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Article ; Online: How the virus outsmarts the host: function and structure of cytomegalovirus MHC-I-like molecules in the evasion of natural killer cell surveillance.

Revilleza, Maria Jamela / Wang, Rui / Mans, Janet / Hong, Manqing / Natarajan, Kannan / Margulies, David H

2011 Volume 2011, Page(s) 724607

Abstract: Natural killer (NK) cells provide an initial host immune response to infection by many viral pathogens. Consequently, the viruses have evolved mechanisms to attenuate the host response, leading to improved viral fitness. One mechanism employed by members ...

Abstract	Natural killer (NK) cells provide an initial host immune response to infection by many viral pathogens. Consequently, the viruses have evolved mechanisms to attenuate the host response, leading to improved viral fitness. One mechanism employed by members of the β-herpesvirus family, which includes the cytomegaloviruses, is to modulate the expression of cell surface ligands recognized by NK cell activation molecules. A novel set of cytomegalovirus (CMV) genes, exemplified by the mouse m145 family, encode molecules that have structural and functional features similar to those of host major histocompatibility-encoded (MHC) class I molecules, some of which are known to contribute to immune evasion. In this review, we explore the function, structure, and evolution of MHC-I-like molecules of the CMVs and speculate on the dynamic development of novel immunoevasive functions based on the MHC-I protein fold.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cytomegalovirus/genetics ; Cytomegalovirus/immunology ; Cytomegalovirus/pathogenicity ; Cytomegalovirus Infections/immunology ; Cytomegalovirus Infections/virology ; Evolution, Molecular ; Genes, MHC Class I/genetics ; Genes, MHC Class I/immunology ; Host-Pathogen Interactions/genetics ; Host-Pathogen Interactions/immunology ; Humans ; Immune Evasion ; Immunologic Surveillance ; Killer Cells, Natural/immunology ; Mice ; Molecular Sequence Data ; Receptors, Natural Killer Cell/immunology ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Viral Proteins/immunology
Chemical Substances	Receptors, Natural Killer Cell ; Viral Proteins
Language	English
Publishing date	2011-06-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	2052552-7
ISSN	1110-7251 ; 1110-7243
ISSN (online)	1110-7251
ISSN	1110-7243
DOI	10.1155/2011/724607
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Article ; Online: How the Virus Outsmarts the Host

Maria Jamela Revilleza / Rui Wang / Janet Mans / Manqing Hong / Kannan Natarajan / David H. Margulies

Journal of Biomedicine and Biotechnology, Vol

Function and Structure of Cytomegalovirus MHC-I-Like Molecules in the Evasion of Natural Killer Cell Surveillance

2011 Volume 2011

Abstract	Natural killer (NK) cells provide an initial host immune response to infection by many viral pathogens. Consequently, the viruses have evolved mechanisms to attenuate the host response, leading to improved viral fitness. One mechanism employed by members of the β-herpesvirus family, which includes the cytomegaloviruses, is to modulate the expression of cell surface ligands recognized by NK cell activation molecules. A novel set of cytomegalovirus (CMV) genes, exemplified by the mouse m145 family, encode molecules that have structural and functional features similar to those of host major histocompatibility-encoded (MHC) class I molecules, some of which are known to contribute to immune evasion. In this review, we explore the function, structure, and evolution of MHC-I-like molecules of the CMVs and speculate on the dynamic development of novel immunoevasive functions based on the MHC-I protein fold.
Keywords	Biotechnology ; TP248.13-248.65 ; Medicine ; R
Subject code	570
Language	English
Publishing date	2011-01-01T00:00:00Z
Publisher	Hindawi Limited
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Structural basis of mouse cytomegalovirus m152/gp40 interaction with RAE1γ reveals a paradigm for MHC/MHC interaction in immune evasion.

Wang, Rui / Natarajan, Kannan / Revilleza, Maria Jamela R / Boyd, Lisa F / Zhi, Li / Zhao, Huaying / Robinson, Howard / Margulies, David H

Proceedings of the National Academy of Sciences of the United States of America

2012 Volume 109, Issue 51, Page(s) E3578–87

Abstract: Natural killer (NK) cells are activated by engagement of the NKG2D receptor with ligands on target cells stressed by infection or tumorigenesis. Several human and rodent cytomegalovirus (CMV) immunoevasins down-regulate surface expression of NKG2D ... ...

