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More recently, smart agriculture has received widespread attention, which is a deep combination of modern agriculture and the Internet of Things (IoT) technology. To achieve the aim of scientific cultivation and precise control, the agricultural environments are monitored in real time by using various types of sensors. As a result, smart agricultural IoT generated a large amount of multidimensional time series data. However, due to the limitation of applied scenarios, smart agricultural IoT often suffers from data loss and misrepresentation. Moreover, some intelligent decision-makings for agricultural management also require the detailed analysis of data. To address the above problems, this article proposes a new anomaly detection model based on generative adversarial networks (GAN), which can process the multidimensional time series data generated by smart agricultural IoT. GAN is a deep learning model to learn the distribution patterns of normal data and capture the temporal dependence of time series and the potential correlations between features through learning. For the problem of generator inversion, an encoder-decoder structure incorporating the attention mechanism is designed to improve the performance of the model in learning normal data. In addition, we also present a new reconstruction error calculation method that measures the error in terms of both point-wise difference and curve similarity to improve the detection effect. Finally, based on three smart agriculture-related datasets, experimental results show that our proposed model can accurately achieve anomaly detection. The experimental precision, recall, and F1 score exceeded the counterpart models by reaching 0.9351, 0.9625, and 0.9482, respectively.
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In some emerging wireless applications, such as wearable communication and low-power sensor network applications, wireless devices or nodes not only require simple physical implementation approaches but also require certain reliable receiver techniques to overcome the effects of multipath or shadowed fading. Switched diversity combining (SDC) systems could be a simple and promising solution to the above requirements. Recently, a Fisher-Snedecor â± composited fading model has gained much interest because of its modeling accuracy and calculation tractability. However, the performance of SDC systems over â± fading channels has not yet been analyzed in the open literature. To this end, this paper presents a systematic analysis of SDC systems over â± fading channels, including dual-branch switch-and-stay combining (SSC), multibranch switch-and examine combining (SEC), and SEC with post-examining selection (SECps) systems. We first investigate the statistical characteristics of univariate and bivariate â± distributions. Then, these statistical expressions are introduced into the above SDC systems and the statistical metrics of the output signal-to-noise ratio (SNR) for these systems are deduced in different â± fading scenarios. Thirdly, certain exact and novel expressions of performance criteria, such as the outage probability, the average bit error probability and average symbol error probability, as well as the average channel capacity for SSC, SEC, and SECps are derived. To find the optimum performance, optimal analysis is performed for the independent and identically distributed cases. Finally, numerical evaluation and simulations are carried out to demonstrate the validity of the theoretical analysis under various â± fading scenarios. According to the obtained results, the multipath fading parameter has more influence on the performance of SDC systems than the shadowing parameter, the correlation coefficient, or the average SNR. Importantly, the SDC systems can provide switched diversity gains only when the switching threshold is not too large or too small compared to the average SNR.
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Power dissipation is a fundamental issue for future chip-based electronics. As promising channel materials, two-dimensional semiconductors show excellent capabilities of scaling dimensions and reducing off-state currents. However, field-effect transistors based on two-dimensional materials are still confronted with the fundamental thermionic limitation of the subthreshold swing of 60 mV decade-1 at room temperature. Here, we present an atomic threshold-switching field-effect transistor constructed by integrating a metal filamentary threshold switch with a two-dimensional MoS2 channel, and obtain abrupt steepness in the turn-on characteristics and 4.5 mV decade-1 subthreshold swing (over five decades). This is achieved by using the negative differential resistance effect from the threshold switch to induce an internal voltage amplification across the MoS2 channel. Notably, in such devices, the simultaneous achievement of efficient electrostatics, very small sub-thermionic subthreshold swings, and ultralow leakage currents, would be highly desirable for next-generation energy-efficient integrated circuits and ultralow-power applications.
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Correlation electromagnetic analysis (CEMA) is a method prevalent in side-channel analysis of cryptographic devices. Its success mostly depends on the quality of electromagnetic signals acquired from the devices. In the past, only one byte of the key was analyzed and other bytes were regarded as noise. Apparently, other bytes' useful information was wasted, which may increase the difficulty of recovering the key. Multi-objective optimization is a good way to solve the problem of a single byte of the key. In this work, we applied multi-objective optimization to correlation electromagnetic analysis taking all bytes of the key into consideration. Combining the advantages of multi-objective optimization and genetic algorithm, we put forward a novel multi-objective electromagnetic analysis based on a genetic algorithm to take full advantage of information when recovering the key. Experiments with an Advanced Encryption Standard (AES) cryptographic algorithm on a Sakura-G board demonstrate the efficiency of our method in practice. The experimental results show that our method reduces the number of traces required in correlation electromagnetic analysis. It achieved approximately 42.72% improvement for the corresponding case compared with CEMA.
