HIV-1 Transcription and Virus Production Are Both Accentuated by the Proinflammatory Myeloid-Related Proteins in Human CD4+ T Lymphocytes

Ryckman, Carle; Robichaud, Gilles A.; Roy, J. L. A. M. Van; Cantin, Réjean; Tremblay, Michel J.; Tessier, Philippe A.

doi:10.4049/jimmunol.169.6.3307

Cited by 47 publications

(43 citation statements)

References 63 publications

(45 reference statements)

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“…Blockade of IL-10 signaling increased virus-specific CD8 ϩ and CD4 ϩ T cells and enhanced their function, resulting in resolution (72,73). Since S100A8 levels may be maintained in conditions where IL-10 is raised and human S100A8 accentuates HIV-1 transcription and virus production (23,24), this amplification may reflect clinical manifestations in patients with HIV-1.…”

Section: Discussionmentioning

confidence: 99%

“…ϩ T lymphocytes latently infected with HIV-1 and S100A8-induced HIV-1 transcriptional activity via an NF-B-dependent pathway (24). It was proposed that these S100 proteins may particularly contribute to HIV-1 progression in seropositive patients with opportunistic infections and/or inflammatory conditions because such conditions would likely have elevated systemic levels.…”

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confidence: 99%

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IL-10-Dependent S100A8 Gene Induction in Monocytes/Macrophages by Double-Stranded RNA

Endoh¹,

Chung²,

Clark

et al. 2009

The Journal of Immunology

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The S100 calcium-binding proteins S100A8 and S100A9 are elevated systemically in patients with viral infections. The S100A8-S100A9 complex facilitated viral replication in human CD4+ T lymphocytes latently infected with HIV-1- and S100A8-induced HIV-1 transcriptional activity. Mechanisms inducing the S100 genes and the potential source of these proteins following viral activation are unknown. In this study, we show that S100A8 was induced in murine macrophages, and S100A8 and S100A9 in human monocytes and macrophages, by polyinosinic:polycytidylic acid, a dsRNA mimetic. Induction was at the transcriptional level and was IL-10 dependent. Similar to LPS-induced S100A8, induction by dsRNA was dependent on p38 and ERK MAPK. Protein kinase R (PKR) mediates antiviral defense and participates in MyD88-dependent/independent signaling triggered by TLR4 or TLR3. Like IL-10, S100 induction by polyinosinic:polycytidylic acid and by LPS was inhibited by the specific PKR inhibitor 2-aminopurine, indicating a novel IL-10, PKR-dependent pathway. Other mediators such as IFN-β, which synergized with dsRNA, may also be involved. C/EBPβ bound the defined promoter region in response to dsRNA. S100A8 was expressed in lungs of mice infected with influenza virus and was maximal at day 8 with strong immunoreactivity in epithelial cells lining the airways and in mononuclear cells and declined early in the recovery phase, implying down-regulation by mediator(s) up-regulated during resolution of the infection. IL-10 is implicated in viral persistence. Since S100A8/S100A9 levels are likely to be maintained in conditions where IL-10 is raised, these proteins may contribute to viral persistence in patients infected by some RNA viruses.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

IL-10-Dependent S100A8 Gene Induction in Monocytes/Macrophages by Double-Stranded RNA

Endoh¹,

Chung²,

Clark

et al. 2009

The Journal of Immunology

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“…Recombinant proteins were produced as previously described (21,39). Contamination by endotoxins was Ͻ1 pg/g recombinant proteins as assessed using the Limulus amebocyte assay.…”

Section: Methodsmentioning

confidence: 99%

Blockade of S100A8 and S100A9 Suppresses Neutrophil Migration in Response to Lipopolysaccharide

