Regulation of T cell trafficking by the T cell immunoglobulin and mucin domain 1 glycoprotein

Angiari, Stefano; Constantin, Gabriela

doi:10.1016/j.molmed.2014.10.003

Cited by 26 publications

(23 citation statements)

References 132 publications

(244 reference statements)

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“…Tim-1 functions as a costimulatory molecule following T-cell receptor (TCR) signaling, particularly after Th2 polarization [7][8][9]. Additionally, Tim-1 has been reported to be a major ligand for endothelial P-selectin, and have a function to regulate T-cell trafficking in inflamed tissues [39,40]. Tim-1 is also expressed in other immune cells such as dendritic cells and mast cells, and plays different roles in each cell type [41][42][43][44].…”

Section: Discussionmentioning

confidence: 99%

Expression of Tim‐1 in primary CNS lymphoma

et al. 2016

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Primary central nervous system lymphoma (PCNSL) is a distinct subtype of extranodal lymphoma with aggressive clinical course and poor outcome. As increased IL‐10/IL‐6 ratio is recognized in the cerebrospinal fluid (CSF) of PCNSL patients, we hypothesized that PCNSL might originate from a population of B cells with high IL‐10‐producing capacity, an equivalent of “regulatory B cells” in mice. We intended in this study to clarify whether Tim‐1, a molecule known as a marker for regulatory B cells in mice, is expressed in PCNSL. By immunohistochemical analysis, Tim‐1 was shown to be positive in as high as 54.2% of PCNSL (26 of 58 samples), while it was positive in 19.1% of systemic diffuse large B‐cell lymphoma (DLBCL) samples (17 of 89 samples; P < 0.001). Tim‐1 expression positively correlated with IL‐10 expression in PCNSL (Cramer's V = 0.55, P < 0.001), and forced expression of Tim‐1 in a PCNSL cell line resulted in increased IL‐10 secretion, suggesting that Tim‐1 is functionally linked with IL‐10 production in PCNSL. Moreover, soluble Tim‐1 was detectable in the CSF of PCNSL patients, and was suggested to parallel disease activity. In summary, PCNSL is characterized by frequent Tim‐1 expression, and its soluble form in CSF may become a useful biomarker for PCNSL.

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Section: Discussionmentioning

confidence: 99%

Expression of Tim‐1 in primary CNS lymphoma

et al. 2016

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“…The following are available online at http://www.mdpi.com/2079-6412/10/4/403/s1, Figure S1: Schematic illustration of fabrication of Au nanoporous substrate, Figure S2: HR-FETEM image of optimized Au nanoporous substrate and EDS mappings of areas marked in HR-FETEM image, Figure S3: SPR spectra of as-fabricated Au nanoporous substrate created at deposition rates of (a) 0.3 Å/s and (b) 1 Å/s with optimized dealloying times (120 and 150 s, respectively). (c) COMSOL calculation of smooth and roughed Au nanocavity, Figure S4: Relationship of relative Raman intensities for various mutants and antibody-sulfotyrosine interactions on Au nanoporous substrate determined using ISERS peak regions at 990-1010 and 1601-1636 cm −1 , Figure S5: VP1 of EV71 on Au nanoporous substrate examined at Raman laser wavelength of 633 nm, Table S1: Nanopore size and contact angle of as-fabricated Au nanoporous substrates, Table S2: Raman assignment for protein immobilized on Au nanoporous substrate [1][2][3][4][5][6][7][8][9][10][11][12], Table S3: Raman assignment for protein mutants on Au nanoporous substrate [1][2][3][4][5][6][7][8][9][10][11][12], Table S4: Raman assignment for protein-antibody interaction on Au nanoporous substrate [1][2][3][4][5][6]…”

Section: Supplementary Materialsmentioning

confidence: 99%

“…Protein tyrosine sulfation (PTS) is a significant post-translational modification that occurs via the tyrosyl protein sulfotransferase (TPST) catalyst through the transfer of the sulfuryl group (SO 3 −1 ) from 3'-phosphoadenosine-5'-phosphosulfate, resulting in the addition of a specific tyrosyl residue within a target protein [1][2][3][4]. PTS is of vital importance as it facilitates protein-protein interactions (PPIs), which regulate many biological events, such as virus infection, inflammation, immune responses, and physiological and pathological diseases [3,[5][6][7][8]. Notably, the pathogenic mechanism can be…”

Section: Introductionmentioning

confidence: 99%

Mutated Human P-Selectin Glycoprotein Ligand-1 and Viral Protein-1 of Enterovirus 71 Interactions on Au Nanoplasmonic Substrate for Specific Recognition by Surface-Enhanced Raman Spectroscopy

et al. 2020

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Protein tyrosine sulfation is a common post-translational modification that stimulates intercellular or extracellular protein-protein interactions and is responsible for various important biological processes, including coagulation, inflammation, and virus infections. Recently, human P-selectin glycoprotein ligand-1 (PSGL-1) has been shown to serve as a functional receptor for enterovirus 71 (EV71). It has been proposed that the capsid viral protein VP1 of EV71 is directly involved in this specific interaction with sulfated or mutated PSGL-1. Surface-enhanced Raman spectroscopy (SERS) is used to distinguish PSGL-1 and VP1 interactions on an Au nanoporous substrate and identify specific VP1 interaction positions of tyrosine residue sites (46, 48, and 51). The three tyrosine sites in PSGL-1 were replaced by phenylalanine (F), as determined using SERS. A strong phenylalanine SERS signal was obtained in three regions of the mutated protein on the nanoporous substrate. The mutated protein positions at (51F) and (48F, 51F) produced a strong SERS peak at 1599–1666 cm−1, which could be related to a binding with the mutated protein and anti-sulfotyrosine interactions on the nanoporous substrate. A strong SERS effect of the mutated protein and VP1 interactions appeared at (48F), (51F), and (46F, 48F). In these positions, there was less interaction with VP1, as indicated by a strong phenylalanine signal from the mutated protein.

