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Article ; Online: Adenovirus-Extracellular Protein Interactions and Their Impact on Innate Immune Responses by Human Mononuclear Phagocytes.

Chéneau, Coraline / Kremer, Eric J

2020 Volume 12, Issue 12

Abstract: The aim of this review is to highlight how, in a syngeneic system, human mononuclear phagocytes respond to environments containing human adenovirus (HAdV) and soluble extracellular proteins that influence their innate immune response. Soluble ... ...

Abstract	The aim of this review is to highlight how, in a syngeneic system, human mononuclear phagocytes respond to environments containing human adenovirus (HAdV) and soluble extracellular proteins that influence their innate immune response. Soluble extracellular proteins, including immunoglobulins, blood clotting factors, proteins of the complement system, and/or antimicrobial peptides (AMPs) can exert direct effects by binding to a virus capsid that modifies interactions with pattern recognition receptors and downstream signaling. In addition, the presence, generation, or secretion of extracellular proteins can indirectly influence the response to HAdVs via the activation and recruitment of cells at the site of infection.
MeSH term(s)	Adenovirus Infections, Human/immunology ; Adenovirus Infections, Human/virology ; Adenoviruses, Human/immunology ; Animals ; Antibodies, Viral/immunology ; Cellular Microenvironment ; Complement System Proteins/immunology ; Dendritic Cells ; Extracellular Space/metabolism ; Host-Pathogen Interactions/immunology ; Humans ; Immunity, Innate ; Leukocytes, Mononuclear/immunology ; Leukocytes, Mononuclear/metabolism ; Lymphocytes/immunology ; Lymphocytes/metabolism ; Phagocytes/immunology ; Phagocytes/metabolism
Chemical Substances	Antibodies, Viral ; Complement System Proteins (9007-36-7)
Language	English
Publishing date	2020-11-26
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v12121351
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Article ; Online: Adenovirus-α-Defensin Complexes Induce NLRP3-Associated Maturation of Human Phagocytes via Toll-Like Receptor 4 Engagement.

Eichholz, Karsten / Tran, Tuan Hiep / Chéneau, Coraline / Tran, Thi Thu Phuong / Paris, Océane / Pugniere, Martine / Kremer, Eric J

Journal of virology

2022 Volume 96, Issue 6, Page(s) e0185021

Abstract: Intramuscular delivery of human adenovirus (HAdV)-based vaccines leads to rapid recruitment of neutrophils, which then release antimicrobial peptides/proteins (AMPs). How these AMPs influence vaccine efficacy over the subsequent 24 h is poorly understood. ...

Abstract	Intramuscular delivery of human adenovirus (HAdV)-based vaccines leads to rapid recruitment of neutrophils, which then release antimicrobial peptides/proteins (AMPs). How these AMPs influence vaccine efficacy over the subsequent 24 h is poorly understood. In this study, we asked if human neutrophil protein 1 (HNP-1), an α-defensin that influences direct and indirect innate immune responses to a range of pathogens, impacts the response of human phagocytes to three HAdV species/types (HAdV-C5, -D26, -B35). We show that HNP-1 binds to the capsids and redirects HAdV-C5, -D26, and -B35 to Toll-like receptor 4 (TLR4), which leads to internalization, an NLRP3-mediated inflammasome response, and interleukin 1 beta (IL-1β) release. Surprisingly, IL-1β release was not associated with notable disruption of plasma membrane integrity. These data further our understanding of HAdV vaccine immunogenicity and may provide pathways to extend the efficacy.
MeSH term(s)	Adenoviridae Infections/immunology ; Adenovirus Vaccines/immunology ; Adenoviruses, Human/immunology ; Humans ; Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein/genetics ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Phagocytes/cytology ; Phagocytes/metabolism ; Toll-Like Receptor 4/metabolism ; alpha-Defensins/immunology
Chemical Substances	Adenovirus Vaccines ; Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; Toll-Like Receptor 4 ; alpha-Defensins
Language	English
Publishing date	2022-01-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.01850-21
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Article ; Online: Lactoferrin Retargets Human Adenoviruses to TLR4 to Induce an Abortive NLRP3-Associated Pyroptotic Response in Human Phagocytes.

Chéneau, Coraline / Eichholz, Karsten / Tran, Tuan Hiep / Tran, Thi Thu Phuong / Paris, Océane / Henriquet, Corinne / Bajramovic, Jeffrey J / Pugniere, Martine / Kremer, Eric J

Frontiers in immunology

2021 Volume 12, Page(s) 685218

Abstract: Despite decades of clinical and preclinical investigations, we still poorly grasp our innate immune response to human adenoviruses (HAdVs) and their vectors. In this study, we explored the impact of lactoferrin on three HAdV types that are being used as ... ...

