Molecular cloning and functional characterization of the avian macrophage migration inhibitory factor (MIF)

Kim, Sung-Won; Miska, Katarzyna B.; Jenkins, Mark C.; Fetterer, Raymond H.; Cox, Catherine A.; Stuard, Lindsay H; Dalloul, Rami A.

doi:10.1016/j.dci.2010.05.005

Cited by 29 publications

(29 citation statements)

References 21 publications

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“…Our previous findings determined that avian MIF is expressed by various tissues and cell types including monocytes/macrophages (Kim et al, 2010a), historically considered as "targets" of MIF action (Bloom and Bennett, 1966). MIF is present in dimer and tetramer forms in macrophages -and in T cells -and it exerts important autocrine/paracrine activation effects upon its release (Bacher et al, 1996;Calandra et al, 1994;Kim et al, 2010a).…”

Section: Discussionmentioning

confidence: 99%

“…Fresh blood was collected from 7/8-week-old broilers and PBMCs were isolated using Histopaque-1077 (Sigma, MO) as described (Kim et al, 2010a). Cells from the transformed chicken macrophage cell line HTC (Rath et al, 2003) and the chicken fibroblast cell line DF-1 (Kim et al, 2001) were cultured and maintained with Dulbecco's Modified Eagle Medium (DMEM; Mediatech, VA) supplemented with 100 units/mL of penicillin, 100 μg/mL of streptomycin, and 10% (v/v) of fetal calf serum (FCS) (all supplied by Atlanta Biologicals, GA) at 39°C with 5% CO2 humidified air.…”

Section: Birds and Cellsmentioning

confidence: 99%

“…Although elevated MIF mRNA was observed during Eimeria infection (Hong et al, 2006a(Hong et al, , 2006b, there was no biological characterization until 2010. Using a chemotaxis assay and qRT-PCR, we showed that ChMIF inhibits random migration of chicken macrophages in a dose-dependent manner (Kim et al, 2010a). Unlike mammals, ChMIF alone had no significant effect on chicken innate and adaptive immune cells; however, it did enhance mRNA levels of pro-inflammatory cytokines including IL-1β, IL-8, iNOS and IFN-γ when chicken peripheral blood mononuclear cells (PBMCs) were primed by LPS (Kim et al, 2010a).…”

Section: Introductionmentioning

confidence: 98%

“…Using a chemotaxis assay and qRT-PCR, we showed that ChMIF inhibits random migration of chicken macrophages in a dose-dependent manner (Kim et al, 2010a). Unlike mammals, ChMIF alone had no significant effect on chicken innate and adaptive immune cells; however, it did enhance mRNA levels of pro-inflammatory cytokines including IL-1β, IL-8, iNOS and IFN-γ when chicken peripheral blood mononuclear cells (PBMCs) were primed by LPS (Kim et al, 2010a). Similar to innate immune cells, ChMIF alone does not induce proliferation of lymphocytes and expression of Th1/Th2 cytokines.…”

Section: Introductionmentioning

confidence: 98%

“…When lymphocytes were prestimulated with a mitogen (e.g. Con A), ChMIF enhanced expression of IFN-γ and IL-2, while reducing mRNA levels of IL-4 and IL-13 (Kim et al, 2010a).…”

Section: Introductionmentioning

confidence: 98%

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Both host and parasite MIF molecules bind to chicken macrophages via CD74 surface receptor

Kim

Cox

Jenkins

et al. 2014

Developmental & Comparative Immunology

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Section: Discussionmentioning

confidence: 99%

Section: Birds and Cellsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 98%

“…When lymphocytes were prestimulated with a mitogen (e.g. Con A), ChMIF enhanced expression of IFN-γ and IL-2, while reducing mRNA levels of IL-4 and IL-13 (Kim et al, 2010a).…”

Section: Introductionmentioning

confidence: 98%

See 3 more Smart Citations

Both host and parasite MIF molecules bind to chicken macrophages via CD74 surface receptor

Kim

Cox

Jenkins

et al. 2014

Developmental & Comparative Immunology

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Macrophage migration inhibitory factor (MIF) of the protozoan parasite Eimeria influences the components of the immune system of its host, the chicken

et al. 2013

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Macrophage migration inhibitory factor (MIF) is a soluble factor produced by sensitized T lymphocytes that inhibits the random migration of macrophages. Homologues of MIF from invertebrates have been identified, making it an interesting molecule from a functional perspective. In the present study, the localization of a parasite MIF protein as well as its effect on the host was characterized. Western blot analysis shows that Eimeria MIF (EMIF) is found during all parasite developmental stages tested. Transmission electron microscopy shows that MIF is distributed throughout cytosol and nucleus of Eimeria acervulina merozoites. Immunohistochemical analysis suggests that EMIF may be released into the surrounding tissues as early as 24 h after infection, while later during oocyst formation, MIF expression is localized to areas immediately surrounding the oocysts, as well as in wall-forming bodies. The chemotaxis assay revealed an inhibitory function of EMIF on chicken monocyte migration. Quantitative real-time PCR was performed to examine the effect of EMIF on host immune system by measuring the transcripts of inflammatory mediators. An ex vivo stimulation study showed that E. acervulina MIF (EaMIF) enhanced expression of pro-inflammatory cytokines and chemokines in the presence of lipopolysaccharide (LPS). Furthermore, sequential treatment of adherent peripheral blood mononuclear cells with EaMIF, chicken MIF, and LPS in 2-h intervals led to the highest levels of interleukin (IL)-1B, chemokine CCLi3, IL-18, and interferon-gamma mRNA expression. This study shows that parasite MIF is widely expressed and may have potential effects on the immune system of the host.

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Characterization and localization of an Eimeria-specific protein in Eimeria maxima

et al. 2013

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A recently completed analysis of Eimeria maxima transcriptome identified a gene with homology to sequences expressed by E. tenella and E. acervulina but lacking homology with other organisms including other apicomplexans. This gene, designated Eimeria-specific protein (ESP), codes for a protein with a predicted molecular weight of 19 kDa. The ESP gene was cloned and the recombinant protein expressed in bacteria and purified for preparation of specific antisera. Quantitative RT-PCR showed transcription of ESP was low in unsporulated oocysts and after 24 h of sporulation. However, transcription nearly doubled after 48 h of sporulation and reached its highest levels in sporozoites (SZ) and merozoites (MZ). The protein was detectable by Western blot in both sporulated oocysts and in SZ and MZ. Immuno-localization by light microscopy identified ESP in paired structures in the anterior of SZ and MZ. Immuno-localization by electron microscopy identified ESP in MZ rhoptries but no specific staining of any SZ structures was detected. In addition, localization studies on intestinal sections recovered from birds 120-h post-infection indicates that oocysts do not stain with anti-ESP but staining of microgametocytes and developing oocysts was observed. The results indicate that ESP is associated with the rhoptry of E. maxima and that the protein may have functions in other developmental stages.

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Molecular cloning and functional characterization of the avian macrophage migration inhibitory factor (MIF)

Cited by 29 publications

References 21 publications

Both host and parasite MIF molecules bind to chicken macrophages via CD74 surface receptor

Both host and parasite MIF molecules bind to chicken macrophages via CD74 surface receptor

Macrophage migration inhibitory factor (MIF) of the protozoan parasite Eimeria influences the components of the immune system of its host, the chicken

Characterization and localization of an Eimeria-specific protein in Eimeria maxima

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