Abstract	Natural killer (NK) cells are activated by engagement of the NKG2D receptor with ligands on target cells stressed by infection or tumorigenesis. Several human and rodent cytomegalovirus (CMV) immunoevasins down-regulate surface expression of NKG2D ligands. The mouse CMV MHC class I (MHC-I)-like m152/gp40 glycoprotein down-regulates retinoic acid early inducible-1 (RAE1) NKG2D ligands as well as host MHC-I. Here we describe the crystal structure of an m152/RAE1γ complex and confirm the intermolecular contacts by mutagenesis. m152 interacts in a pincer-like manner with two sites on the α1 and α2 helices of RAE1 reminiscent of the NKG2D interaction with RAE1. This structure of an MHC-I-like immunoevasin/MHC-I-like ligand complex explains the binding specificity of m152 for RAE1 and allows modeling of the interaction of m152 with classical MHC-I and of related viral immunoevasins.
MeSH term(s)	Animals ; Drosophila/metabolism ; Escherichia coli/metabolism ; Gene Expression Regulation, Viral ; HEK293 Cells ; Humans ; Immune System ; Killer Cells, Natural/metabolism ; Ligands ; Major Histocompatibility Complex/immunology ; Membrane Glycoproteins/metabolism ; Mice ; Molecular Conformation ; Muromegalovirus/metabolism ; Mutation ; NK Cell Lectin-Like Receptor Subfamily K/chemistry ; Nuclear Matrix-Associated Proteins/metabolism ; Nucleocytoplasmic Transport Proteins/metabolism ; Protein Conformation ; Protein Isoforms ; Protein Structure, Secondary ; Surface Plasmon Resonance ; Viral Proteins/metabolism ; X-Ray Diffraction
Chemical Substances	KLRK1 protein, human ; Klrk1 protein, mouse ; Ligands ; Membrane Glycoproteins ; NK Cell Lectin-Like Receptor Subfamily K ; Nuclear Matrix-Associated Proteins ; Nucleocytoplasmic Transport Proteins ; Protein Isoforms ; RAE1 protein, human ; Rae1 protein, mouse ; Viral Proteins ; m152 protein, cytomegalovirus
Language	English
Publishing date	2012-11-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1214088109
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Article ; Online: A structural and molecular dynamics approach to understanding the peptide-receptive transition state of MHC-I molecules.

Mage, Michael G / Dolan, Michael A / Wang, Rui / Boyd, Lisa F / Revilleza, Maria Jamela / Robinson, Howard / Natarajan, Kannan / Myers, Nancy B / Hansen, Ted H / Margulies, David H

Molecular immunology

2012 Volume 55, Issue 2, Page(s) 123–125

Abstract: The mature conformation of major histocompatibility complex class I (MHC-I) proteins depends on the presence of bound peptides, permitting recognition at the cell surface by CD8(+) T lymphocytes. Newly synthesized MHC-I molecules in the endoplasmic ... ...

Abstract	The mature conformation of major histocompatibility complex class I (MHC-I) proteins depends on the presence of bound peptides, permitting recognition at the cell surface by CD8(+) T lymphocytes. Newly synthesized MHC-I molecules in the endoplasmic reticulum are maintained in a peptide-receptive (PR) transition state by several chaperones until they are released concomitant with the loading of peptides. By determining the crystallographic structure of a region of an MHC-I molecule that is recognized by a unique monoclonal antibody and comparing this with docking and molecular dynamics simulations with the whole molecule, we demonstrate the movement of a hinged unit supporting the part of the binding groove that interacts with the amino terminal residues of the bound peptide. This unit contains a conserved 310 helix that flips from an exposed "open" position in the PR form to a "closed" position in the peptide-loaded (PL) mature molecule. These analyses indicate how this segment of the MHC-I molecule moves to help establish the A and B pockets critical for tight peptide binding and the stable structure required for antigen presentation and T cell recognition at the cell surface.
MeSH term(s)	Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/metabolism ; Antigen Presentation ; CD8-Positive T-Lymphocytes/immunology ; Crystallography, X-Ray ; Histocompatibility Antigens Class I/immunology ; Histocompatibility Antigens Class I/metabolism ; Humans ; Molecular Dynamics Simulation ; Protein Binding ; Protein Structure, Tertiary ; Receptors, Pattern Recognition/immunology ; Receptors, Pattern Recognition/ultrastructure
Chemical Substances	Antibodies, Monoclonal ; Histocompatibility Antigens Class I ; Receptors, Pattern Recognition
Language	English
Publishing date	2012-11-28
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2012.10.021
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Article ; Online: The peptide-receptive transition state of MHC class I molecules: insight from structure and molecular dynamics.

