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2. The human CD47 checkpoint is targeted by an immunosuppressive Aedes aegypti salivary factor to enhance arboviral skin infectivity.

Author

Marin-Lopez, Alejandro, Huck, John D., Esterly, Allen T., Azcutia, Veronica, Rosen, Connor, Garcia-Milian, Rolando, Sefik, Esen, Vidal-Pedrola, Gemma, Raduwan, Hamidah, Chen, Tse-Yu, Arora, Gunjan, Halene, Stephanie, Shaw, Albert C., Palm, Noah W., Flavell, Richard A., Parkos, Charles A., Thangamani, Saravanan, Ring, Aaron M., and Fikrig, Erol

Subjects
SALIVARY proteins, ZIKA virus infections, ARBOVIRUS diseases, LEUCOCYTES, ARBOVIRUSES, ZIKA virus, AEDES aegypti
Abstract

The Aedes aegypti mosquito is a vector of many infectious agents, including flaviviruses such as Zika virus. Components of mosquito saliva have pleomorphic effects on the vertebrate host to enhance blood feeding, and these changes also create a favorable niche for pathogen replication and dissemination. Here, we demonstrate that human CD47, which is known to be involved in various immune processes, interacts with a 34-kilodalton mosquito salivary protein named Nest1. Nest1 is up-regulated in blood-fed female A. aegypti and facilitates Zika virus dissemination in human skin explants. Nest1 has a stronger affinity for CD47 than its natural ligand, signal regulatory protein α, competing for binding at the same interface. The interaction between Nest1 with CD47 suppresses phagocytosis by human macrophages and inhibits proinflammatory responses by white blood cells, thereby suppressing antiviral responses in the skin. This interaction elucidates how an arthropod protein alters the human response to promote arbovirus infectivity. Editor's summary: Aedes aegypti mosquitos can transmit arboviruses during blood feeding, and components of mosquito saliva may enhance both blood feeding and virus transmission. Marin-Lopez et al. identified a 34-kDa mosquito salivary protein called Nest1, highly expressed in the saliva of female A. aegypti mosquitos, as a high-affinity binder to human CD47. In human skin explants infected with Zika virus, Nest1 increased virus burden and inhibited some CD47-governed immune functions like phagocytosis and proinflammatory responses in immune cells, thus inhibiting antiviral responses. These findings provide insight into how mosquito salivary proteins can potentially facilitate arbovirus infection. —Christiana Fogg [ABSTRACT FROM AUTHOR]

Published
2024
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7. Macrophage-derived IL-10 mediates mucosal repair by epithelial WISP-1 signaling

Author

Quiros, Miguel, Nishio, Hikaru, Neumann, Philipp A., Siuda, Dorothee, Brazil, Jennifer C., Azcutia, Veronica, Hilgarth, Roland, O'Leary, Monique N., Garcia-Hernandez, Vicky, Leoni, Giovanna, Feng, Mingli, Bernal, Gabriela, Williams, Holly, Dedhia, Priya H., Gerner-Smidt, Christian, Spence, Jason, Parkos, Charles A., Denning, Timothy L., and Nusrat, Asma

Subjects
Interleukins -- Health aspects, Macrophages -- Health aspects, Epithelial cells -- Health aspects, Cellular signal transduction -- Health aspects, Health care industry
Abstract

In response to injury, epithelial cells migrate and proliferate to cover denuded mucosal surfaces and repair the barrier defect. This process is orchestrated by dynamic crosstalk between immune cells and the epithelium; however, the mechanisms involved remain incompletely understood. Here, we report that IL-10 was rapidly induced following intestinal mucosal injury and was required for optimal intestinal mucosal wound closure. Conditional deletion of IL-10 specifically in CD11c-expressing cells in vivo implicated macrophages as a critical innate immune contributor to IL-10-induced wound closure. Consistent with these findings, wound closure in T cell- and B cell-deficient [Rag1.sup.-/ -] mice was unimpaired, demonstrating that adaptive immune cells are not absolutely required for this process. Further, following mucosal injury, macrophage-derived IL-10 resulted in epithelial cAMP response element-binding protein (CREB) activation and subsequent synthesis and secretion of the pro-repair WNT1-inducible signaling protein 1 (WISP-1). WISP-1 induced epithelial cell proliferation and wound closure by activating epithelial pro-proliferative pathways. These findings define the involvement of macrophages in regulating an IL-10/CREB/WISP-1 signaling axis, with broad implications in linking innate immune activation to mucosal wound repair., Introduction The gastrointestinal epithelium forms a selective barrier that plays a pivotal role in separating the microbe-rich luminal contents from underlying tissue compartments, while also regulating the absorption of nutrients. [...]

