CAR1, a TNFR–Related Protein, Is a Cellular Receptor for Cytopathic Avian Leukosis–Sarcoma Viruses and Mediates Apoptosis

Brojatsch, Jürgen; Naughton, John; Rolls, Melissa M.; Zingler, Kurt; Young, John A. T.

doi:10.1016/s0092-8674(00)81992-3

Cited by 225 publications

(249 citation statements)

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“…ALV uses certain membrane proteins as receptor sites to attach and get access into the cell. The main receptor proteins are those designated as Tva receptors for ALV subtype A (ALV-A), CAR1 for subtypes B & D, and SEAR for subtype E [2,15,55]. These proteins are encoded by autosomal genes called tumour virus (Tv) genes [7].…”

Section: Leukosis Virus Receptor Proteinsmentioning

confidence: 99%

Immunological basis of differences in disease resistance in the chicken

Zekarias

Huurne²,

Landman

et al. 2002

Vet. Res.

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-Genetic resistance to diseases is a multigenic trait governed mainly by the immune system and its interactions with many physiologic and environmental factors. In the adaptive immunity, T cell and B cell responses, the specific recognition of antigens and interactions between antigen presenting cells, T cells and B cells are crucial. It occurs through a network of mediator proteins such as the molecules of the major histocompatibility complex (MHC), T cell receptors, immunoglobulins and secreted proteins such as the cytokines and antibodies. The diversity of these proteins that mainly is due to an intrinsic polymorphism of the genes causes phenotypic variation in disease resistance. The well-known linkage of MHC polymorphism and Marek's disease resistance difference represents a classic model revealing immunological factors in resistance differences and diversity of mediator molecules. The molecular bases in any resistance variation to infectious pathogens are vaguely understood. This paper presents a review of the major immune mediators involved in resistance and susceptibility to infectious diseases and their functional mechanisms in the chicken. The genetic interaction of disease resistance with production traits and the environment is mentioned. et les interactions entre les cellules présentant des antigènes, les cellules T et B, sont cruciales. Cela se produit à travers un réseau de protéines médiatrices telles que les molécules du complexe majeur d'histocompatibilité (CMH), les récepteurs des cellules T, les immunoglobulines et les protéines sé-crétées telles que les cytokines et les anticorps. La diversité de ces protéines, qui est surtout due au polymorphisme intrinsèque des gènes, entraîne une variation phénotypique dans la résistance aux maladies. Le lien bien connu entre le polymorphisme du CMH et les différences dans la résistance à la maladie de Marek représente un modèle classique révélant les facteurs immunologiques dans les différences de résistance et la diversité dans les molécules médiatrices. Les bases moléculaires impliquées dans toute variation de résistance aux pathogènes infectieux sont à peu près comprises. Cet article présente une synthèse sur les principaux médiateurs de l'immunité impliqués dans la résis-tance et la sensibilité aux maladies infectieuses chez le poulet et leurs mécanismes fonctionnels. L'interaction génétique entre la résistance aux maladies et les traits de production et l'environnement est mentionnée.

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Section: Leukosis Virus Receptor Proteinsmentioning

confidence: 99%

Immunological basis of differences in disease resistance in the chicken

Zekarias

Huurne²,

Landman

et al. 2002

Vet. Res.

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“…Interestingly, ELR1 is a member of the TNFR protein family, and TNFR-like proteins have been identified as receptors for certain avian oncoviruses and as a co-receptor component (CD134) for FIV (Brojatsch et al, 1996;Adkins et al, 1997Adkins et al, , 2000de Parseval et al, 2004;Shimojima et al, 2004;Zhang et al, 2005;Barnard et al, 2006). Taken together, these observations suggest that EIAV may represent a critical transitional link between the simple oncoviruses and the more complex immunodeficiency lentiviruses in terms of genetic composition and receptor usage.…”

Section: Discussionmentioning

confidence: 99%

Binding of equine infectious anemia virus to the equine lentivirus receptor-1 is mediated by complex discontinuous sequences in the viral envelope gp90 protein