Mage, Michael G / Dolan, Michael A / Wang, Rui / Boyd, Lisa F / Revilleza, Maria Jamela / Robinson, Howard / Natarajan, Kannan / Myers, Nancy B / Hansen, Ted H / Margulies, David H

Journal of immunology (Baltimore, Md. : 1950)

2012 Volume 189, Issue 3, Page(s) 1391–1399

Abstract: MHC class I (MHC-I) proteins of the adaptive immune system require antigenic peptides for maintenance of mature conformation and immune function via specific recognition by MHC-I-restricted CD8(+) T lymphocytes. New MHC-I molecules in the endoplasmic ... ...

Abstract	MHC class I (MHC-I) proteins of the adaptive immune system require antigenic peptides for maintenance of mature conformation and immune function via specific recognition by MHC-I-restricted CD8(+) T lymphocytes. New MHC-I molecules in the endoplasmic reticulum are held by chaperones in a peptide-receptive (PR) transition state pending release by tightly binding peptides. In this study, we show, by crystallographic, docking, and molecular dynamics methods, dramatic movement of a hinged unit containing a conserved 3(10) helix that flips from an exposed "open" position in the PR transition state to a "closed" position with buried hydrophobic side chains in the peptide-loaded mature molecule. Crystallography of hinged unit residues 46-53 of murine H-2L(d) MHC-I H chain, complexed with mAb 64-3-7, demonstrates solvent exposure of these residues in the PR conformation. Docking and molecular dynamics predict how this segment moves to help form the A and B pockets crucial for the tight peptide binding needed for stability of the mature peptide-loaded conformation, chaperone dissociation, and Ag presentation.
MeSH term(s)	Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; H-2 Antigens/chemistry ; H-2 Antigens/metabolism ; Histocompatibility Antigen H-2D ; Humans ; Ligands ; Mice ; Molecular Dynamics Simulation ; Molecular Sequence Data ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Structure-Activity Relationship ; beta 2-Microglobulin/chemistry ; beta 2-Microglobulin/metabolism
Chemical Substances	H-2 Antigens ; Histocompatibility Antigen H-2D ; Ligands ; Peptide Fragments ; beta 2-Microglobulin
Language	English
Publishing date	2012-06-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.1200831
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Article: Structure and function of murine cytomegalovirus MHC-I-like molecules: how the virus turned the host defense to its advantage.

Mans, Janet / Zhi, Li / Revilleza, Maria Jamela R / Smith, Lee / Redwood, Alec / Natarajan, Kannan / Margulies, David H

Immunologic research

2008 Volume 43, Issue 1-3, Page(s) 264–279

Abstract: The mouse cytomegalovirus (CMV), a beta-herpesvirus, exploits its large (~230 kb) double-stranded DNA genome for both essential and non-essential functions. Among the non-essential functions are those that offer the virus a selective advantage in eluding ...