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“…TIM-1 also serves as a pattern recognition receptor on invariant natural killer cells (iNKT), which mediate cell activation by TIMs binding to phosphatidylserine on the surface of cells undergoing apoptosis (147). It is very likely that TIM-3, an inhibitory checkpoint receptor on membrane effector cells, binds also to phosphatidylserine of the EBOV envelope (92,93). EBOV can induce dysfunction and even apoptosis in effector cells by binding to Siglecs-7,-5,-3,-8,-9, TIM-3 (91,(148)(149)(150)(151) and probably to other inhibitory receptors and thus cause immune escape (91,152,153).…”

Section: Ebov-gp Protects Hek-293 Cells From Lysis By Polyclonal Nk Cmentioning

confidence: 99%

“…Recently it was found that TIM-1 (T-cell-immunoglobin and mucine-domain 1) is a filovirus-receptor (88) and interacts by its PtdSer binding pocket directly with phosphatidylserine (PtdSer) located on the viral capsid (89)(90)(91). Furthermore, TIM-1 binds the adhesion receptor P-selectin and mediates T cell trafficking during inflammation and autoimmunity (92,93). TIM-1 can regulate and enhance type 1 immune response against tumors (94).…”

Section: Introductionmentioning

confidence: 99%

Activating NK- receptors, homing selectins and inhibitory Siglecs recognize EBOLA-GP and HPV-L1NK

Jarahian

Marstaller

Wurmbäck

et al. 2020

Preprint

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The Ebola virus glycoprotein (EBOV)-GP is extensively glycosylated. Its expression induces a physical alteration of surface adhesion molecules, which causes cell rounding and detachment of the infected cells. This phenomenon likely plays a crucial role in viral pathogenicity. In this study, we show that such morphological changes are cell line-dependent as well as dependent on the surface proteins that interact with EBOV-GP in cis and trans. We have generated data showing that natural killer (NK) cell receptors (NCRs: NKp44 and NKp46), selectins (CD62E/P/L) and inhibitory Siglecs function as receptors for Ebola-GP and human papilloma virus (HPV-L1). We used HEK293 cells transfected with Ebola-GP and recombinant fusion proteins containing the extracellular domain of each of these receptors linked to the Fc of human IgG1, which showed significant differences in their virus-binding behavior compared to HEK293 cells transfected with empty vector. Further, to demonstrate that EBOV-GP is a ligand for NKp44 and other NK-receptors, and to investigate their role in immune escape, we also used human HEK-293, HeLa- and hamster CHO-GP-transfectants. Our data show that the NK receptors NKp44 and NKp46 play a key role in recognizing EBOV (Ebolavirus) and strongly suggest that other inhibitory (Siglec-7, Siglec-5) and non-inhibitory homing receptors (P-Selectin, L-Selectin, E-Selectin, and DC-SIGNR/DC-SIGN) take part in the interaction with virus particles. In addition, we show that NKp44, and NKp46, Siglec-7, and -5, and P-, L-, E-selectins as well as of and DC-SIGNR/DC-SIGN bind to the artificial viral envelope of a lentiviral vector that contains EBOV-GP. Altogether we prove that NCRs and a range of other inhibitory and activating receptors can interact with viral envelope/capsid proteins and that such interaction could play an important role in the elimination of virus infected cells. Our findings could be used to develop new strategies for prevention and treatment of infections by these viruses.Author summaryThe innate immune system is able to recognize specifically certain virus components. Here we show that activating NK-cell receptors (NKp44, and NKp46) are involved in such interaction by using HEK293 and CHOK1 cells transfected with the Ebola virus glycoprotein (EBOV-GP) and by binding studies with purified EBOV-GP. In detail, we have found moderate to strong affinity of Siglecs (Siglec-7, and -5), selectins (P-, L-, E-Selectin) and DC-SIGNR/DC-SIGN to purified EBOV-GP, and to cells transfected with EBOV-GP as well as to the envelope of a lentiviral vector carrying the EBOV-GP. Our findings show that NKp44, and NKp46, Siglec-7, and -5, as well as P-and L-selectins have a strong affinity to EBOV-G.

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Regulation of T cell trafficking by the T cell immunoglobulin and mucin domain 1 glycoprotein

Cited by 26 publications

References 132 publications

Expression of Tim‐1 in primary CNS lymphoma

Expression of Tim‐1 in primary CNS lymphoma

Mutated Human P-Selectin Glycoprotein Ligand-1 and Viral Protein-1 of Enterovirus 71 Interactions on Au Nanoplasmonic Substrate for Specific Recognition by Surface-Enhanced Raman Spectroscopy

Activating NK- receptors, homing selectins and inhibitory Siglecs recognize EBOLA-GP and HPV-L1NK

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