulum aminopeptidase 1 (ERAP1) and ERAP2 is an important event in the cell biology of antigen presentation. To date, the molecular context by which the ERAP enzymes trim precursor peptides, and how ERAPs shape peptide repertoires, remain open questions. Using ERAP1 and ERAP2 heterodimers (ERAP1/2), and N-terminally extended model and natural peptides in their free and HLA-B*0801-bound forms, we characterized the mode of action of ERAPs. We provide evidence that ERAP1/2 can trim MHC I-bound precursor peptides to their correct and final lengths, albeit more slowly than the corresponding free precursors. Trimming of MHC I-bound precursors by ERAP1/2 increases the conformational stability of MHC I/peptide complexes. From the data, we propose a molecular mechanistic model of ERAP1/2 as peptide editors. Overall, our study provides new findings on a significant issue of the ERAP-mediated processing pathway of MHC class I antigens.

ACS Style

Hanna Chen; Lenong Li; Mirjana Weimershaus; Irini Evnouchidou; Peter van Endert; Marlene Bouvier. ERAP1-ERAP2 dimers trim MHC I-bound precursor peptides; implications for understanding peptide editing. Scientific Reports 2016, 6, 28902 .

AMA Style

Hanna Chen, Lenong Li, Mirjana Weimershaus, Irini Evnouchidou, Peter van Endert, Marlene Bouvier. ERAP1-ERAP2 dimers trim MHC I-bound precursor peptides; implications for understanding peptide editing. Scientific Reports. 2016; 6 (1):28902.

Chicago/Turabian Style

Hanna Chen; Lenong Li; Mirjana Weimershaus; Irini Evnouchidou; Peter van Endert; Marlene Bouvier. 2016. "ERAP1-ERAP2 dimers trim MHC I-bound precursor peptides; implications for understanding peptide editing." Scientific Reports 6, no. 1: 28902.

Journal article
Published: 06 July 2016 in The Journal of Immunology
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Adenoviruses (Ads) subvert MHC class I Ag presentation and impair host anti-Ad cellular activities. Specifically, the Ad-encoded E3-19K immunomodulatory protein targets MHC class I molecules for retention within the endoplasmic reticulum of infected cells. We report the x-ray crystal structure of the Ad type 4 (Ad4) E3-19K of species E bound to HLA-A2 at 2.64-Å resolution. Structural analysis shows that Ad4 E3-19K adopts a tertiary fold that is shared only with Ad2 E3-19K of species C. A comparative analysis of the Ad4 E3-19K/HLA-A2 structure with our x-ray structure of Ad2 E3-19K/HLA-A2 identifies species-specific features in HLA-A2 recognition. Our analysis also reveals common binding characteristics that explain the promiscuous, and yet high-affinity, association of E3-19K proteins with HLA-A and HLA-B molecules. We also provide structural insights into why E3-19K proteins do not associate with HLA-C molecules. Overall, our study provides new information about how E3-19K proteins selectively engage with MHC class I to abrogate Ag presentation and counteract activation of CD8+ T cells. The significance of MHC class I Ag presentation for controlling viral infections, as well as the threats of viral infections in immunocompromised patients, underline our efforts to characterize viral immunoevasins, such as E3-19K.

ACS Style

Lenong Li; Bernard D. Santarsiero; Marlene Bouvier. Structure of the Adenovirus Type 4 (Species E) E3-19K/HLA-A2 Complex Reveals Species-Specific Features in MHC Class I Recognition. The Journal of Immunology 2016, 197, 1399 -1407.

AMA Style

Lenong Li, Bernard D. Santarsiero, Marlene Bouvier. Structure of the Adenovirus Type 4 (Species E) E3-19K/HLA-A2 Complex Reveals Species-Specific Features in MHC Class I Recognition. The Journal of Immunology. 2016; 197 (4):1399-1407.

Chicago/Turabian Style

Lenong Li; Bernard D. Santarsiero; Marlene Bouvier. 2016. "Structure of the Adenovirus Type 4 (Species E) E3-19K/HLA-A2 Complex Reveals Species-Specific Features in MHC Class I Recognition." The Journal of Immunology 197, no. 4: 1399-1407.