Published
2017
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9. A DOCK8-WIP-WASp complex links T cell receptors to the actin cytoskeleton

Author

Janssen, Erin, Tohme, Mira, Hedayat, Mona, Leick, Marion, Kumari, Sudha, Ramesh, Narayanaswamy, Massaad, Michel J., Ullas, Sumana, Azcutia, Veronica, Goodnow, Christopher C., Randall, Katrina L., Qiao, Qi, Wu, Hao, Herz, Waleed Al-, Cox, Dianne, Hartwig, John, Irvine, Darrell J., Luscinskas, Francis W., and Geha, Raif S.

Subjects
Gene mutations -- Health aspects, Cytoskeletal proteins -- Properties, Wiskott-Aldrich syndrome -- Genetic aspects -- Development and progression, Phenotype -- Health aspects, Health care industry
Abstract

Wiskott-Aldrich syndrome (WAS) is associated with mutations in the WAS protein (WASp), which plays a critical role in the initiation of T cell receptor-driven (TCR-driven) actin polymerization. The clinical phenotype of WAS includes susceptibility to infection, allergy, autoimmunity, and malignancy and overlaps with the symptoms of dedicator of cytokinesis 8 (DOCK8) deficiency, suggesting that the 2 syndromes share common pathogenic mechanisms. Here, we demonstrated that the WASp-interacting protein (WIP) bridges DOCK8 to WASp and actin in T cells. We determined that the guanine nucleotide exchange factor activity of DOCK8 is essential for the integrity of the subcortical actin cytoskeleton as well as for TCR-driven WASp activation, F-actin assembly, immune synapse formation, actin foci formation, mechanotransduction, T cell transendothelial migration, and homing to lymph nodes, all of which also depend on WASp. These results indicate that DOCK8 and WASp are in the same signaling pathway that links TCRs to the actin cytoskeleton in TCR-driven actin assembly. Further, they provide an explanation for similarities in the clinical phenotypes of WAS and DOCK8 deficiency., Introduction The integrity of the actin cytoskeleton is important for T cell migration into tissues, defense against pathogens, and immunosurveillance (1). The Wiskott-Aldrich syndrome (WAS) protein WASp plays an important [...]

Published
2016
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23. Formyl peptide receptor 2 regulates monocyte recruitment to promote intestinal mucosal wound repair

Author

Birkl, Dorothee, primary, O'Leary, Monique N., additional, Quiros, Miguel, additional, Azcutia, Veronica, additional, Schaller, Matthew, additional, Reed, Michelle, additional, Nishio, Hikaru, additional, Keeney, Justin, additional, Neish, Andrew S., additional, Lukacs, Nicholas W., additional, Parkos, Charles A., additional, and Nusrat, Asma, additional

Published
2019
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24. FPR2 regulates monocyte recruitment to promote mucosal wound repair

Author

O'Leary, Monique N., primary, Birkl, Dorothee, additional, Quiros, Miguel, additional, Reed, Michelle, additional, Azcutia, Veronica, additional, Schaller, Matthew, additional, Nishio, Hikaru, additional, Keeney, Justin, additional, Lukacs, Nicholas W., additional, Neish, Andrew S., additional, Parkos, Charles A., additional, and Nusrat, Asma, additional

Published
2019
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31. A DOCK8-WIP-WASp complex links T cell receptors to the actin cytoskeleton

Author

Massachusetts Institute of Technology. Department of Biological Engineering, Koch Institute for Integrative Cancer Research at MIT, Kumari, Sudha, Irvine, Darrell J, Janssen, Erin, Tohme, Mira, Hedayat, Mona, Leick, Marion, Ramesh, Narayanaswamy, Massaad, Michel J., Ullas, Sumana, Azcutia, Veronica, Goodnow, Christopher C., Randall, Katrina L., Qiao, Qi, Wu, Hao, Al-Herz, Waleed, Cox, Dianne, Hartwig, John, Luscinskas, Francis W., Geha, Raif S., Massachusetts Institute of Technology. Department of Biological Engineering, Koch Institute for Integrative Cancer Research at MIT, Kumari, Sudha, Irvine, Darrell J, Janssen, Erin, Tohme, Mira, Hedayat, Mona, Leick, Marion, Ramesh, Narayanaswamy, Massaad, Michel J., Ullas, Sumana, Azcutia, Veronica, Goodnow, Christopher C., Randall, Katrina L., Qiao, Qi, Wu, Hao, Al-Herz, Waleed, Cox, Dianne, Hartwig, John, Luscinskas, Francis W., and Geha, Raif S.

