Database : MEDLINE
Search on : Arenaviridae and Infections [Words]
References found : 627 [refine]
Displaying: 1 .. 10   in format [Detailed]

page 1 of 63 go to page                         

  1 / 627 MEDLINE  
              next record last record
select
to print
Photocopy
Full text

[PMID]: 28449693
[Au] Autor:Mariën J; Borremans B; Gryseels S; Soropogui B; De Bruyn L; Bongo GN; Becker-Ziaja B; de Bellocq JG; Günther S; Magassouba N; Leirs H; Fichet-Calvet E
[Ad] Address:Evolutionary Ecology Group, University of Antwerp, Antwerp, Belgium. Joachim.marien@uantwerpen.be.
[Ti] Title:No measurable adverse effects of Lassa, Morogoro and Gairo arenaviruses on their rodent reservoir host in natural conditions.
[So] Source:Parasit Vectors;10(1):210, 2017 Apr 27.
[Is] ISSN:1756-3305
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:BACKGROUND: In order to optimize net transmission success, parasites are hypothesized to evolve towards causing minimal damage to their reservoir host while obtaining high shedding rates. For many parasite species however this paradigm has not been tested, and conflicting results have been found regarding the effect of arenaviruses on their rodent host species. The rodent Mastomys natalensis is the natural reservoir host of several arenaviruses, including Lassa virus that is known to cause Lassa haemorrhagic fever in humans. Here, we examined the effect of three arenaviruses (Gairo, Morogoro and Lassa virus) on four parameters of wild-caught Mastomys natalensis: body mass, head-body length, sexual maturity and fertility. After correcting for the effect of age, we compared these parameters between arenavirus-positive (arenavirus RNA or antibody) and negative animals using data from different field studies in Guinea (Lassa virus) and Tanzania (Morogoro and Gairo viruses). RESULTS: Although the sample sizes of our studies (1297, 749 and 259 animals respectively) were large enough to statistically detect small differences in body conditions, we did not observe any adverse effects of these viruses on Mastomys natalensis. We did find that sexual maturity was significantly positively related with Lassa virus antibody presence until a certain age, and with Gairo virus antibody presence in general. Gairo virus antibody-positive animals were also significantly heavier and larger than antibody-free animals. CONCLUSION: Together, these results suggest that the pathogenicity of arenaviruses is not severe in M. natalensis, which is likely to be an adaptation of these viruses to optimize transmission success. They also suggest that sexual behaviour might increase the probability of M. natalensis to become infected with arenaviruses.
[Mh] MeSH terms primary: Arenaviridae Infections/veterinary
Arenavirus/isolation & purification
Carrier State/veterinary
Disease Vectors
Murinae/physiology
Murinae/virology
[Mh] MeSH terms secundary: Animals
Arenaviridae Infections/pathology
Arenaviridae Infections/virology
Carrier State/pathology
Carrier State/virology
Guinea
Tanzania
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180109
[Lr] Last revision date:180109
[Js] Journal subset:IM
[Da] Date of entry for processing:170429
[St] Status:MEDLINE
[do] DOI:10.1186/s13071-017-2146-0