Sun

Zhang

Jin

et al. 2008

Journal of General Virology

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The identification and characterization of a functional cellular receptor for equine infectious anemia virus (EIAV), designated equine lentivirus receptor-1 (ELR1), a member of the tumour necrosis factor receptor protein family, has been reported previously . Proc Natl Acad Sci U S A, 102 , [9918][9919][9920][9921][9922][9923]. The finding of a single receptor for EIAV is distinct from feline, simian and human immunodeficiency viruses, which typically utilize two co-receptors for infection, but is similar to avian and murine oncoviruses, which use single receptors. This study sought to determine ELR1-binding domains of EIAV gp90. Towards this goal, a GFP-tagged gp90 fusion protein (gp90GFP) expression vector was constructed and a specific cell-cell binding assay was developed to measure EIAV gp90 binding to ELR1. Using these assays, the receptor-binding properties of 41 gp90GFP mutants were evaluated, each with a sequential replacement 11 aa linear epitope peptide from the vesicular stomatitis virus glycoprotein (VSV-G tag), as well as eight mutants containing individual gp90 variable-domain deletions. The results of these studies demonstrated that, in general, gp90 constructs containing substitutions or deletions in the N-terminal third of gp90 retained their receptor-binding activity. In contrast, segment substitutions or deletions in the C-terminal two-thirds of gp90 eliminated receptorbinding activity. Thus, these results reveal for the first time that the ELR1-binding domains of EIAV gp90 are located in the C-terminal two-thirds of EIAV gp90, apparently as a complex of discontinuous determinants. INTRODUCTIONAdsorption and entry of retroviruses into target cells requires the interaction of viral envelope (Env) glycoproteins with specific cellular receptor proteins. Retroviral envelope glycoproteins are synthesized as polyprotein precursors that are cleaved, during transport to the surface of infected cells, into the surface (SU) subunit and transmembrane (TM) subunit. The SU protein is bound at the virion surface through interaction with the TM protein and is responsible for the initial binding to receptor proteins on the target cell surface. Studies of the specificity of functional receptors for various retroviruses have indicated a general pattern of single receptor protein use by oncoviruses (such as murine and avian leukemia viruses) that is in distinct contrast to the dual co-receptor usage observed with the lentiviruses human immunodeficiency virus (HIV), simian immunodeficiency virus (SIV) and feline immunodeficiency virus (FIV) (Eiden et al., 1993;de Parseval et al., 2004;Douglas et al., 1997;Barnard et al., 2006). Whilst the general assumption has been that all lentiviruses may use dual co-receptors for infection of target cells, the recent identification of a single functional receptor for equine infectious anemia virus (EIAV) has revealed an unexpected diversity in lentivirus receptor specificity and interactions .Murine leukemia virus (MuLV) Env SU proteins and their interactions with receptors ...

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“…Interestingly, the chicken TVB receptor was originally isolated because of its ability to bind to envelope proteins of the cytopathic avian leukosis-sarcoma virus. 56 Although viruses may interact with the TVB receptor to mediate infection, the identification of a naturally occurring (as yet unidentified) ligand is anticipated. Its role in viral immune response is especially fascinating in the light of our results showing the TVB death domain to be relatively divergent from all other death receptors.…”

Section: G E L G -Y Q D E I I D S F T -R E E F P ----V R a M L S D W mentioning

confidence: 99%

All in the family: evolutionary and functional relationships among death receptors

et al. 2003

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Over the last decade, significant progress has been made towards identifying the signaling pathways within mammalian cells that lead to apoptosis mediated by death receptors. The simultaneous expression of more than one death receptor in many, if not all, cell types suggests that functional innovation has driven the divergence of these receptors and their cognate ligands. To better understand the physiological divergence of the death receptors, a phylogenetic analysis of vertebrate death receptors was conducted based upon aminoacid sequences encoding the death domain regions of currently known and newly identified members of the family. Evidence is presented to indicate an ancient radiation of death receptors that predates the emergence of vertebrates, as well as ongoing divergence of additional receptors both within several receptor lineages as well as modern taxonomic lineages. We speculate that divergence among death receptors has led to their functional specialization. For instance, some receptors appear to be primarily involved in mediating the immune response, while others play critical roles during development and tissue differentiation. The following represents an evolutionary approach towards an understanding of the complex relationship among death receptors and their proposed physiological functions in vertebrate species.

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CAR1, a TNFR–Related Protein, Is a Cellular Receptor for Cytopathic Avian Leukosis–Sarcoma Viruses and Mediates Apoptosis

Cited by 225 publications

References 64 publications

Immunological basis of differences in disease resistance in the chicken

Immunological basis of differences in disease resistance in the chicken

Binding of equine infectious anemia virus to the equine lentivirus receptor-1 is mediated by complex discontinuous sequences in the viral envelope gp90 protein

All in the family: evolutionary and functional relationships among death receptors

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