Vandal

Rouleau

Boivin

et al. 2003

The Journal of Immunology

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201

169

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Recently, proinflammatory activities had been described for S100A8 and S100A9, two proteins found at inflammatory sites and within the neutrophil cytoplasm. In this study, we investigated the role of these proteins in neutrophil migration in vivo in response to LPS. LPS was injected into the murine air pouch, which led to the release of S100A8, S100A9, and S100A8/A9 in the pouch exudates that preceded accumulation of neutrophils. Passive immunization against S100A8 and S100A9 led to a 52% inhibition of neutrophil migration in response to LPS at 3 h postinjection. Injection of LPS was also associated with an increase in peripheral blood neutrophils and the presence in serum of S100A9 and S100A8/A9. Intravenous injection of S100A8, S100A9, or S100A8/A9 augmented the number of circulating neutrophils and diminished the number of neutrophils in the bone marrow, demonstrating that S100A8 and S100A9 induced the mobilization of neutrophils from the bone marrow to the blood. Finally, passive immunization with anti-S100A9 inhibited the neutrophilia associated with LPS injection in the air pouch. These results suggest that S100A8 and S100A9 play a role in the inflammatory response to LPS by inducing the release of neutrophils from the bone marrow and directing their migration to the inflammatory site.

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“…The cDNA was then cloned into the pET28 expression vector (Novagen, Madison, WI) and transformed in Escherichia coli HMS174. Recombinant protein was expressed and purified as previously described (38). Contamination by endotoxins was Ͻ1 pg/g of S100A8 or S100A9 protein, as measured by the Limulus amebocyte assay (Sigma, St. Louis, MO).…”

Section: Methodsmentioning

confidence: 99%

Role of S100A8 and S100A9 in neutrophil recruitment in response to monosodium urate monohydrate crystals in the air‐pouch model of acute gouty arthritis

Ryckman¹,

McColl²,

Vandal³

et al. 2003

Arthritis & Rheumatism

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168

150

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Objective. To examine the role of chemokines, S100A8, and S100A9 in neutrophil accumulation induced by the causative agent of gout, monosodium urate monohydrate (MSU) crystals.Methods. MSU crystal-induced neutrophil migration was studied in the murine air-pouch model. Release of chemokines, S100A8, S100A9, and S100A8/A9 in response to MSU crystals was quantified by enzymelinked immunosorbent assays. Recruited cells were counted following acetic blue staining, and the subpopulations were characterized by Wright-Giemsa staining of cytospins.Results. MSU crystals induced the accumulation of neutrophils following injection in the air pouch, which correlated with the release of the chemokines CXCL1, CXCL2, CCL2, and CCL3. However, none of these was found to play an important role in neutrophil migration induced by MSU crystals by passive immunization with antibodies directed against each chemokine. S100A8, S100A9, and S100A8/A9 were also found at high levels in the pouch exudates following injection of MSU crystals. In addition, injection of S100A8, S100A9, or S100A8/A9 led to the accumulation of neutrophils in the murine air pouch, demonstrating their proinflammatory activities in vivo. Passive immunization with anti-S100A8 and anti-S100A9 led to a total inhibition of the accumulation of neutrophils. Finally, S100A8/A9 was found at high concentrations in the synovial fluid of patients with gout.Conclusion. S100A8 and S100A8/A9 are essential to neutrophil migration induced by MSU crystals. These results suggest that they might be involved in the pathogenesis of gout.

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HIV-1 Transcription and Virus Production Are Both Accentuated by the Proinflammatory Myeloid-Related Proteins in Human CD4+ T Lymphocytes

Cited by 47 publications

References 63 publications

IL-10-Dependent S100A8 Gene Induction in Monocytes/Macrophages by Double-Stranded RNA

IL-10-Dependent S100A8 Gene Induction in Monocytes/Macrophages by Double-Stranded RNA

Blockade of S100A8 and S100A9 Suppresses Neutrophil Migration in Response to Lipopolysaccharide

Role of S100A8 and S100A9 in neutrophil recruitment in response to monosodium urate monohydrate crystals in the air‐pouch model of acute gouty arthritis

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