Abstract	Despite decades of clinical and preclinical investigations, we still poorly grasp our innate immune response to human adenoviruses (HAdVs) and their vectors. In this study, we explored the impact of lactoferrin on three HAdV types that are being used as vectors for vaccines. Lactoferrin is a secreted globular glycoprotein that influences direct and indirect innate immune response against a range of pathogens following a breach in tissue homeostasis. The mechanism by which lactoferrin complexes increases HAdV uptake and induce maturation of human phagocytes is unknown. We show that lactoferrin redirects HAdV types from species B, C, and D to Toll-like receptor 4 (TLR4) cell surface complexes. TLR4-mediated internalization of the HAdV-lactoferrin complex induced an NLRP3-associated response that consisted of cytokine release and transient disruption of plasma membrane integrity, without causing cell death. These data impact our understanding of HAdV immunogenicity and may provide ways to increase the efficacy of HAdV-based vectors/vaccines.
MeSH term(s)	Adenoviridae Infections/immunology ; Adenoviridae Infections/pathology ; Adenoviruses, Human/genetics ; Adenoviruses, Human/immunology ; Cytokines/metabolism ; Flow Cytometry ; Humans ; Immunity, Innate ; Lactoferrin/immunology ; Lactoferrin/metabolism ; NLR Family, Pyrin Domain-Containing 3 Protein/genetics ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Phagocytes/virology ; Toll-Like Receptor 4/genetics ; Toll-Like Receptor 4/metabolism
Chemical Substances	Cytokines ; NLR Family, Pyrin Domain-Containing 3 Protein ; NLRP3 protein, human ; TLR4 protein, human ; Toll-Like Receptor 4 ; Lactoferrin (EC 3.4.21.-)
Language	English
Publishing date	2021-05-20
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2021.685218
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Article ; Online: Low-Valent Calix[4]arene Glycoconjugates Based on Hydroxamic Acid Bearing Linkers as Potent Inhibitors in a Model of Ebola Virus Cis-Infection and HCMV-gB-Recombinant Glycoprotein Interaction with MDDC Cells by Blocking DC-SIGN.

Chakroun, Khouloud / Taouai, Marwa / Porkolab, Vanessa / Luczkowiak, Joanna / Sommer, Roman / Cheneau, Coraline / Mathiron, David / Ben Maaouia, Mohamed Amine / Pilard, Serge / Abidi, Rym / Mullié, Catherine / Fieschi, Franck / Cragg, Peter J / Halary, Franck / Delgado, Rafael / Benazza, Mohammed

Journal of medicinal chemistry

2021 Volume 64, Issue 19, Page(s) 14332–14343

Abstract: In addition to a variety of viral-glycoprotein receptors (e.g., heparan sulfate, Niemann-Pick C1, etc.), dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN), from the C-type lectin receptor family, plays one of the ... ...

Abstract	In addition to a variety of viral-glycoprotein receptors (e.g., heparan sulfate, Niemann-Pick C1, etc.), dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN), from the C-type lectin receptor family, plays one of the most important pathogenic functions for a wide range of viruses (e.g., Ebola, human cytomegalovirus (HCMV), HIV-1, severe acute respiratory syndrome coronavirus 2, etc.) that invade host cells before replication; thus, its inhibition represents a relevant extracellular antiviral therapy. We report two novel
MeSH term(s)	Antiviral Agents/chemistry ; Antiviral Agents/metabolism ; Antiviral Agents/pharmacology ; Calixarenes/chemistry ; Cell Adhesion Molecules/antagonists & inhibitors ; Cell Adhesion Molecules/metabolism ; Cell Line ; Cytomegalovirus/metabolism ; Dendritic Cells/cytology ; Dendritic Cells/metabolism ; Ebolavirus/physiology ; Glycoconjugates/chemistry ; Glycoconjugates/metabolism ; Glycoconjugates/pharmacology ; Glycoproteins/antagonists & inhibitors ; Glycoproteins/genetics ; Glycoproteins/metabolism ; Humans ; Hydroxamic Acids/chemistry ; Jurkat Cells ; Lectins, C-Type/antagonists & inhibitors ; Lectins, C-Type/metabolism ; Models, Biological ; Phenols/chemistry ; Protein Binding ; Receptors, Cell Surface/antagonists & inhibitors ; Receptors, Cell Surface/metabolism ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification ; Viral Proteins/antagonists & inhibitors ; Viral Proteins/genetics ; Viral Proteins/metabolism
Chemical Substances	Antiviral Agents ; Cell Adhesion Molecules ; DC-specific ICAM-3 grabbing nonintegrin ; Glycoconjugates ; Glycoproteins ; Hydroxamic Acids ; Lectins, C-Type ; Phenols ; Receptors, Cell Surface ; Recombinant Proteins ; Viral Proteins ; calix(4)arene ; Calixarenes (130036-26-9)
Language	English
Publishing date	2021-09-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218133-2
ISSN	1520-4804 ; 0022-2623
ISSN (online)	1520-4804
ISSN	0022-2623
DOI	10.1021/acs.jmedchem.1c00818
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Article ; Online: Unprecedented Thiacalixarene Fucoclusters as Strong Inhibitors of Ebola cis-Cell Infection and HCMV-gB Glycoprotein/DC-SIGN C-type Lectin Interaction.