  2 / 627 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28827827
[Au] Autor:Shin HM; Kapoor VN; Kim G; Li P; Kim HR; Suresh M; Kaech SM; Wherry EJ; Selin LK; Leonard WJ; Welsh RM; Berg LJ
[Ad] Address:Dept of Pathology, University of Massachusetts Medical School, Worcester, Massachusetts, United States of America.
[Ti] Title:Transient expression of ZBTB32 in anti-viral CD8+ T cells limits the magnitude of the effector response and the generation of memory.
[So] Source:PLoS Pathog;13(8):e1006544, 2017 Aug.
[Is] ISSN:1553-7374
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Virus infections induce CD8+ T cell responses comprised of a large population of terminal effector cells and a smaller subset of long-lived memory cells. The transcription factors regulating the relative expansion versus the long-term survival potential of anti-viral CD8+ T cells are not completely understood. We identified ZBTB32 as a transcription factor that is transiently expressed in effector CD8+ T cells. After acute virus infection, CD8+ T cells deficient in ZBTB32 showed enhanced virus-specific CD8+ T cell responses, and generated increased numbers of virus-specific memory cells; in contrast, persistent expression of ZBTB32 suppressed memory cell formation. The dysregulation of CD8+ T cell responses in the absence of ZBTB32 was catastrophic, as Zbtb32-/- mice succumbed to a systemic viral infection and showed evidence of severe lung pathology. We found that ZBTB32 and Blimp-1 were co-expressed following CD8+ T cell activation, bound to each other, and cooperatively regulated Blimp-1 target genes Eomes and Cd27. These findings demonstrate that ZBTB32 is a key transcription factor in CD8+ effector T cells that is required for the balanced regulation of effector versus memory responses to infection.
[Mh] MeSH terms primary: Arenaviridae Infections/immunology
CD8-Positive T-Lymphocytes/immunology
Immunologic Memory/immunology
Repressor Proteins/immunology
[Mh] MeSH terms secundary: Adoptive Transfer
Animals
Chromatin Immunoprecipitation
Disease Models, Animal
Flow Cytometry
Lymphocyte Activation/immunology
Lymphocytic choriomeningitis virus/immunology
Male
Mice
Mice, Inbred C57BL
Mice, Knockout
Microscopy, Confocal
Polymerase Chain Reaction
Repressor Proteins/biosynthesis
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Repressor Proteins); 0 (Rog protein, mouse)
[Em] Entry month:1710
[Cu] Class update date: 171102
[Lr] Last revision date:171102
[Js] Journal subset:IM
[Da] Date of entry for processing:170823
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006544

  3 / 627 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28777079
[Au] Autor:Yekwa E; Khourieh J; Canard B; Papageorgiou N; Ferron F
[Ad] Address:CNRS, AFMB UMR 7257, 13288 Marseille, France.
[Ti] Title:Activity inhibition and crystal polymorphism induced by active-site metal swapping.
[So] Source:Acta Crystallogr D Struct Biol;73(Pt 8):641-649, 2017 Aug 01.
[Is] ISSN:2059-7983
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The Arenaviridae family is one of the two RNA viral families that encode a 3'-5' exonuclease in their genome. An exonuclease domain is found in the Arenaviridae nucleoprotein and targets dsRNA specifically. This domain is directly involved in suppression of innate immunity in the host cell. Like most phosphate-processing enzymes, it requires a divalent metal ion such as Mg (or Mn ) as a cofactor to catalyse nucleotide-cleavage and nucleotide-transfer reactions. On the other hand, calcium (Ca ) inhibits this enzymatic activity, in spite of the fact that Mg and Ca present comparable binding affinities and biological availabilities. Here, the molecular and structural effects of the replacement of magnesium by calcium and its inhibition mechanism for phosphodiester cleavage, an essential reaction in the viral process of innate immunity suppression, are studied. Biochemical data and high-resolution structures of the Mopeia virus exonuclease domain complexed with each ion are reported for the first time. The consequences of the ion swap for the stability of the protein, the catalytic site and the functional role of a specific metal ion in enabling the catalytic cleavage of a dsRNA substrate are outlined.
[Mh] MeSH terms primary: Arenavirus/chemistry
Arenavirus/enzymology
Exonucleases/chemistry
Nucleocapsid Proteins/chemistry
Nucleoproteins/chemistry
[Mh] MeSH terms secundary: Arenaviridae Infections/virology
Arenavirus/metabolism
Binding Sites
Calcium/metabolism
Catalytic Domain
Cations, Divalent/metabolism
Crystallization
Crystallography, X-Ray
Exonucleases/metabolism
Magnesium/metabolism
Manganese/metabolism
Molecular Docking Simulation
Nucleocapsid Proteins/metabolism
Nucleoproteins/metabolism
Protein Domains
RNA, Viral/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Cations, Divalent); 0 (Nucleocapsid Proteins); 0 (Nucleoproteins); 0 (RNA, Viral); 42Z2K6ZL8P (Manganese); EC 3.1.- (Exonucleases); I38ZP9992A (Magnesium); SY7Q814VUP (Calcium)
[Em] Entry month:1709
[Cu] Class update date: 170926
[Lr] Last revision date:170926
[Js] Journal subset:IM
[Da] Date of entry for processing:170805
[St] Status:MEDLINE
[do] DOI:10.1107/S205979831700866X