Abstract	The mouse cytomegalovirus (CMV), a beta-herpesvirus, exploits its large (~230 kb) double-stranded DNA genome for both essential and non-essential functions. Among the non-essential functions are those that offer the virus a selective advantage in eluding both the innate and adaptive immune responses of the host. Several non-essential genes of MCMV are thought to encode MHC-I-like genes and to function as immunoevasins. To understand further the evolution and function of these viral MHC-I (MHC-Iv) molecules, X-ray structures of several of them have been determined, not only confirming the overall MHC-I-like structure, but also elucidating features unique to this family. Future efforts promise to clarify the nature of the molecular ligands of these molecules, their evolution in the context of the adapting immune response of the murine host, and by analogy the evolution of the host response to human CMV as well.
MeSH term(s)	Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; Histocompatibility Antigens Class I/chemistry ; Histocompatibility Antigens Class I/immunology ; Host-Pathogen Interactions/immunology ; Humans ; Mice ; Molecular Sequence Data ; Muromegalovirus/chemistry ; Muromegalovirus/genetics ; Muromegalovirus/immunology ; Muromegalovirus/pathogenicity ; Rats ; Sequence Alignment ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Viral Proteins/immunology
Chemical Substances	Histocompatibility Antigens Class I ; Viral Proteins
Language	English
Publishing date	2008-11-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	632857-x
ISSN	1559-0755 ; 0257-277X
ISSN (online)	1559-0755
ISSN	0257-277X
DOI	10.1007/s12026-008-8081-6
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Article: A structural and molecular dynamics approach to understanding the peptide-receptive transition state of MHC-I molecules

Mage, Michael G / Dolan, Michael A / Wang, Rui / Boyd, Lisa F / Revilleza, Maria Jamela / Robinson, Howard / Natarajan, Kannan / Myers, Nancy B / Hansen, Ted H / Margulies, David H

Molecular immunology. 2013 Sept., v. 55, no. 2

2013

Abstract: The mature conformation of major histocompatibility complex class I (MHC-I) proteins depends on the presence of bound peptides, permitting recognition at the cell surface by CD8⁺ T lymphocytes. Newly synthesized MHC-I molecules in the endoplasmic ... ...

Abstract	The mature conformation of major histocompatibility complex class I (MHC-I) proteins depends on the presence of bound peptides, permitting recognition at the cell surface by CD8⁺ T lymphocytes. Newly synthesized MHC-I molecules in the endoplasmic reticulum are maintained in a peptide-receptive (PR) transition state by several chaperones until they are released concomitant with the loading of peptides. By determining the crystallographic structure of a region of an MHC-I molecule that is recognized by a unique monoclonal antibody and comparing this with docking and molecular dynamics simulations with the whole molecule, we demonstrate the movement of a hinged unit supporting the part of the binding groove that interacts with the amino terminal residues of the bound peptide. This unit contains a conserved 3₁₀ helix that flips from an exposed “open” position in the PR form to a “closed” position in the peptide-loaded (PL) mature molecule. These analyses indicate how this segment of the MHC-I molecule moves to help establish the A and B pockets critical for tight peptide binding and the stable structure required for antigen presentation and T cell recognition at the cell surface.
Keywords	CD8-positive T-lymphocytes ; antigen presentation ; endoplasmic reticulum ; major histocompatibility complex ; molecular dynamics ; molecular models ; monoclonal antibodies ; peptides ; proteins
Language	English
Dates of publication	2013-09
Size	p. 123-125.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2012.10.021
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Article ; Online: Availability of autoantigenic epitopes controls phenotype, severity, and penetrance in TCR Tg autoimmune gastritis.

Levin, Ditza / DiPaolo, Richard J / Brinster, Carine / Revilleza, Maria Jamela R / Boyd, Lisa F / Teyton, Luc / Natarajan, Kannan / Mage, Michael G / Shevach, Ethan M / Margulies, David H

European journal of immunology

2008 Volume 38, Issue 12, Page(s) 3339–3353

Abstract: We examined TCR:MHC/peptide interactions and in vivo epitope availability to explore the Th1- or Th2-like phenotype of autoimmune disease in two TCR Tg mouse models of autoimmune gastritis (AIG). The TCR of strains A23 and A51 recognize distinct IA(d)- ... ...