Taouai, Marwa / Porkolab, Vanessa / Chakroun, Khouloud / Cheneau, Coraline / Luczkowiak, Joanna / Abidi, Rym / Lesur, David / Cragg, Peter J / Halary, Franck / Delgado, Rafael / Fieschi, Franck / Benazza, Mohammed

Bioconjugate chemistry

2019 Volume 30, Issue 4, Page(s) 1114–1126

Abstract: Glycan-protein interactions control numerous biological events from cell-cell recognition and signaling to pathogen host cell attachment for infections. To infect cells, some viruses bind to immune cells with the help of DC-SIGN (dendritic cell [DC]- ... ...

Abstract	Glycan-protein interactions control numerous biological events from cell-cell recognition and signaling to pathogen host cell attachment for infections. To infect cells, some viruses bind to immune cells with the help of DC-SIGN (dendritic cell [DC]-specific ICAM3-grabbing nonintegrin) C-type lectin expressed on dendritic and macrophage cell membranes, via their envelope protein. Prevention of this infectious interaction is a serious therapeutic option. Here, we describe the synthesis of the first water-soluble tetravalent fucocluster pseudopeptide-based 1,3-alternate thiacalixarenes as viral antigen mimics designed for the inhibition of DC-SIGN, to prevent viral particle uptake. Their preparation exploits straightforward convergent strategies involving one-pot Ugi four-component (Ugi-4CR) and azido-alkyne click chemistry reactions as key steps. Surface plasmon resonance showed strong inhibition of DC-SIGN interaction properties by tetravalent ligands designed with high relative potencies and β avidity factors. All ligands block DC-SIGN active sites at nanomolar IC
MeSH term(s)	Antiviral Agents/pharmacology ; Calixarenes/chemistry ; Calixarenes/pharmacology ; Cell Adhesion Molecules/metabolism ; Hemorrhagic Fever, Ebola/prevention & control ; Humans ; Jurkat Cells ; Lectins, C-Type/metabolism ; Protein Binding ; Receptors, Cell Surface/metabolism ; Viral Envelope Proteins/metabolism
Chemical Substances	Antiviral Agents ; Cell Adhesion Molecules ; DC-specific ICAM-3 grabbing nonintegrin ; Lectins, C-Type ; Receptors, Cell Surface ; Viral Envelope Proteins ; glycoprotein B, Simplexvirus ; Calixarenes (130036-26-9)
Language	English
Publishing date	2019-04-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1024041-x
ISSN	1520-4812 ; 1043-1802
ISSN (online)	1520-4812
ISSN	1043-1802
DOI	10.1021/acs.bioconjchem.9b00066
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Article ; Online: Correction to Unprecedented Thiacalixarene Fucoclusters as Strong Inhibitors of Ebola cis-Cell Infection and HCMV-gB Glycoprotein/DC-SIGN C-type Lectin Interaction.

Bioconjugate chemistry

2019 Volume 30, Issue 6, Page(s) 1830–1831

Language	English
Publishing date	2019-05-10
Publishing country	United States
Document type	Journal Article ; Published Erratum
ZDB-ID	1024041-x
ISSN	1520-4812 ; 1043-1802
ISSN (online)	1520-4812
ISSN	1043-1802
DOI	10.1021/acs.bioconjchem.9b00300
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Article ; Online: Fine Mapping the Interaction Between Dendritic Cell-Specific Intercellular Adhesion Molecule (ICAM)-3-Grabbing Nonintegrin and the Cytomegalovirus Envelope Glycoprotein B.