Abstract

Wiskott-Aldrich syndrome (WAS) is associated with mutations in the WAS protein (WASp), which plays a critical role in the initiation of T cell receptor–driven (TCR-driven) actin polymerization. The clinical phenotype of WAS includes susceptibility to infection, allergy, autoimmunity, and malignancy and overlaps with the symptoms of dedicator of cytokinesis 8 (DOCK8) deficiency, suggesting that the 2 syndromes share common pathogenic mechanisms. Here, we demonstrated that the WASp-interacting protein (WIP) bridges DOCK8 to WASp and actin in T cells. We determined that the guanine nucleotide exchange factor activity of DOCK8 is essential for the integrity of the subcortical actin cytoskeleton as well as for TCR-driven WASp activation, F-actin assembly, immune synapse formation, actin foci formation, mechanotransduction, T cell transendothelial migration, and homing to lymph nodes, all of which also depend on WASp. These results indicate that DOCK8 and WASp are in the same signaling pathway that links TCRs to the actin cytoskeleton in TCR-driven actin assembly. Further, they provide an explanation for similarities in the clinical phenotypes of WAS and DOCK8 deficiency., United States. Public Health Service (RO1AI114588), United States. Public Health Service (K08AI114968 )

Published
2017

33. Defects in CD4+ T cell LFA-1 integrin-dependent adhesion and proliferation protect Cd47−/− mice from EAE

Author

Azcutia, Veronica, primary, Bassil, Ribal, additional, Herter, Jan M, additional, Engelbertsen, Daniel, additional, Newton, Gail, additional, Autio, Anu, additional, Mayadas, Tanya, additional, Lichtman, Andrew H, additional, Khoury, Samia J, additional, Parkos, Charles A, additional, Elyaman, Wassim, additional, and Luscinskas, Francis W, additional

Published
2016
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35. Role of negative regulation of immune signaling pathways in neutrophil function.

Author

Azcutia, Veronica, Parkos, Charles A., and Brazil, Jennifer C.

Subjects
NEUTROPHILS, INFLAMMATION, AUTOIMMUNE diseases, IMMUNE system, TISSUES
Abstract

Polymorphonuclear neutrophils (PMNs) play a critical role in host defense against infection and in the resolution of inflammation. However, immune responses mediated by PMN must be tightly regulated to facilitate elimination of invading pathogens without inducing detrimental inflammation and host tissue damage. Specific engagement of cell surface immunoreceptors by a diverse range of extracellular signals regulates PMN effector functions through differential activation of intracellular signaling cascades. Althoughmechanisms of PMNactivation mediated via cell signaling pathways have been well described, less is known about negative regulation of PMN function by immune signaling cascades. Here, we provide an overview of immunoreceptor-mediated negative regulation of keyPMNeffector functions including maturation, migration, phagocytosis, reactive oxygen species release, degranulation, apoptosis, and NET formation. Increased understanding of mechanisms of suppression of PMN effector functions may point to possible future therapeutic targets for the amelioration of PMN-mediated autoimmune and inflammatory diseases. [ABSTRACT FROM AUTHOR]

Published
2018
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38. Migration of Myeloid Cells during Inflammation Is Differentially Regulated by the Cell Surface Receptors Slamf1 and Slamf8

Author

Wang, Guoxing, primary, van Driel, Boaz J., additional, Liao, Gongxian, additional, O’Keeffe, Michael S., additional, Halibozek, Peter J., additional, Flipse, Jacky, additional, Yigit, Burcu, additional, Azcutia, Veronica, additional, Luscinskas, Francis W., additional, Wang, Ninghai, additional, and Terhorst, Cox, additional

Published
2015
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41. CD47 plays a critical role in T-cell recruitment by regulation of LFA-1 and VLA-4 integrin adhesive functions

Author

Azcutia, Veronica, primary, Routledge, Matthew, additional, Williams, Marcie R., additional, Newton, Gail, additional, Frazier, William A., additional, Manica, Andrè, additional, Croce, Kevin J., additional, Parkos, Charles A., additional, Schmider, Angela B., additional, Turman, Melissa V., additional, Soberman, Roy J., additional, and Luscinskas, Francis W., additional

Published
2013
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45. IL-17 and TNF-α Sustain Neutrophil Recruitment during Inflammation through Synergistic Effects on Endothelial Activation

Author

Griffin, Gabriel K., primary, Newton, Gail, additional, Tarrio, Margarite L., additional, Bu, De-xiu, additional, Maganto-Garcia, Elena, additional, Azcutia, Veronica, additional, Alcaide, Pilar, additional, Grabie, Nir, additional, Luscinskas, Francis W., additional, Croce, Kevin J., additional, and Lichtman, Andrew H., additional

Published
2012
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46. Slamf1 controls monocyte / macrophage migration in experimental colitis. (117.5)

