B30.2-like Domain Proteins: A Growing Family

Henry, Joëlle; Mt, Ribouchon; Offer, Claudine; Pontarotti, Pierre

doi:10.1006/bbrc.1997.6751

Cited by 81 publications

(57 citation statements)

References 17 publications

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“…This binding is most likely not due to unspecific 'stickyness' of the RFP domain, because interaction with the CARD of procaspase-1, the LRR 36,37 Recently, it was shown that the RFP domain of TRIM5 is responsible for HIV-1 restriction in rhesus monkeys. 38 This finding and our results suggest that this domain is a crucial protein-binding domain.…”

Section: Discussionmentioning

confidence: 99%

The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

et al. 2006

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The estrogen-responsive B box protein (EBBP) and Pyrin belong to a family of structurally related proteins. While mutations in the pyrin gene cause an autoinflammatory disease, the biological function of EBBP is unknown. In this study, we identified the proinflammatory cytokine interleukin1b (IL-1b) as an EBBP-binding partner. Furthermore, caspase-1 and NACHT, LRR and Pyrin domain containing protein (NALP) 1, two components of the recently identified inflammasome, a platform for the activation of caspase-1, also interact with EBBP. These proteins bind to the RFP domain of EBBP, suggesting that this domain of so far unknown function is an important protein-binding domain. EBBP was secreted in a caspase-1-dependent manner from cultured cells, and its secretion was enhanced by IL-1b. Vice versa, endogenous and overerexpressed EBBP increased IL-1b secretion. These results provide evidence for a role of EBBP in innate immunity by enhancing the alternative secretion pathway of IL-1b.

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Section: Discussionmentioning

confidence: 99%

The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

et al. 2006

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“…It was, therefore, named after the B30.2 exon in the MHC I region in which it was originally identified. The B30.2-like domain occurs in nuclear, cytoplasmic, transmembrane, or secreted proteins, particularly at the C-terminal regions and these proteins are classified according to the type and/or the function of N-terminal domains (20,21) domain proteins are found in diverse species and in different protein contexts, the function(s) of the B30.2-like domain is not clearly understood yet (20,21). Based on the structural similarity, we include ohanin as a new member of the rapidly expanding B30.2-like domain family.…”

Section: For Details)mentioning

confidence: 99%

“…Its B30.2-like domain interacts with xanthine dehydrogenase/oxidase and this interaction appears to be important for its function (26,27). Based on the assumption that proteins containing similar domains exert their functions through similar protein-protein interaction and mechanisms, Henry et al (20,21) proposed a mechanism for the hypotensive action of SNTX that is mediated through the release of endothelium-derived relaxing factor (probably NO or NO-yielding substances). Accordingly, SNTX through its B30.2-like domain would interact with xanthine oxidase relieving the xanthine oxidase-mediated inhibition of NO synthase.…”

Section: For Details)mentioning

confidence: 99%

“…Accordingly, SNTX through its B30.2-like domain would interact with xanthine oxidase relieving the xanthine oxidase-mediated inhibition of NO synthase. This in turn would lead to increased synthesis of NO and vasorelaxation (20,21,28,29). In our study, ohanin did not exhibit any significant effect on the blood pressure in anesthetized Sprague-Dawley rats up to the dose of 1 mg/kg when given intravenously.…”

Section: For Details)mentioning

confidence: 99%

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Ohanin, a Novel Protein from King Cobra Venom, Induces Hypolocomotion and Hyperalgesia in Mice