Abstract	We examined TCR:MHC/peptide interactions and in vivo epitope availability to explore the Th1- or Th2-like phenotype of autoimmune disease in two TCR Tg mouse models of autoimmune gastritis (AIG). The TCR of strains A23 and A51 recognize distinct IA(d)-restricted peptides from the gastric parietal cell H/K-ATPase. Both peptides form extremely stable MHC/peptide (MHC/p) complexes. All A23 animals develop a Th1-like aggressive, inflammatory AIG early in life, while A51 mice develop indolent Th2-like AIG at 6-8 wk with incomplete penetrance. A51 T cells were more sensitive than A23 to low doses of soluble antigen and to MHC/p complexes. Staining with IA(d)/peptide tetramers was only detectable on previously activated T cells from A51. Thus, despite inducing a milder AIG, the A51 TCR displays a higher avidity for its cognate IA(d)/peptide. Nonetheless, in vivo proliferation of adoptively transferred A51 CFSE-labeled T cells in the gastric lymph node was relatively poor compared with A23 T cells. Also, DC from WT gastric lymph node, presenting processed antigen available in vivo, stimulated proliferation of A23 T cells better than A51. Thus, the autoimmune potential of these TCR in their respective Tg lines is strongly influenced by the availability of the peptide epitope, rather than by differential avidity for their respective MHC/p complexes.
MeSH term(s)	Amino Acid Sequence ; Animals ; Autoantigens/immunology ; Autoimmune Diseases/genetics ; Autoimmune Diseases/immunology ; Autoimmune Diseases/metabolism ; Autoimmune Diseases/pathology ; CD4-Positive T-Lymphocytes/cytology ; CD4-Positive T-Lymphocytes/immunology ; Cation Transport Proteins/metabolism ; Cell Proliferation ; Cells, Cultured ; Dendritic Cells/immunology ; Epitopes/immunology ; Female ; Gastritis/genetics ; Gastritis/immunology ; Gastritis/metabolism ; Gastritis/pathology ; Lymph Nodes/immunology ; Mice ; Mice, Inbred BALB C ; Mice, Transgenic ; Peptides/chemistry ; Peptides/immunology ; Phenotype ; Receptors, Antigen, T-Cell/genetics ; Receptors, Antigen, T-Cell/immunology ; Receptors, Antigen, T-Cell/metabolism
Chemical Substances	Autoantigens ; Cation Transport Proteins ; Epitopes ; Peptides ; Receptors, Antigen, T-Cell
Language	English
Publishing date	2008-09-14
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural
ZDB-ID	120108-6
ISSN	1521-4141 ; 0014-2980
ISSN (online)	1521-4141
ISSN	0014-2980
DOI	10.1002/eji.200838584
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Article: Availability of autoantigenic epitopes controls phenotype, severity, and penetrance in TCR Tg autoimmune gastritis

Levin, Ditza / DiPaolo, Richard J / Brinster, Carine / Revilleza, Maria Jamela R / Boyd, Lisa F / Teyton, Luc / Natarajan, Kannan / Mage, Michael G / Shevach, Ethan M / Margulies, David H

European journal of immunology. 2008 Dec., v. 38, no. 12

2008

Abstract	We examined TCR:MHC/peptide interactions and in vivo epitope availability to explore the Th1- or Th2-like phenotype of autoimmune disease in two TCR Tg mouse models of autoimmune gastritis (AIG). The TCR of strains A23 and A51 recognize distinct IAd-restricted peptides from the gastric parietal cell H/K-ATPase. Both peptides form extremely stable MHC/peptide (MHC/p) complexes. All A23 animals develop a Th1-like aggressive, inflammatory AIG early in life, while A51 mice develop indolent Th2-like AIG at 6-8 wk with incomplete penetrance. A51 T cells were more sensitive than A23 to low doses of soluble antigen and to MHC/p complexes. Staining with IAd/peptide tetramers was only detectable on previously activated T cells from A51. Thus, despite inducing a milder AIG, the A51 TCR displays a higher avidity for its cognate IAd/peptide. Nonetheless, in vivo proliferation of adoptively transferred A51 CFSE-labeled T cells in the gastric lymph node was relatively poor compared with A23 T cells. Also, DC from WT gastric lymph node, presenting processed antigen available in vivo, stimulated proliferation of A23 T cells better than A51. Thus, the autoimmune potential of these TCR in their respective Tg lines is strongly influenced by the availability of the peptide epitope, rather than by differential avidity for their respective MHC/p complexes.
Language	English
Dates of publication	2008-12
Size	p. 3339-3353.
Publishing place	Wiley-VCH Verlag
Document type	Article
ZDB-ID	120108-6
ISSN	1521-4141 ; 0014-2980
ISSN (online)	1521-4141
ISSN	0014-2980
DOI	10.1002/eji.200838584
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