Journal article
Published: 01 January 2013 in Frontiers in Immunology
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The cell-surface presentation of viral antigens by MHC class I molecules is critical for eliminating host infected cells. In turn, viruses have evolved various strategies to interfere with antigen processing and presentation. The adenovirus (Ad) E3-19K protein binds to and retains MHC class I molecules in the endoplasmic reticulum (ER), thereby suppressing anti-Ad activities of CD8+ T-cells. E3-19K is a type I transmembrane glycoprotein that comprises a N-terminus ER-lumenal domain, a transmembrane domain, and a C-terminus cytosolic tail. The ER-lumenal domain of E3-19K associates with the ER-lumenal domain of MHC I, while the dilysine motif in the cytosolic tail of E3-19K provides the signal for localization of the E3-19K/MHC I complex in the ER. We will describe a novel rescue refolding strategy that allowed formation of the Ad serotype 2 (Ad2) E3-19K/HLA-A2 complex, from which we recently grew crystals diffracting to 1.95 Å resolution. Ad2 E3-19K binds to the N-terminus of the HLA-A2 groove, contacting the α1-, α2-, and α3-domains and β2m. Ad2 E3-19K has a unique structure comprised of a large N-terminal domain, formed by two partially overlapping β-sheets arranged in a V-shape, a C-terminal α-helix and tail. The structure reveals determinants in E3-19K and HLA-A2 that are important for complex formation; conservation of some of these determinants in E3-19K of different Ad species and MHC I of different HLA loci suggests a universal binding mode for all E3-19K proteins. Our structure offers explanations for the mechanism by which E3-19K modulates antiviral cellular immunity.

ACS Style

Li Lenong; Muzahim Yasameen; Bouvier Marlene. Crystal structure of adenovirus E3-19K protein bound to HLA-A2 reveals mechanism for immunomodulation. Frontiers in Immunology 2013, 4, 1 .

AMA Style

Li Lenong, Muzahim Yasameen, Bouvier Marlene. Crystal structure of adenovirus E3-19K protein bound to HLA-A2 reveals mechanism for immunomodulation. Frontiers in Immunology. 2013; 4 ():1.

Chicago/Turabian Style

Li Lenong; Muzahim Yasameen; Bouvier Marlene. 2013. "Crystal structure of adenovirus E3-19K protein bound to HLA-A2 reveals mechanism for immunomodulation." Frontiers in Immunology 4, no. : 1.

Book chapter
Published: 29 October 2012 in Advanced Structural Safety Studies
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In the endoplasmic reticulum (ER), MHC class I molecules associate with several specialized proteins, forming a large macromolecular complex referred to as the “peptide-loading complex” (PLC). In the PLC, antigenic peptides undergo a stringent selection process for binding onto MHC class I molecules. This ensures that the immune system elicits robust CD8+ T-cell responses to viruses and solid tumors. The ability to reconstitute in vitro MHC class I molecules in association with key proteins of the PLC provides a mean for studying at the molecular level how antigenic peptides are selected for presentation to CD8+ T-cells. Here, we describe practical procedures for generating a cell-free system involving MHC class I molecules and tapasin, a critical protein of the PLC, that can be used as a versatile tool for biochemical and mechanistic studies of peptide loading and exchange.

ACS Style

Marlene Bouvier; Peter Van Endert. Studying MHC Class I Peptide Loading and Exchange In vitro. Advanced Structural Safety Studies 2012, 960, 81 -91.

AMA Style

Marlene Bouvier, Peter Van Endert. Studying MHC Class I Peptide Loading and Exchange In vitro. Advanced Structural Safety Studies. 2012; 960 ():81-91.

Chicago/Turabian Style

Marlene Bouvier; Peter Van Endert. 2012. "Studying MHC Class I Peptide Loading and Exchange In vitro." Advanced Structural Safety Studies 960, no. : 81-91.

Journal article
Published: 07 October 2012 in Nature Structural & Molecular Biology
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Adenovirus infection can suppress antigen presentation by MHC I, by the action of transmembrane protein E3-19K, whose N-terminal domain localizes to the ER lumen and binds MHC I luminal domain. Now the crystal structure of E3-19K in complex with MHC I molecule HLA-A2 is presented, providing atomic-level insight into this interaction. E3-19K binds to and retains MHC class I molecules in the endoplasmic reticulum, suppressing anti-adenovirus activities of T cells. We determined the structure of the adenovirus serotype 2 (Ad2, species C) E3-19K–HLA-A2 complex to 1.95-Å resolution. Ad2 E3-19K binds to the N terminus of the HLA-A2 groove, contacting the α1, α2 and α3 domains and β2m. Ad2 E3-19K has a unique structure comprising a large N-terminal domain, formed by two partially overlapping β-sheets arranged in a V shape, and a C-terminal α-helix and tail. The structure reveals determinants in E3-19K and HLA-A2 that are important for complex formation; conservation of some of these determinants in E3-19K proteins of different species and MHC I molecules of different loci suggests a universal binding mode for all E3-19K proteins. Our structure is important for understanding the immunomodulatory function of E3-19K.