Chéneau, Coraline / Coulon, Flora / Porkolab, Vanessa / Fieschi, Franck / Laurant, Stéphanie / Razanajaona-Doll, Diane / Pin, Jean-Jacques / Borst, Eva Maria / Messerle, Martin / Bressollette-Bodin, Céline / Halary, Franck

The Journal of infectious diseases

2018 Volume 218, Issue 3, Page(s) 490–503

Abstract: Background: Human cytomegalovirus (HCMV) is a leading cause of virally induced congenital disorders and morbidities in immunocompromised individuals, ie, transplant, cancer, or acquired immune deficiency syndrome patients. Human cytomegalovirus infects ... ...

Abstract	Background: Human cytomegalovirus (HCMV) is a leading cause of virally induced congenital disorders and morbidities in immunocompromised individuals, ie, transplant, cancer, or acquired immune deficiency syndrome patients. Human cytomegalovirus infects virtually all cell types through the envelope glycoprotein complex gH/gL/gO with or without a contribution of the pentameric gH/gL/pUL128L. Together with gH/gL, the HCMV envelope glycoprotein B (gB) contributes to the viral fusion machinery. Methods: We previously showed that gB is a ligand for the C-type lectin dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) contributing to HCMV attachment to and infection of DC-SIGN-expressing cells. However, the features of the DC-SIGN/gB interaction remain unclear. To address this point, the role of glycans on gB and the consequences of mutagenesis and antibody-mediated blockades on both partners were examined in this study. Results: We identified DC-SIGN amino acid residues involved in this interaction through an extensive mutagenesis study. We also showed the importance of high-mannose N-glycans decorating the asparagine residue at position 208, demonstrating that the antigenic domain 5 on gB is involved in the interaction with DC-SIGN. Finally, antibody-mediated blockades allowed us to identify DC-SIGN as a major HCMV attachment receptor on monocyte-derived dendritic cells. Conclusions: Taken together, these results have permitted us to fine-map the interaction between DC-SIGN and HCMV gB.
MeSH term(s)	Cell Adhesion Molecules/genetics ; Cell Adhesion Molecules/metabolism ; Cells, Cultured ; Cytomegalovirus/physiology ; DNA Mutational Analysis ; Dendritic Cells/virology ; Host-Pathogen Interactions ; Humans ; Lectins, C-Type/genetics ; Lectins, C-Type/metabolism ; Mutant Proteins/genetics ; Mutant Proteins/metabolism ; Polysaccharides/metabolism ; Protein Binding ; Protein Interaction Mapping ; Receptors, Cell Surface/genetics ; Receptors, Cell Surface/metabolism ; Receptors, Virus/genetics ; Receptors, Virus/metabolism ; Viral Envelope Proteins/genetics ; Viral Envelope Proteins/metabolism ; Virus Attachment
Chemical Substances	Cell Adhesion Molecules ; DC-specific ICAM-3 grabbing nonintegrin ; Lectins, C-Type ; Mutant Proteins ; Polysaccharides ; Receptors, Cell Surface ; Receptors, Virus ; Viral Envelope Proteins ; glycoprotein B, Simplexvirus
Language	English
Publishing date	2018-04-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3019-3
ISSN	1537-6613 ; 0022-1899
ISSN (online)	1537-6613
ISSN	0022-1899
DOI	10.1093/infdis/jiy194
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Article ; Online: Functional Langerinhigh-Expressing Langerhans-like Cells Can Arise from CD14highCD16- Human Blood Monocytes in Serum-Free Condition.

Picarda, Gaëlle / Chéneau, Coraline / Humbert, Jean-Marc / Bériou, Gaëlle / Pilet, Paul / Martin, Jérôme / Duteille, Franck / Perrot, Pierre / Bellier-Waast, Frédérique / Heslan, Michèle / Haspot, Fabienne / Guillon, Fabien / Josien, Regis / Halary, Franck Albert

Journal of immunology (Baltimore, Md. : 1950)

2016 Volume 196, Issue 9, Page(s) 3716–3728

Abstract: Langerhans cells (LCs) are epithelial APCs that sense danger signals and in turn trigger specific immune responses. In steady-state, they participate in the maintenance of peripheral tolerance to self-antigens whereas under inflammation LCs efficiently ... ...