Pung

Wong

Kumar

et al. 2005

Journal of Biological Chemistry

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We have identified, purified, and determined the complete amino acid sequence of a novel protein, ohanin from Ophiophagus hannah (king cobra) venom. It is a small protein containing 107 amino acid residues with a molecular mass of 11951.47 ؎ 0.67 Da as assessed by electrospray ionization-mass spectrometry. It does not show similarity to any known families of snake venom proteins and hence is the first member of a new family of snake venom proteins. It shows similarity to PRY and SPRY domain proteins. It is nontoxic up to 10 mg/kg when injected intraperitoneally in mice. Ohanin produced statistically significant and dose-dependent hypolocomotion in mice. In a pain threshold assay, it showed dose-dependent hyperalgesic effect. The ability of the protein to elicit a response at greatly reduced doses when injected intracerebroventricularly as compared with intraperitoneal administration in both the locomotion and hot plate experiments strongly suggests that ohanin acts on the central nervous system. Since the natural abundance of the protein in the venom is low (ϳ1 mg/g), a synthetic gene was constructed and expressed. The recombinant protein, which was obtained in the insoluble fraction in Escherichia coli, was purified under denaturing condition and was refolded. Recombinant ohanin is structurally and functionally similar to native protein as determined by circular dichroism and hot plate assay, suggesting that it will be useful in future structure-function relationship studies.

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“…SNTX is a soluble heterodimeric assembly of two closely related proteins termed SNTX-α and -β that share sequence identity of ∼50% (3). With the exception of a C-terminal PRY SPla and the RYanodine Receptor (PRYSPRY) domain in each protein (4), SNTX shares no obvious sequence similarity to any structurally or functionally characterized molecule. SNTX induces species-specific hemolytic activity (2) by an apparent pore-forming mechanism (5).…”

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confidence: 99%

Stonefish toxin defines an ancient branch of the perforin-like superfamily

Ellisdon

Reboul

Panjikar

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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The lethal factor in stonefish venom is stonustoxin (SNTX), a heterodimeric cytolytic protein that induces cardiovascular collapse in humans and native predators. Here, using X-ray crystallography, we make the unexpected finding that SNTX is a pore-forming member of an ancient branch of the Membrane Attack ComplexPerforin/Cholesterol-Dependent Cytolysin (MACPF/CDC) superfamily. SNTX comprises two homologous subunits (α and β), each of which comprises an N-terminal pore-forming MACPF/CDC domain, a central focal adhesion-targeting domain, a thioredoxin domain, and a C-terminal tripartite motif family-like PRY SPla and the RYanodine Receptor immune recognition domain. Crucially, the structure reveals that the two MACPF domains are in complex with one another and arranged into a stable early prepore-like assembly. These data provide long sought after near-atomic resolution insights into how MACPF/CDC proteins assemble into prepores on the surface of membranes. Furthermore, our analyses reveal that SNTX-like MACPF/CDCs are distributed throughout eukaryotic life and play a broader, possibly immune-related function outside venom.H uman envenoming by the tropical stonefish (Synanceia horrida and related species) results in extreme pain, edema, hypotension, respiratory distress, and on rare occasions, death (1). The lethal factor in stonefish venom is an ∼150-kDa protein termed stonustoxin (SNTX), an unusual example of a vertebrate cytolytic protein complex (2). SNTX is a soluble heterodimeric assembly of two closely related proteins termed SNTX-α and -β that share sequence identity of ∼50% (3). With the exception of a C-terminal PRY SPla and the RYanodine Receptor (PRYSPRY) domain in each protein (4), SNTX shares no obvious sequence similarity to any structurally or functionally characterized molecule. SNTX induces species-specific hemolytic activity (2) by an apparent pore-forming mechanism (5). It induces platelet aggregation (6), and like the closely related Trachynilysin (from Synanceia trachynis), SNTX exhibits activity suggesting that it may function as a neurotoxin (7,8).Because eukaryote pore-forming toxins are relatively rare, we reasoned that SNTX might represent a new exemplar of a vertebrate pore-forming protein. Previous studies had shown that it was possible to purify and crystallize SNTX (9); however, no structure has been reported to date. Accordingly, to address the structural basis for SNTX activity, we determined its X-ray crystal structure.

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B30.2-like Domain Proteins: A Growing Family

Cited by 81 publications

References 17 publications

The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

Ohanin, a Novel Protein from King Cobra Venom, Induces Hypolocomotion and Hyperalgesia in Mice

Stonefish toxin defines an ancient branch of the perforin-like superfamily

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