  4 / 627 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28714979
[Au] Autor:Araki K; Morita M; Bederman AG; Konieczny BT; Kissick HT; Sonenberg N; Ahmed R
[Ad] Address:Emory Vaccine Center and Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia, USA.
[Ti] Title:Translation is actively regulated during the differentiation of CD8 effector T cells.
[So] Source:Nat Immunol;18(9):1046-1057, 2017 Sep.
[Is] ISSN:1529-2916
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Translation is a critical process in protein synthesis, but translational regulation in antigen-specific T cells in vivo has not been well defined. Here we have characterized the translatome of virus-specific CD8 effector T cells (T cells) during acute infection of mice with lymphocytic choriomeningitis virus (LCMV). Antigen-specific T cells exerted dynamic translational control of gene expression that correlated with cell proliferation and stimulation via the T cell antigen receptor (TCR). The translation of mRNAs that encode translation machinery, including ribosomal proteins, was upregulated during the T cell clonal-expansion phase, followed by inhibition of the translation of those transcripts when the CD8 T cells stopped dividing just before the contraction phase. That translational suppression was more pronounced in terminal effector cells than in memory precursor cells and was regulated by antigenic stimulation and signals from the kinase mTOR. Our studies show that translation of transcripts encoding ribosomal proteins is regulated during the differentiation of CD8 T cells and might have a role in fate 'decisions' involved in the formation of memory cells.
[Mh] MeSH terms primary: Arenaviridae Infections/immunology
CD8-Positive T-Lymphocytes/immunology
Cell Differentiation/immunology
Protein Biosynthesis/immunology
[Mh] MeSH terms secundary: Animals
Arenaviridae Infections/genetics
Arenaviridae Infections/metabolism
CD8-Positive T-Lymphocytes/metabolism
Cell Differentiation/genetics
Flow Cytometry
Gene Expression Regulation
Immunologic Memory/immunology
Interferon-gamma/immunology
Lymphocytic choriomeningitis virus
Mice
Protein Biosynthesis/genetics
RNA, Messenger/metabolism
Receptors, Antigen, T-Cell/immunology
Reverse Transcriptase Polymerase Chain Reaction
Ribosomal Proteins/genetics
Ribosomal Proteins/metabolism
TOR Serine-Threonine Kinases/immunology
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (RNA, Messenger); 0 (Receptors, Antigen, T-Cell); 0 (Ribosomal Proteins); 82115-62-6 (Interferon-gamma); EC 2.7.1.1 (TOR Serine-Threonine Kinases)
[Em] Entry month:1709
[Cu] Class update date: 170911
[Lr] Last revision date:170911
[Js] Journal subset:IM
[Da] Date of entry for processing:170718
[St] Status:MEDLINE
[do] DOI:10.1038/ni.3795