Abstract	Langerhans cells (LCs) are epithelial APCs that sense danger signals and in turn trigger specific immune responses. In steady-state, they participate in the maintenance of peripheral tolerance to self-antigens whereas under inflammation LCs efficiently trigger immune responses in secondary lymphoid organs. It has been demonstrated in mice that LC-deprived epithelia are rapidly replenished by short half-life langerin-expressing monocyte-derived LCs (MDLCs). These surrogate LCs are thought to be progressively replaced by langerin(high) LCs arising from self-renewing epithelial precursors of hematopoietic origin. How LCs arise from blood monocytes is not fully understood. Hence, we sought to characterize key factors that induce differentiation of langerin(high)-expressing monocyte-derived Langerhans-like cells. We identified GM-CSF and TGF-β1 as key cytokines to generate langerin(high)-expressing cells but only in serum-free conditions. These cells were shown to express the LC-specific TROP-2 and Axl surface markers and contained Birbeck granules. Surprisingly, E-cadherin was not spontaneously expressed by these cells but required a direct contact with keratinocytes to be stably induced. MDLCs induced stronger allogeneic T cell proliferations but released low amounts of inflammatory cytokines upon TLR stimulation compared with donor-paired monocyte-derived dendritic cells. Immature langerin(high) MDLCs were responsive to MIP-3β/CCL20 and CTAC/CCL27 chemokine stimulations. Finally, we demonstrated that those cells behaved as bona fide LCs when inserted in a three-dimensional rebuilt epithelium by becoming activated upon TLR or UV light stimulations. Collectively, these results prompt us to propose these langerin(high) MDLCs as a relevant model to address LC biology-related questions.
MeSH term(s)	Antigens, Neoplasm/metabolism ; Blood Cells/physiology ; Cell Adhesion Molecules/metabolism ; Cell Differentiation ; Cells, Cultured ; Granulocyte-Macrophage Colony-Stimulating Factor/metabolism ; Humans ; Isoantigens/immunology ; Keratinocytes/physiology ; Langerhans Cells/immunology ; Lipopolysaccharide Receptors/metabolism ; Lymphocyte Activation ; Monocytes/physiology ; Proto-Oncogene Proteins/metabolism ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptors, IgG/metabolism ; Self Tolerance ; T-Lymphocytes/immunology ; Transforming Growth Factor beta1/metabolism ; Ultraviolet Rays
Chemical Substances	Antigens, Neoplasm ; Cell Adhesion Molecules ; Isoantigens ; Lipopolysaccharide Receptors ; Proto-Oncogene Proteins ; Receptors, IgG ; TACSTD2 protein, human ; Transforming Growth Factor beta1 ; Granulocyte-Macrophage Colony-Stimulating Factor (83869-56-1) ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; axl receptor tyrosine kinase (EC 2.7.10.1)
Language	English
Publishing date	2016--01
Publishing country	United States
Document type	Journal Article
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.1501304
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Article ; Online: RhoB Mediates Phosphoantigen Recognition by Vγ9Vδ2 T Cell Receptor.

Sebestyen, Zsolt / Scheper, Wouter / Vyborova, Anna / Gu, Siyi / Rychnavska, Zuzana / Schiffler, Marleen / Cleven, Astrid / Chéneau, Coraline / van Noorden, Martje / Peigné, Cassie-Marie / Olive, Daniel / Lebbink, Robert Jan / Oostvogels, Rimke / Mutis, Tuna / Schuurhuis, Gerrit Jan / Adams, Erin J / Scotet, Emmanuel / Kuball, Jürgen

Cell reports

2016 Volume 15, Issue 9, Page(s) 1973–1985

Abstract: Human Vγ9Vδ2 T cells respond to tumor cells by sensing elevated levels of phosphorylated intermediates of the dysregulated mevalonate pathway, which is translated into activating signals by the ubiquitously expressed butyrophilin A1 (BTN3A1) through yet ... ...

