Cloning and Biologic Activities of a Bovine Interferon-α Isolated from the Epithelium of a Rotavirus-Infected Calf

Chaplin, Paul; Entrican, Gary; Gelder, K.I.; Collins, Robert A.

doi:10.1089/jir.1996.16.25

Cited by 20 publications

(13 citation statements)

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“…The IFN genes (including pseudogenes) in cattle include 10-12 IFN-␣, 5-6 IFN-␤, 3-5 IFN-, and 15-20 IFN- (Capon et al, 1985;Chaplin et al, 1996;Velan et al, 1985). Despite the high degree of identity among IFN subtypes from the same species, the function and magnitude of their biological activities differ; for example, different antiviral activities between intact PoIFN-␣ and C-terminal-deleted PoIFN-␣ and unusual characteristics of murine IFN-␣13 (Cheng et al, 2006;Tsang et al, 2007;van Pesch and Michiels, 2003;Zhao et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

Characterization and antivirus activities of a novel bovine IFN-omega24

Luo

Guo

Bao

et al. 2015

Molecular Immunology

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Section: Discussionmentioning

confidence: 99%

Characterization and antivirus activities of a novel bovine IFN-omega24

Luo

Guo

Bao

et al. 2015

Molecular Immunology

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“…The role of IFN in rotavirus infection is unclear, as the data are conflicting and dependent on the species studied. Both humans and animals infected with rotavirus have serum IFN-␣ and excrete IFN-␣ in stool (11,14,27). Calves treated with recombinant human IFN-␣2 were protected from diarrhea induced by tissue culture-adapted bovine rotavirus (42), whereas piglets were not (28).…”

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confidence: 99%

Interferon Regulatory Factor 3 Is a Cellular Partner of Rotavirus NSP1

Graff

Mitzel

Weisend

et al. 2002

J Virol

101

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The rotavirus nonstructural protein NSP1 is the least conserved protein in the rotavirus genome, and its function in the replication cycle is not known. We employed NSP1 as bait in the yeast two-hybrid interaction trap to identify candidate cellular partners of NSP1 that may provide clues to its function. Interferon regulatory factor 3 (IRF-3) was identified as an NSP1 interactor. NSP1 synthesized in rotavirus-infected cells bound IRF-3 in a glutathione S-transferase pull-down assay, indicating that the interaction was not unique to the two-hybrid system. NSP1 of murine rotavirus strain EW also interacted with IRF-3. NSP1 deletion and point mutants were constructed to map domains important in the interaction between NSP1 and IRF-3. The data suggest that a binding domain resides in the C terminus of NSP1 and that the N-terminal conserved zinc finger is important but not sufficient to mediate binding to IRF-3. We predict that a role for NSP1 in rotavirus-infected cells is to inhibit activation of IRF-3 and diminish the cellular interferon response.Rotaviruses are the most important cause of severe, often life-threatening gastroenteritis in infants and children under 2 years of age (33). These viruses are ubiquitous in nature and are also responsible for a significant proportion of neonatal diarrheal illness in domestic animals, particularly in bovine and porcine species (18,40). Substantial research efforts have thus focused on understanding the correlates of a protective immune response to rotavirus infection and the molecular mechanisms of virus replication so that efficacious vaccines can be developed.The rotavirus segmented double-stranded RNA genome encodes six structural proteins (VP) and six nonstructural proteins (NSP) (reviewed in reference 17). The structural proteins VP1, VP2, VP3, VP4, VP6, and VP7 are well characterized in terms of their antigenic, structural, and biochemical properties. The functions of the rotavirus nonstructural proteins NSP1 to NSP6 are less well defined with regard to the roles that these proteins play in the rotavirus replication cycle. Intriguing functions have recently been described for some. NSP3 binds the 3Ј consensus sequence of viral mRNAs (37) and acts as a functional analog of poly(A) binding protein through its interaction with eIF4GI (36). NSP4 is both an intracellular glycoprotein receptor for maturating rotavirus particles that bud through the endoplasmic reticulum (3, 32) and a viral enterotoxin that induces diarrhea in mice in the absence of any other viral protein (5). Functions of the remaining nonstructural proteins, NSP1, NSP2, NSP5, and NSP6, have been proposed based predominately on biochemical properties and activities of recombinant proteins (reviewed in reference 17).NSP1 displays several interesting properties that warrant investigation. NSP1 has a calculated molecular weight of approximately 54,000 and is the least conserved protein encoded by the rotavirus genome when NSP1s of different strains are compared (23,34). The N terminus contains a conserved ...

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“…Numerous studies have demonstrated that rBoIFN-a can reduce and inhibit replication of many viruses including bovine herpesvirus type 1(BHV-1) (12,17,18), bovine viral diarrhea virus (BVDV) (13,18), parainfluenza-3 (13,18,19), bovine adenovirus (15), bovine respiratory syncytial virus (12), rotavirus (7), and foot and mouth disease virus (FMDV) (16). Although the findings with rHuIFN-a and rBoIFN-a administered to cattle in vivo have yielded promising results, the application of rBoIFN-a in clinics has been 70 JU ET AL.…”

Section: Discussionmentioning

confidence: 99%

Interferon-α Genes fromBosandBubalus bubalus

Shi

Xia

Pan

et al. 2006

Animal Biotechnology

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Interferon-a genes were cloned from six breeds of three species of two genera (three Chinese native cattle breeds of yellow cattle, wild yak and HuanHu domestic yak, one European breed of Holstein cow, and two water buffalo breeds of FuAn water buffalo and FuZhong water buffalo) by direct PCR. The PCR products were directly inserted into the expression vector to be sequenced and expressed. Sequence analysis showed that IFN-a genes of six clones were composed of 498 nucleotides, encoding a mature polypeptide with 166 amino acids. Compared with the published BoIFN-a subtypes, the IFN-a gene of Holstein cow had only one point mutation with the BoIFN-aA subtype. The IFN-a gene of yellow cattle was similar to the BoIFN-aD subtype with amino acid identity of 97.0% and may be considered as a new subtype, namely, BoIFN-aD1. The other four IFN-a genes, cloned from wild yak and HuanHu domestic yak, FuAn water buffalo, and FuZhong water buffalo, represented four new subtypes, namely, BoIFN-aI, BoIFN-aJ, BuIFN-a1, and BuIFN-a2, respectively. Each of the six clones was expressed in E. coli with molecular weight of approximately 20 kDa by SDS-PAGE and Western blot analyses. Antiviral activity assays showed that the six recombinant IFN-a (rIFN-a) all exhibited 1,000 times higher antiviral activity in the MDBK/VSV cell line than in the CEF/VSV one. Moreover, the rIFN-as could inhibit infectious bovine rhinotracheitis virus replication in the MDBK cell line using CPE inhibition method. The results suggested that rIFN-as a potential agent for clinical application against virus diseases in cattle industry.

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Cloning and Biologic Activities of a Bovine Interferon-α Isolated from the Epithelium of a Rotavirus-Infected Calf

Cited by 20 publications

References 12 publications

Characterization and antivirus activities of a novel bovine IFN-omega24

Characterization and antivirus activities of a novel bovine IFN-omega24

Interferon Regulatory Factor 3 Is a Cellular Partner of Rotavirus NSP1

Interferon-α Genes fromBosandBubalus bubalus

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