  5 / 627 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28645238
[Au] Autor:Sarute N; Ross SR
[Ad] Address:Department of Microbiology and Immunology, University of Illinois College of Medicine at Chicago, Chicago, Illinois 60612; email: sarute@uic.edu , srross@uic.edu.
[Ti] Title:New World Arenavirus Biology.
[So] Source:Annu Rev Virol;4(1):141-158, 2017 Sep 29.
[Is] ISSN:2327-0578
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Hemorrhagic fevers caused by viruses were identified in the late 1950s in South America. These viruses have existed in their hosts, the New World rodents, for millions of years. Their emergence as infectious agents in humans coincided with changes in the environment and farming practices that caused explosions in their host rodent populations. Zoonosis into humans likely occurs because the pathogenic New World arenaviruses use human transferrin receptor 1 to enter cells. The mortality rate after infection with these viruses is high, but the mechanism by which disease is induced is still not clear. Possibilities include direct effects of cellular infection or the induction of high levels of cytokines by infected sentinel cells of the immune system, leading to endothelia and thrombocyte dysfunction and neurological disease. Here we provide a review of the ecology and molecular and cellular biology of New World arenaviruses, as well as a discussion of the current animal models of infection. The development of animal models, coupled with an improved understanding of the infection pathway and host response, should lead to the discovery of new drugs for treating infections.
[Mh] MeSH terms primary: Arenaviridae Infections/virology
Arenaviruses, New World/genetics
Arenaviruses, New World/pathogenicity
[Mh] MeSH terms secundary: Animals
Antigens, CD/metabolism
Arenaviridae Infections/complications
Arenaviridae Infections/immunology
Arenaviridae Infections/transmission
Arenaviruses, New World/immunology
Disease Models, Animal
Hemorrhagic Fevers, Viral/transmission
Hemorrhagic Fevers, Viral/virology
Host-Pathogen Interactions
Humans
Mice
Receptors, Transferrin/metabolism
Receptors, Virus/metabolism
Rodentia/virology
Zoonoses/virology
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (Antigens, CD); 0 (CD71 antigen); 0 (Receptors, Transferrin); 0 (Receptors, Virus)
[Em] Entry month:1710
[Cu] Class update date: 171027
[Lr] Last revision date:171027
[Js] Journal subset:IM
[Da] Date of entry for processing:170625
[St] Status:MEDLINE
[do] DOI:10.1146/annurev-virology-101416-042001

  6 / 627 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28530712
[Au] Autor:Moffett HF; Cartwright ANR; Kim HJ; Godec J; Pyrdol J; Äijö T; Martinez GJ; Rao A; Lu J; Golub TR; Cantor H; Sharpe AH; Novina CD; Wucherpfennig KW
[Ad] Address:Department of Cancer Immunology &Virology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA.
[Ti] Title:The microRNA miR-31 inhibits CD8 T cell function in chronic viral infection.
[So] Source:Nat Immunol;18(7):791-799, 2017 Jul.
[Is] ISSN:1529-2916
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:During infection, antigen-specific T cells undergo tightly regulated developmental transitions controlled by transcriptional and post-transcriptional regulation of gene expression. We found that the microRNA miR-31 was strongly induced by activation of the T cell antigen receptor (TCR) in a pathway involving calcium and activation of the transcription factor NFAT. During chronic infection with lymphocytic choriomeningitis virus (LCMV) clone 13, miR-31-deficent mice recovered from clinical disease, while wild-type mice continued to show signs of disease. This disease phenotype was explained by the presence of larger numbers of cytokine-secreting LCMV-specific CD8 T cells in miR-31-deficent mice than in wild-type mice. Mechanistically, miR-31 increased the sensitivity of T cells to type I interferons, which interfered with effector T cell function and increased the expression of several proteins related to T cell dysfunction during chronic infection. These studies identify miR-31 as an important regulator of T cell exhaustion in chronic infection.
[Mh] MeSH terms primary: Arenaviridae Infections/immunology
CD8-Positive T-Lymphocytes/immunology
Cytokines/immunology
MicroRNAs/immunology
Receptors, Antigen, T-Cell/immunology
[Mh] MeSH terms secundary: Animals
Antibodies, Viral/immunology
Arenaviridae Infections/genetics
CD8-Positive T-Lymphocytes/drug effects
Calcium/metabolism
Chromatin Immunoprecipitation
Dendritic Cells/immunology
Enzyme-Linked Immunosorbent Assay
Flow Cytometry
Gene Expression Profiling
Immunoblotting
Interferon Type I/pharmacology
Lymphocytic choriomeningitis virus/immunology
Mice
Mice, Knockout
MicroRNAs/genetics
NFATC Transcription Factors/metabolism
Real-Time Polymerase Chain Reaction
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Antibodies, Viral); 0 (Cytokines); 0 (Interferon Type I); 0 (MicroRNAs); 0 (Mirn31 microRNA, mouse); 0 (NFATC Transcription Factors); 0 (Nfatc2 protein, mouse); 0 (Receptors, Antigen, T-Cell); SY7Q814VUP (Calcium)
[Em] Entry month:1708
[Cu] Class update date: 170828
[Lr] Last revision date:170828
[Js] Journal subset:IM
[Da] Date of entry for processing:170523
[St] Status:MEDLINE
[do] DOI:10.1038/ni.3755

