Biological properties of recombinant chicken interferon‐γ

Weining, Kirsten C.; Schultz, Ursula; Münster, Uwe; Kaspers, Bernd; Staeheli, Peter

doi:10.1002/eji.1830261026

Cited by 108 publications

(76 citation statements)

References 38 publications

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“…RNA samples were size fractionated by electrophoresis through agarose gels containing 4% formaldehyde using standard procedures before blotting onto nylon membranes and hybridization with the indicated cDNA probes that were radiolabeled with 32 Purification of Histidine-tagged Recombinant Proteins from Escherichia coli-Purification of histidine-tagged chIFN-␥ and MxA by affinity chromatography on nickel chelate agarose was described previously (45,46).…”

Section: Methodsmentioning

confidence: 99%

An Interferon-γ-binding Protein of Novel Structure Encoded by the Fowlpox Virus

Puehler¹,

Schwarz²,

Waidner³

et al. 2003

Journal of Biological Chemistry

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Section: Methodsmentioning

confidence: 99%

An Interferon-γ-binding Protein of Novel Structure Encoded by the Fowlpox Virus

Puehler¹,

Schwarz²,

Waidner³

et al. 2003

Journal of Biological Chemistry

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“…COS-7 cells were grown in DMEM supplemented with 10% fetal calf serum. Primary macrophages were prepared from chicken blood and cultured as described [28].…”

Section: Methodsmentioning

confidence: 99%

“…His-ChIL-1β was purified by affinity chromatography on a nickel chelate agarose column. Purification conditions were exactly as described for chicken interferon-γ [28]. Peak column fractions were pooled and samples were frozen at Ϫ20°C.…”

Section: Methodsmentioning

confidence: 99%

A chicken homolog of mammalian interleukin‐1β : cDNA cloning and purification of active recombinant protein

Weining

Sick

Kaspers

et al. 1998

European Journal of Biochemistry

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140

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Upon induction with lipopolysaccharide (LPS) the chicken macrophage cell line HD-11 secretes an activity that stimulates the synthesis of a CXC chemokine in the chicken fibroblast cell line CEC-32. We used a cDNA expression cloning strategy in COS cells to characterize this activity. The isolated cDNA clone codes for a polypeptide of 267 amino acids which lacks a hydrophobic N-terminal domain that could serve as secretory signal. Sequence homology and structural features indicate that this protein is the chicken homolog of mammalian interleukin-1β (ChIL-1β). Northern blot analysis showed that ChIL-1β RNA is quickly induced in blood monocyte-derived macrophages reaching maximal levels within one hour after onset of LPS treatment. To test for biological activity of putative mature ChIL-1β, a cDNA fragment comprising amino acids 106 to 267 of the open reading frame was expressed in Escherichia coli so that the resulting polypeptide carried a histidine tag at its N-terminus for easy purification by nickel chelate affinity chromatography. Purified His-ChIL-1β potently induced CXC chemokine RNA synthesis in CEC-32 cells. When injected intravenously into adult chickens, it quickly induced a transient increase in serum corticosterone levels.Keywords : chicken; lipopolysaccharide inducibility ; interleukin-1β; CXC chemokine ; cDNA expression cloning.Interleukin-1 (IL-1) is an important pro-inflammatory cytokine that exhibits pleiotropic activities on a wide range of target cells [1]. It is secreted by many different cell types, with stimulated macrophages being the main producers of IL-1. The diverse biological effects of IL-1 include induction of fever, elevation of serum corticosterone levels, activation of the cytokine network, triggering of the acute-phase response in the liver and activation of vascular endothelium [2]. It further stimulates T-cell proliferation via interleukin-2 induction, and it induces B-cell maturation and antibody production. IL-1 also stimulates collagenase and prostaglandin production by fibroblasts and exerts stimulating effects on cells engaged in developmental, differentiation and repair processes [2]. Furthermore, IL-1 induces the synthesis of IL-8 and other CXC chemokines in human fibroblasts [3] and other cell types [4,5].In mammals the IL-1 gene family comprises three members: IL-1A, IL-1β and the IL-1 receptor antagonist (IL-1Ra) [6]. IL-1A and IL-1β are only distantly related to each other with 45% similarity at the nucleic acid level and 26% similarity at the amino acid level in humans [7]. Despite low sequence similarity, both molecules bind the same receptor [8,9] and induce nearly indistinguishable biological responses [10]. Furthermore, both molecules are similar with regard to their overall structures. Though secreted, both IL-1A and IL-1β lack a typical hydrophoCorrespondence to P. Staeheli,

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“…3). IFN-γ has been demonstrated to possess potent stimulatory effects on cell-mediated immunity in chickens [24]. Protection of newly hatched chickens against infection by invasive salmonellae has been associated with enhanced cell-mediated indices of immunity [6].…”

Section: Discussionmentioning

confidence: 99%

“…Since the gene coding a chicken IFN-γ (ChIFN-γ) was isolated and sequenced by Digby and Lowenthal [3], many reports have been published to produce recombinant ChIFN-γs [3,8,20,21,24]. Lowenthal et al [11] showed enhancement of antibody responses in chickens co-administered of ChIFN-γ with sheep red blood cells.…”

mentioning

confidence: 99%

Adjuvant Effect of Chicken Interferon-.GAMMA. for Inactivated Salmonella Enteritidis Antigen

Takehara

Kobayashi

Ruttanapumma

et al. 2003

The Journal of Veterinary Medical Science

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ABSTRACT. The adjuvant effect of chicken interferon-γ (ChIFN-γ) was examined for protecting chickens against intestinal colonization of Salmonella Enteritidis (SE) following oral exposure. Ten 7-week-old chickens per group were immunized with inactivated SE twice with or without co-administration of ChIFN-γ intramuscularly, and all chickens were challenged with SE. Sera collected from immunized groups with or without ChIFN-γ, and from unimmunized group were measured for SE antibody by agglutination test. The levels of antibodies were raised by 1 week post-immunization and did not show any difference between groups with and without ChIFN-γ. No antibodies were detected in unimmunized group before challenge. Fecal samples from each group were cultured at 1, 4, 7, and 13 days postchallenge to determine the incidence of intestinal colonization and the numbers of SE shed into the environment. Co-administration of ChIFN-γ, significantly reduced the incidence of intestinal colonization (P<0.05). At 13 days post-challenge, the bacterial counts of SE in organs were also reduced in ChIFN-γ administered group. These data suggest co-administration of ChIFN-γ with SE antigen enhances protection against SE challenge without acceleration of antibody production.

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Biological properties of recombinant chicken interferon‐γ

Cited by 108 publications

References 38 publications

An Interferon-γ-binding Protein of Novel Structure Encoded by the Fowlpox Virus

An Interferon-γ-binding Protein of Novel Structure Encoded by the Fowlpox Virus

A chicken homolog of mammalian interleukin‐1β : cDNA cloning and purification of active recombinant protein

Adjuvant Effect of Chicken Interferon-.GAMMA. for Inactivated Salmonella Enteritidis Antigen

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