title: Poxvirus antagonism of innate immunity by Bcl-2 fold proteins.
abstract: Poxviruses have evolved numerous mechanisms to evade host innate immunity. Sensory pathways that are activated by Toll-like and nucleotide receptors, as well as innate cell death pathways, are both targets of antagonism by viral proteins. Recent structural, biochemical and functional studies of poxvirus proteins have identified a family of α-helical proteins that adopt a Bcl-2 fold despite highly divergent polypeptide sequences from cellular proteins that regulate apoptosis. These newly identified proteins have assumed new roles in antagonism of NF-κB and interferon signaling pathways and interfere with the release of pro-inflammatory cytokines. Structures of isolated viral proteins and their complexes with cellular targets provide insight into the diverse ways that the Bcl-2 scaffold can be exploited for antagonism of host immunity.
authors.affiliation: School of Biochemistry & Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Pearse Street, Dublin 2, Ireland.
authors.forename: Edward
authors.initials: E
authors.lastname: Franklin
authors.forename: Amir R
authors.initials: AR
authors.lastname: Khan
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017209:Apoptosis; D017124:Conserved Sequence; D054884:Host-Pathogen Interactions; D006801:Humans; D007113:Immunity, Innate; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011212:Poxviridae / Q000276:immunology / Q000502:physiology*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D019253:Proto-Oncogene Proteins c-bcl-2 / Q000737:chemistry / Q000502:physiology*; D015398:Signal Transduction; D040681:Structural Homology, Protein; D014764:Viral Proteins / Q000737:chemistry / Q000502:physiology*
chemical_list: D019253:Proto-Oncogene Proteins c-bcl-2; D014764:Viral Proteins