Author

van Driel, Boaz, primary, Liao, Gongxian, additional, Romero, Javier, additional, Faubion, William, additional, Wang, Guoxing, additional, Berger, Scott, additional, O'Keeffe, Michael, additional, Magelky, Erica, additional, Manocha, Monika, additional, Azcutia, Veronica, additional, de Waal Malefyt, Rene, additional, Grisham, Matthew, additional, Luscinskas, F., additional, Mizoguchi, Emiko, additional, Bhan, Atul, additional, Wang, Ninghai, additional, and Terhorst, Cox, additional

Published
2012
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48. Defects in CD4+T cell LFA-1 integrin-dependent adhesion and proliferation protect Cd47-/-mice from EAE

Author

Azcutia, Veronica, Bassil, Ribal, Herter, Jan M., Engelbertsen, Daniel, Newton, Gail, Autio, Anu, Mayadas, Tanya, Lichtman, Andrew H., Khoury, Samia J., Parkos, Charles A., Elyaman, Wassim, and Luscinskas, Francis W.

Abstract

CD47 is known to play an important role in CD4+T cell homeostasis. We recently reported a reduction in mice deficient in the Cd47gene (Cd47-/-) CD4+T cell adhesion and transendothelial migration (TEM) in vivo and in vitro as a result of impaired expression of high-affinity forms of LFA-1 and VLA-4 integrins. A prior study concluded that Cd47-/-mice were resistant to experimental autoimmune encephalomyelitis (EAE) as a result of complete failure in CD4+T cell activation after myelin oligodendrocyte glycoprotein peptide 35–55 aa (MOG35–55) immunization. As the prior EAE study was published before our report, authors could not have accounted for defects in T cell integrin function as a mechanism to protect Cd47-/-in EAE. Thus, we hypothesized that failure of T cell activation involved defects in LFA-1 and VLA-4 integrins. We confirmed that Cd47-/-mice were resistant to MOG35–55-induced EAE. Our data, however, supported a different mechanism that was not a result of failure of CD4+T cell activation. Instead, we found that CD4+T cells in MOG35–55-immunized Cd47-/-mice were activated, but clonal expansion contracted within 72 h after immunization. We used TCR crosslinking and mitogen activation in vitro to investigate the underlying mechanism. We found that naïve Cd47-/-CD4+T cells exhibited a premature block in proliferation and survival because of impaired activation of LFA-1, despite effective TCR-induced activation. These results identify CD47 as an important regulator of LFA-1 and VLA-4 integrin-adhesive functions in T cell proliferation, as well as recruitment, and clarify the roles played by CD47 in MOG35–55-induced EAE.

Published
2017
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50. Glycosylated human oxyhaemoglobin activates nuclear factor-kappaB and activator protein-1 in cultured human aortic smooth muscle.

Author

Peiro, Concepcion, Matesanz, Nuria, Nevado, Julian, Lafuente, Nuria, Cercas, Elena, Azcutia, Veronica, Vallejo, Susana, Rodriguez-Manas, Leocadio, and Sanchez-Ferrer, Carlos F

Abstract

Diabetic vessels undergo structural changes that are linked to a high incidence of cardiovascular diseases. Reactive oxygen species (ROS) mediate cell signalling in the vasculature, where they can promote cell growth and activate redox-regulated transcription factors, like activator protein-1 (AP-1) or nuclear factor-kappaB (NF-kappaB), which are involved in remodelling and inflammation processes. Amadori adducts, formed through nonenzymatic glycosylation, can contribute to ROS formation in diabetes. In this study, we analysed whether Amadori-modified human oxyhaemoglobin, glycosylated at either normal (N-Hb) or elevated (E-Hb) levels, can induce cell growth and activate AP-1 and NF-kappaB in cultured human aortic smooth muscle cells (HASMC). E-Hb (1 nm-1 x microm), but not N-Hb, promoted a concentration-dependent increase in cell size from nanomolar concentrations, although it failed to stimulate HASMC proliferation. At 10 nm, E-Hb stimulated both AP-1 and NF-kappaB activity, as assessed by transient transfection, electromobility shift assays or immunofluorescence staining. The effects of E-Hb resembled those of the proinflammatory cytokine tumour necrosis factor-alpha (TNF-alpha). E-Hb enhanced intracellular superoxide anions content and its effects on HASMC were abolished by different ROS scavengers. In conclusion, E-Hb stimulates growth and activates AP-1 and NF-kappaB in human vascular smooth muscle by redox-sensitive pathways, thus suggesting a possible direct role for Amadori adducts in diabetic vasculopathy. [ABSTRACT FROM AUTHOR]

Published
2003
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