  7 / 627 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28515291
[Au] Autor:Stenglein MD; Sanchez-Migallon Guzman D; Garcia VE; Layton ML; Hoon-Hanks LL; Boback SM; Keel MK; Drazenovich T; Hawkins MG; DeRisi JL
[Ad] Address:Department of Microbiology, Immunology, and Pathology, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, Colorado, USA.
[Ti] Title:Differential Disease Susceptibilities in Experimentally Reptarenavirus-Infected Boa Constrictors and Ball Pythons.
[So] Source:J Virol;91(15), 2017 Aug 01.
[Is] ISSN:1098-5514
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Inclusion body disease (IBD) is an infectious disease originally described in captive snakes. It has traditionally been diagnosed by the presence of large eosinophilic cytoplasmic inclusions and is associated with neurological, gastrointestinal, and lymphoproliferative disorders. Previously, we identified and established a culture system for a novel lineage of arenaviruses isolated from boa constrictors diagnosed with IBD. Although ample circumstantial evidence suggested that these viruses, now known as reptarenaviruses, cause IBD, there has been no formal demonstration of disease causality since their discovery. We therefore conducted a long-term challenge experiment to test the hypothesis that reptarenaviruses cause IBD. We infected boa constrictors and ball pythons by cardiac injection of purified virus. We monitored the progression of viral growth in tissues, blood, and environmental samples. Infection produced dramatically different disease outcomes in snakes of the two species. Ball pythons infected with Golden Gate virus (GoGV) and with another reptarenavirus displayed severe neurological signs within 2 months, and viral replication was detected only in central nervous system tissues. In contrast, GoGV-infected boa constrictors remained free of clinical signs for 2 years, despite high viral loads and the accumulation of large intracellular inclusions in multiple tissues, including the brain. Inflammation was associated with infection in ball pythons but not in boa constrictors. Thus, reptarenavirus infection produces inclusions and inclusion body disease, although inclusions are neither necessarily associated with nor required for disease. Although the natural distribution of reptarenaviruses has yet to be described, the different outcomes of infection may reflect differences in geographical origin. New DNA sequencing technologies have made it easier than ever to identify the sequences of microorganisms in diseased tissues, i.e., to identify organisms that appear to cause disease, but to be certain that a candidate pathogen actually causes disease, it is necessary to provide additional evidence of causality. We have done this to demonstrate that reptarenaviruses cause inclusion body disease (IBD), a serious transmissible disease of snakes. We infected boa constrictors and ball pythons with purified reptarenavirus. Ball pythons fell ill within 2 months of infection and displayed signs of neurological disease typical of IBD. In contrast, boa constrictors remained healthy over 2 years, despite high levels of virus throughout their bodies. This difference matches previous reports that pythons are more susceptible to IBD than boas and could reflect the possibility that boas are natural hosts of these viruses in the wild.
[Mh] MeSH terms primary: Arenaviridae Infections/veterinary
Arenaviridae/growth & development
Arenaviridae/immunology
Boidae/virology
Disease Susceptibility
[Mh] MeSH terms secundary: Animal Structures/pathology
Animal Structures/virology
Animals
Arenaviridae Infections/immunology
Arenaviridae Infections/pathology
Inflammation/pathology
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1707
[Cu] Class update date: 171025
[Lr] Last revision date:171025
[Js] Journal subset:IM
[Da] Date of entry for processing:170519
[St] Status:MEDLINE