ACS Style

Lenong Li; Yasameen Muzahim; Marlene Bouvier. Crystal structure of adenovirus E3-19K bound to HLA-A2 reveals mechanism for immunomodulation. Nature Structural & Molecular Biology 2012, 19, 1176 -1181.

AMA Style

Lenong Li, Yasameen Muzahim, Marlene Bouvier. Crystal structure of adenovirus E3-19K bound to HLA-A2 reveals mechanism for immunomodulation. Nature Structural & Molecular Biology. 2012; 19 (11):1176-1181.

Chicago/Turabian Style

Lenong Li; Yasameen Muzahim; Marlene Bouvier. 2012. "Crystal structure of adenovirus E3-19K bound to HLA-A2 reveals mechanism for immunomodulation." Nature Structural & Molecular Biology 19, no. 11: 1176-1181.

Conference abstract
Published: 31 May 2012 in Molecular Immunology
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ACS Style

Marlene Bouvier; Lenong Li; Yasameen Muzahim. Suppression of antigen presentation by the adenovirus E3-19 K protein; a crystallographic analysis of E3-19 K/MHC I interaction. Molecular Immunology 2012, 51, 1 .

AMA Style

Marlene Bouvier, Lenong Li, Yasameen Muzahim. Suppression of antigen presentation by the adenovirus E3-19 K protein; a crystallographic analysis of E3-19 K/MHC I interaction. Molecular Immunology. 2012; 51 (1):1.

Chicago/Turabian Style

Marlene Bouvier; Lenong Li; Yasameen Muzahim. 2012. "Suppression of antigen presentation by the adenovirus E3-19 K protein; a crystallographic analysis of E3-19 K/MHC I interaction." Molecular Immunology 51, no. 1: 1.

Journal article
Published: 01 May 2011 in Journal of Biological Chemistry
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Our understanding of the mechanism by which the E3-19K protein from adenovirus (Ad) targets major histocompatibility complex (MHC) class I molecules for retention in the endoplasmic reticulum is derived largely from studies of Ad serotype 2 (subgroup C). It is not well understood to what extent observations on the Ad2 E3-19K/MHC I association can be generalized to E3-19K proteins of other serotypes and subgroups. The low levels of amino acid sequence homology between E3-19K proteins suggest that these proteins are likely to manifest distinct MHC I binding properties. This information is important as the E3-19K/MHC I interaction is thought to play a critical role in enabling Ads to cause persistent infections. Here, we characterized interaction between E3-19K proteins of serotypes 7 and 35 (subgroup B), 5 (subgroup C), 37 (subgroup D), and 4 (subgroup E) and a panel of HLA-A, -B, and -C molecules using native gel, surface plasmon resonance (SPR), and flow cytometry. Results show that all E3-19K proteins exhibited allele specificity toward HLA-A and -B molecules; this was less evident for Ad37 E3-19K. The allele specificity for HLA-A molecules was remarkably similar for different serotypes of subgroup B as well as subgroup C. Interestingly, all E3-19K proteins characterized also exhibited MHC I locus specificity. Importantly, we show that Lys91 in the conserved region of Ad2 E3-19K targets the C terminus of the α2-helix (MHC residue 177) on MHC class I molecules. From our data, we propose a model of interaction between E3-19K and MHC class I molecules.

ACS Style

Jie Fu; Lenong Li; Marlene Bouvier. Adenovirus E3-19K Proteins of Different Serotypes and Subgroups Have Similar, Yet Distinct, Immunomodulatory Functions toward Major Histocompatibility Class I Molecules. Journal of Biological Chemistry 2011, 286, 17631 -17639.

AMA Style

Jie Fu, Lenong Li, Marlene Bouvier. Adenovirus E3-19K Proteins of Different Serotypes and Subgroups Have Similar, Yet Distinct, Immunomodulatory Functions toward Major Histocompatibility Class I Molecules. Journal of Biological Chemistry. 2011; 286 (20):17631-17639.