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Carbon nanotubes (CNTs) are promising candidates for smart electronic devices. However, it is challenging to mediate their bandgap or chirality from a vapor-liquid-solid growth process. Here, we demonstrate rate-selected semiconducting CNT arrays based on interlocking between the atomic assembly rate and bandgap of CNTs. Rate analysis confirms the Schulz-Flory distribution which leads to various decay rates as length increases in metallic and semiconducting CNTs. Quantitatively, a nearly ten-fold faster decay rate of metallic CNTs leads to a spontaneous purification of the predicted 99.9999% semiconducting CNTs at a length of 154 mm, and the longest CNT can be 650 mm through an optimized reactor. Transistors fabricated on them deliver a high current of 14 µA µm-1 with on/off ratio around 108 and mobility over 4000 cm2 V-1 s-1. Our rate-selected strategy offers more freedom to control the CNT purity in-situ and offers a robust methodology to synthesize perfectly assembled nanotubes over a long scale.
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Targeted therapy against VEGF and mTOR pathways has been established as the standard-of-care for metastatic clear cell renal cell carcinoma (ccRCC); however, these treatments frequently fail and most patients become refractory requiring subsequent alternative therapeutic options. Therefore, development of innovative and effective treatments is imperative. About 80%-90% of ccRCC tumors express an inactive mutant form of the von Hippel-Lindau protein (pVHL), an E3 ubiquitin ligase that promotes target protein degradation. Strong genetic and experimental evidence supports the correlate that pVHL functional loss leads to the accumulation of the transcription factor hypoxia-inducible factor 2α (HIF2α) and that an overabundance of HIF2α functions as a tumorigenic driver of ccRCC. In this report, we describe an RNAi therapeutic for HIF2α that utilizes a targeting ligand that selectively binds to integrins αvß3 and αvß5 frequently overexpressed in ccRCC. We demonstrate that functional delivery of a HIF2α-specific RNAi trigger resulted in HIF2α gene silencing and subsequent tumor growth inhibition and degeneration in an established orthotopic ccRCC xenograft model. Mol Cancer Ther; 17(1); 140-9. ©2017 AACR.
Assuntos
Carcinoma de Células Renais/terapia , Subunidade alfa do Fator 1 Induzível por Hipóxia/genética , RNA Interferente Pequeno/administração & dosagem , Animais , Carcinoma de Células Renais/genética , Carcinoma de Células Renais/metabolismo , Carcinoma de Células Renais/patologia , Linhagem Celular Tumoral , Feminino , Inativação Gênica , Humanos , Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo , Integrina alfaVbeta3/metabolismo , Camundongos , Camundongos Nus , Interferência de RNA , RNA Interferente Pequeno/genética , Receptores de Vitronectina/metabolismo , Ensaios Antitumorais Modelo de XenoenxertoRESUMO
Bispecific antibodies (bsAbs) that bind to cell surface antigens and to digoxigenin (Dig) were used for targeted small interfering RNA (siRNA) delivery. They are derivatives of immunoglobulins G (IgGs) that bind tumor antigens, such as Her2, IGF1-R, CD22, and LeY, with stabilized Dig-binding variable domains fused to the C-terminal ends of the heavy chains. siRNA that was digoxigeninylated at its 3'end was bound in a 2:1 ratio to the bsAbs. These bsAb-siRNA complexes delivered siRNAs specifically to cells that express the corresponding antigen as demonstrated by flow cytometry and confocal microscopy. The complexes internalized into endosomes and Dig-siRNAs separated from bsAbs, but Dig-siRNA was not released into the cytoplasm; bsAb-targeting alone was thus not sufficient for effective mRNA knockdown. This limitation was overcome by formulating the Dig-siRNA into nanoparticles consisting of dynamic polyconjugates (DPCs) or into lipid-based nanoparticles (LNPs). The resulting complexes enabled bsAb-targeted siRNA-specific messenger RNA (mRNA) knockdown with IC(50) siRNA values in the low nanomolar range for a variety of bsAbs, siRNAs, and target cells. Furthermore, pilot studies in mice bearing tumor xenografts indicated mRNA knockdown in endothelial cells following systemic co-administration of bsAbs and siRNA formulated in LNPs that were targeted to the tumor vasculature.Molecular Therapy - Nucleic Acids (2012) 1, e45; doi:10.1038/mtna.2012.39; published online 18 September 2012.