  8 / 627 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28505175
[Au] Autor:Rosenthal M; Gogrefe N; Vogel D; Reguera J; Rauschenberger B; Cusack S; Günther S; Reindl S
[Ad] Address:Department of Virology, Bernhard-Nocht-Institute for Tropical Medicine, Hamburg, Germany.
[Ti] Title:Structural insights into reptarenavirus cap-snatching machinery.
[So] Source:PLoS Pathog;13(5):e1006400, 2017 May.
[Is] ISSN:1553-7374
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Cap-snatching was first discovered in influenza virus. Structures of the involved domains of the influenza virus polymerase, namely the endonuclease in the PA subunit and the cap-binding domain in the PB2 subunit, have been solved. Cap-snatching endonucleases have also been demonstrated at the very N-terminus of the L proteins of mammarena-, orthobunya-, and hantaviruses. However, a cap-binding domain has not been identified in an arena- or bunyavirus L protein so far. We solved the structure of the 326 C-terminal residues of the L protein of California Academy of Sciences virus (CASV), a reptarenavirus, by X-ray crystallography. The individual domains of this 37-kDa fragment (L-Cterm) as well as the domain arrangement are structurally similar to the cap-binding and adjacent domains of influenza virus polymerase PB2 subunit, despite the absence of sequence homology, suggesting a common evolutionary origin. This enabled identification of a region in CASV L-Cterm with similarity to a cap-binding site; however, the typical sandwich of two aromatic residues was missing. Consistent with this, cap-binding to CASV L-Cterm could not be detected biochemically. In addition, we solved the crystal structure of the corresponding endonuclease in the N-terminus of CASV L protein. It shows a typical endonuclease fold with an active site configuration that is essentially identical to that of known mammarenavirus endonuclease structures. In conclusion, we provide evidence for a presumably functional cap-snatching endonuclease in the N-terminus and a degenerate cap-binding domain in the C-terminus of a reptarenavirus L protein. Implications of these findings for the cap-snatching mechanism in arenaviruses are discussed.
[Mh] MeSH terms primary: Arenaviridae Infections/virology
Arenaviridae/enzymology
Endonucleases/metabolism
Models, Molecular
[Mh] MeSH terms secundary: Arenaviridae/chemistry
Arenaviridae/genetics
Crystallography, X-Ray
Endonucleases/chemistry
Endonucleases/genetics
Protein Conformation
Protein Domains
RNA Caps
Viral Proteins/chemistry
Viral Proteins/genetics
Viral Proteins/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (RNA Caps); 0 (Viral Proteins); EC 3.1.- (Endonucleases)
[Em] Entry month:1709
[Cu] Class update date: 170911
[Lr] Last revision date:170911
[Js] Journal subset:IM
[Da] Date of entry for processing:170516
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006400

  9 / 627 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28419428
[Au] Autor:Mancuso ME; Santagostino E
[Ad] Address:Angelo Bianchi Bonomi Haemophilia and Thrombosis Centre, Fondazione IRCCS Ca' Granda, Ospedale Maggiore Policlinico, Milan, Italy.
[Ti] Title:Platelets: much more than bricks in a breached wall.
[So] Source:Br J Haematol;178(2):209-219, 2017 Jul.
[Is] ISSN:1365-2141
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Platelets have various roles in vascular biology and homeostasis. They are the first actor in primary haemostasis and play important roles in thrombosis pathogenesis, but they are also part of innate immunity, which initiates and accelerate many inflammatory conditions. In some contexts, their immune functions are protective, while in others they contribute to adverse inflammatory outcomes. Platelets express numerous receptors and contain hundreds of secretory molecules that are crucial for platelet functional responses. The capacity of platelets to produce and secrete cytokines, chemokines and related molecules, under the control of specific intracellular pathways, is intimately related to their key role in inflammation. They are also able to intervene in tissue regeneration and repair because they produce pro-angiogenic mediators. Due to this characteristic platelets are involved in cancer progression and spreading. In this review we discuss the complex role of platelets, which bridges haemostasis, inflammation and immune response both in physiological and pathological conditions.
[Mh] MeSH terms primary: Blood Platelets/physiology
[Mh] MeSH terms secundary: Alzheimer Disease/blood
Alzheimer Disease/physiopathology
Arenaviridae Infections/blood
Arenaviridae Infections/physiopathology
Atherosclerosis/blood
Atherosclerosis/physiopathology
Bacterial Infections/blood
Bacterial Infections/physiopathology
Chemokines/physiology
Dengue/blood
Dengue/physiopathology
HIV Infections/blood
HIV Infections/physiopathology
HIV-1
Hemostasis/physiology
Humans
Immunity, Innate/physiology
Inflammation/blood
Inflammation/physiopathology
Malaria/blood
Malaria/physiopathology
Multiple Sclerosis/blood
Multiple Sclerosis/physiopathology
Neoplasms/blood
Neoplasms/physiopathology
Neovascularization, Pathologic/blood
Neovascularization, Pathologic/physiopathology
Platelet Activation/physiology
Receptors, Cell Surface/physiology
Stroke/blood
Stroke/physiopathology
Thrombosis/blood
Thrombosis/etiology
Thrombosis/physiopathology
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (Chemokines); 0 (Receptors, Cell Surface)
[Em] Entry month:1709
[Cu] Class update date: 170906
[Lr] Last revision date:170906
[Js] Journal subset:IM
[Da] Date of entry for processing:170419
[St] Status:MEDLINE
[do] DOI:10.1111/bjh.14653