Abstract	Human Vγ9Vδ2 T cells respond to tumor cells by sensing elevated levels of phosphorylated intermediates of the dysregulated mevalonate pathway, which is translated into activating signals by the ubiquitously expressed butyrophilin A1 (BTN3A1) through yet unknown mechanisms. Here, we developed an unbiased, genome-wide screening method that identified RhoB as a critical mediator of Vγ9Vδ2 TCR activation in tumor cells. Our results show that Vγ9Vδ2 TCR activation is modulated by the GTPase activity of RhoB and its redistribution to BTN3A1. This is associated with cytoskeletal changes that directly stabilize BTN3A1 in the membrane, and the subsequent dissociation of RhoB from BTN3A1. Furthermore, phosphoantigen accumulation induces a conformational change in BTN3A1, rendering its extracellular domains recognizable by Vγ9Vδ2 TCRs. These complementary events provide further evidence for inside-out signaling as an essential step in the recognition of tumor cells by a Vγ9Vδ2 TCR.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Antigens/metabolism ; Antigens, CD/chemistry ; Antigens, CD/metabolism ; Butyrophilins/chemistry ; Butyrophilins/metabolism ; Cell Line, Tumor ; Cell Membrane/metabolism ; Genetic Loci ; HEK293 Cells ; Humans ; Lymphocyte Activation/immunology ; Models, Biological ; Neoplastic Stem Cells/metabolism ; Phosphorylation ; Polymorphism, Single Nucleotide/genetics ; Protein Binding ; Protein Conformation ; Protein Multimerization ; RNA, Small Interfering/metabolism ; Receptors, Antigen, T-Cell, gamma-delta/metabolism ; rhoB GTP-Binding Protein/metabolism
Chemical Substances	Antigens ; Antigens, CD ; BTN3A1 protein, human ; Butyrophilins ; RNA, Small Interfering ; Receptors, Antigen, T-Cell, gamma-delta ; rhoB GTP-Binding Protein (EC 3.6.5.2)
Language	English
Publishing date	2016-05-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2016.04.081
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Article ; Online: HIV-1 Neutralizing Antibody Signatures and Application to Epitope-Targeted Vaccine Design.

Bricault, Christine A / Yusim, Karina / Seaman, Michael S / Yoon, Hyejin / Theiler, James / Giorgi, Elena E / Wagh, Kshitij / Theiler, Maxwell / Hraber, Peter / Macke, Jennifer P / Kreider, Edward F / Learn, Gerald H / Hahn, Beatrice H / Scheid, Johannes F / Kovacs, James M / Shields, Jennifer L / Lavine, Christy L / Ghantous, Fadi / Rist, Michael /

Cell host & microbe

2019 Volume 25, Issue 1, Page(s) 59–72.e8

Abstract: Eliciting HIV-1-specific broadly neutralizing antibodies (bNAbs) remains a challenge for vaccine development, and the potential of passively delivered bNAbs for prophylaxis and therapeutics is being explored. We used neutralization data from four large ... ...

Abstract	Eliciting HIV-1-specific broadly neutralizing antibodies (bNAbs) remains a challenge for vaccine development, and the potential of passively delivered bNAbs for prophylaxis and therapeutics is being explored. We used neutralization data from four large virus panels to comprehensively map viral signatures associated with bNAb sensitivity, including amino acids, hypervariable region characteristics, and clade effects across four different classes of bNAbs. The bNAb signatures defined for the variable loop 2 (V2) epitope region of HIV-1 Env were then employed to inform immunogen design in a proof-of-concept exploration of signature-based epitope targeted (SET) vaccines. V2 bNAb signature-guided mutations were introduced into Env 459C to create a trivalent vaccine, and immunization of guinea pigs with V2-SET vaccines resulted in increased breadth of NAb responses compared with Env 459C alone. These data demonstrate that bNAb signatures can be utilized to engineer HIV-1 Env vaccine immunogens capable of eliciting antibody responses with greater neutralization breadth.
MeSH term(s)	Amino Acid Sequence ; Animals ; Antibodies, Neutralizing/immunology ; Antibodies, Neutralizing/therapeutic use ; Antibody Formation ; Disease Models, Animal ; Epitopes/genetics ; Epitopes/immunology ; Female ; Guinea Pigs ; HEK293 Cells ; HIV Antibodies/immunology ; HIV Envelope Protein gp120/immunology ; HIV Infections/immunology ; HIV Infections/prevention & control ; HIV Infections/virology ; HIV-1/genetics ; Humans ; Immunization ; Inhibitory Concentration 50 ; Models, Molecular ; Mutation ; Peptide Fragments/immunology ; Protein Binding ; Vaccination ; Vaccines ; env Gene Products, Human Immunodeficiency Virus/genetics ; env Gene Products, Human Immunodeficiency Virus/immunology
Chemical Substances	Antibodies, Neutralizing ; Epitopes ; HIV Antibodies ; HIV Envelope Protein gp120 ; HIV envelope protein gp120 (305-321) ; Peptide Fragments ; Vaccines ; env Gene Products, Human Immunodeficiency Virus
Language	English
Publishing date	2019-01-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2018.12.001
Database	MEDical Literature Analysis and Retrieval System OnLINE

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