Chicago/Turabian Style

Jie Fu; Lenong Li; Marlene Bouvier. 2011. "Adenovirus E3-19K Proteins of Different Serotypes and Subgroups Have Similar, Yet Distinct, Immunomodulatory Functions toward Major Histocompatibility Class I Molecules." Journal of Biological Chemistry 286, no. 20: 17631-17639.

Journal article
Published: 31 January 2011 in Molecular Immunology
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The E3-19K immunomodulatory protein from adenoviruses (Ads) inhibits antigen presentation by major histocompatibility complex (MHC) class I molecules. As a result, the ability of Ad-specific cytotoxic T lymphocytes (CTLs) to lyse infected cells is suppressed. The ER-lumenal domain of E3-19K is subdivided into a variable (residues 1 to ∼78/81) and conserved (residues ∼79/82 to 98) region followed by a linker (residues 99–107). Using molecular and cellular approaches, we characterized in detail the properties of the ER-lumenal domain of E3-19K that enable it to target MHC class I molecules. Proteolysis of recombinant serotype 2 E3-19K (residues 1–100) (with six His residues) generated a large N-terminal (residues 1–88) and a small C-terminal fragment (residues 94–100) in solution. Neither of these fragments associates with HLA-A*1101 as shown by a native gel band-shift assay. In contrast, the N-terminal 1-93 residues of Ad2 E3-19K exhibited the same binding affinity to HLA-A*1101 as E3-19K. Using a site-directed mutational analysis and flow cytometry, we show that Tyr93, but not Tyr88, critically modulates the cell-surface expression of MHC class I molecules. Taken together, these results indicate that the sequence comprising residues 89–93 (M89SKQY93), and in particular Tyr93, in the conserved region of E3-19K is critical for its immunomodulatory function. Residues 89–93 likely form a linker or loop in E3-19K. Overall, our data provide novel insights into the structure of E3-19K and identify key determinants for association with and ER-retention of its cellular target protein. This knowledge is important for our understanding of the molecular basis of Ad pathogenesis.

ACS Style

Jie Fu; Marlene Bouvier. Determinants of the endoplasmic reticulum (ER) lumenal-domain of the adenovirus serotype 2 E3-19K protein for association with and ER-retention of major histocompatibility complex class I molecules. Molecular Immunology 2011, 48, 532 -538.

AMA Style

Jie Fu, Marlene Bouvier. Determinants of the endoplasmic reticulum (ER) lumenal-domain of the adenovirus serotype 2 E3-19K protein for association with and ER-retention of major histocompatibility complex class I molecules. Molecular Immunology. 2011; 48 (4):532-538.

Chicago/Turabian Style

Jie Fu; Marlene Bouvier. 2011. "Determinants of the endoplasmic reticulum (ER) lumenal-domain of the adenovirus serotype 2 E3-19K protein for association with and ER-retention of major histocompatibility complex class I molecules." Molecular Immunology 48, no. 4: 532-538.

Review article
Published: 31 March 2008 in Trends in Immunology
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Cytotoxic and helper T cells respond to peptides derived from endogenous and exogenous sources that bind to major histocompatibility complex (MHC) class I and class II molecules and are presented on antigen-presenting cells. MHC class I and class II structures and maturation pathways have evolved to optimize antigen presentation to their respective T cells. The accessory proteins tapasin and HLA-DM (DM) crucially influence the selection of peptides that bind to the MHC molecules. We discuss here the dynamic interactions of tapasin and DM with their corresponding MHC molecules that indicate striking parallels. Utilization of a common mode of peptide selection by two different, but related, biological systems argue for its mechanistic validity.

ACS Style

Scheherazade Sadegh-Nasseri; Mingnan Chen; Kedar Narayan; Marlene Bouvier. The convergent roles of tapasin and HLA-DM in antigen presentation. Trends in Immunology 2008, 29, 141 -147.

AMA Style

Scheherazade Sadegh-Nasseri, Mingnan Chen, Kedar Narayan, Marlene Bouvier. The convergent roles of tapasin and HLA-DM in antigen presentation. Trends in Immunology. 2008; 29 (3):141-147.

Chicago/Turabian Style

Scheherazade Sadegh-Nasseri; Mingnan Chen; Kedar Narayan; Marlene Bouvier. 2008. "The convergent roles of tapasin and HLA-DM in antigen presentation." Trends in Immunology 29, no. 3: 141-147.