  10 / 627 MEDLINE  
              first record previous record
select
to print
Photocopy
Full text

[PMID]: 28378389
[Au] Autor:Kavazovic I; Lenartic M; Jelencic V; Jurkovic S; Lemmermann NAW; Jonjic S; Polic B; Wensveen FM
[Ad] Address:Department of Histology and Embryology, Faculty of Medicine, University of Rijeka, Rijeka, Croatia.
[Ti] Title:NKG2D stimulation of CD8 T cells during priming promotes their capacity to produce cytokines in response to viral infection in mice.
[So] Source:Eur J Immunol;47(7):1123-1135, 2017 Jul.
[Is] ISSN:1521-4141
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:Natural killer group 2 member D (NKG2D) is an activating receptor that is expressed on most cytotoxic cells of the immune system, including NK cells, γδ, and CD8 T cells. It is still a matter of debate whether and how NKG2D mediates priming of CD8 T cells in vivo, due to a lack of studies where NKG2D is eliminated exclusively in these cells. Here, we studied the impact of NKG2D on effector CD8 T-cell formation. NKG2D deficiency that is restricted to murine CD8 T cells did not impair antigen-specific T-cell expansion following mouse CMV and lymphocytic choriomeningitis virus infection, but reduced their capacity to produce cytokines. Upon infection, conventional dendritic cells induce NKG2D ligands, which drive cytokine production on CD8 T cells via the Dap10 signaling pathway. T-cell development, homing, and proliferation were not affected by NKG2D deficiency and cytotoxicity was only impaired when strong T-cell receptor (TCR) stimuli were used. Transfer of antigen-specific CD8 T cells demonstrated that NKG2D deficiency attenuated their capacity to reduce viral loads. The inability of NKG2D-deficient cells to produce cytokines could be overcome with injection of IL-15 superagonist during priming. In summary, our data show that NKG2D has a nonredundant role in priming of CD8 T cells to produce antiviral cytokines.
[Mh] MeSH terms primary: Arenaviridae Infections/immunology
CD8-Positive T-Lymphocytes/immunology
Cytokines/immunology
Herpesviridae Infections/immunology
NK Cell Lectin-Like Receptor Subfamily K/metabolism
[Mh] MeSH terms secundary: Animals
Cytokines/biosynthesis
Cytotoxicity, Immunologic
Dendritic Cells/immunology
Killer Cells, Natural/immunology
Lymphocyte Activation
Lymphocytic choriomeningitis virus/immunology
Mice
Muromegalovirus
NK Cell Lectin-Like Receptor Subfamily K/deficiency
NK Cell Lectin-Like Receptor Subfamily K/genetics
Receptors, Immunologic/immunology
Receptors, Immunologic/metabolism
Signal Transduction
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Cytokines); 0 (Hcst protein, mouse); 0 (Klrk1 protein, mouse); 0 (NK Cell Lectin-Like Receptor Subfamily K); 0 (Receptors, Immunologic)
[Em] Entry month:1709
[Cu] Class update date: 170927
[Lr] Last revision date:170927
[Js] Journal subset:IM
[Da] Date of entry for processing:170406
[St] Status:MEDLINE
[do] DOI:10.1002/eji.201646805


page 1 of 63 go to page                         
   


Refine the search
  Database : MEDLINE Advanced form   

    Search in field  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/PAHO/WHO - Latin American and Caribbean Center on Health Sciences Information