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Previous studies have shown that the skeletal dihydropyridine receptor (DHPR) pore subunit Ca(V)1.1 (alpha1S) physically interacts with ryanodine receptor type 1 (RyR1), and a molecular signal is transmitted from alpha1S to RyR1 to trigger excitation-contraction (EC) coupling. We show that the beta-subunit of the skeletal DHPR also binds RyR1 and participates in this signaling process. A novel binding site for the DHPR beta1a-subunit was mapped to the M(3201) to W(3661) region of RyR1. In vitro binding experiments showed that the strength of the interaction is controlled by K(3495)KKRR_ _R(3502), a cluster of positively charged residues. Phenotypic expression of skeletal-type EC coupling by RyR1 with mutations in the K(3495)KKRR_ _R(3502) cluster was evaluated in dyspedic myotubes. The results indicated that charge neutralization or deletion severely depressed the magnitude of RyR1-mediated Ca(2+) transients coupled to voltage-dependent activation of the DHPR. Meantime the Ca(2+) content of the sarcoplasmic reticulum was not affected, and the amplitude and activation kinetics of the DHPR Ca(2+) currents were slightly affected. The data show that the DHPR beta-subunit, like alpha1S, interacts directly with RyR1 and is critical for the generation of high-speed Ca(2+) signals coupled to membrane depolarization. These findings indicate that EC coupling in skeletal muscle involves the interplay of at least two subunits of the DHPR, namely alpha1S and beta1a, interacting with possibly different domains of RyR1.
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Canais de Cálcio Tipo L/química , Canais de Cálcio/metabolismo , Sequência de Aminoácidos , Animais , Sítios de Ligação , Osso e Ossos/metabolismo , Cálcio/química , Cálcio/metabolismo , Caveolina 1/química , Células Cultivadas , DNA Complementar/metabolismo , Glutationa Transferase/metabolismo , Cinética , Camundongos , Microscopia Confocal , Modelos Genéticos , Dados de Sequência Molecular , Músculo Esquelético/citologia , Músculos/citologia , Músculos/patologia , Mutação , Técnicas de Patch-Clamp , Fenótipo , Ligação Proteica , Estrutura Secundária de Proteína , Estrutura Terciária de Proteína , Proteínas Recombinantes/química , Canal de Liberação de Cálcio do Receptor de Rianodina/química , Retículo Sarcoplasmático/metabolismo , Homologia de Sequência de Aminoácidos , Relação Estrutura-Atividade , Termodinâmica , TransfecçãoRESUMO
Maurocalcine is a scorpion venom toxin of 33 residues that bears a striking resemblance to the domain A of the dihydropyridine voltage-dependent calcium channel type 1.1 (Cav1.1) subunit. This domain belongs to the II-III loop of Cav1.1, which is implicated in excitation-contraction coupling. Besides the structural homology, maurocalcine also modulates RyR1 channel activity in a manner akin to a synthetic peptide of domain A. Because of these similarities, we hypothesized that maurocalcine and domain A may bind onto an identical region(s) of RyR1. Using a set of RyR1 fragments, we demonstrate that peptide A and maurocalcine bind onto two discrete RyR1 regions: fragments 3 and 7 encompassing residues 1021-1631 and 3201-3661, respectively. The binding onto fragment 7 is of greater importance and was thus further investigated. We found that the amino acid region 3351-3507 of RyR1 (fragment 7.2) is sufficient for these interactions. Proof that peptide A and maurocalcine bind onto the same site is provided by competition experiments in which binding of fragment 7.2 to peptide A is inhibited by preincubation with maurocalcine. Moreover, when expressed in COS-7 cells, RyR1 carrying a deletion of fragment 7 shows a loss of interaction with both peptide A and maurocalcine. At the functional level, this deletion abolishes the maurocalcine induced stimulation of [3H]ryanodine binding onto microsomes of transfected COS-7 cells without affecting the caffeine and ATP responses.
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Canais de Cálcio Tipo L/química , Caveolinas/química , Venenos de Escorpião/farmacologia , Trifosfato de Adenosina/química , Animais , Sítios de Ligação , Ligação Competitiva , Células COS , Caveolina 1 , Cromatografia , Clonagem Molecular , Microscopia Crioeletrônica , Microscopia de Fluorescência , Músculo Esquelético/metabolismo , Peptídeos/química , Plasmídeos/metabolismo , Ligação Proteica , Estrutura Terciária de Proteína , Proteínas Recombinantes de Fusão/química , Rianodina/química , Canal de Liberação de Cálcio do Receptor de Rianodina/química , Venenos de Escorpião/química , TransfecçãoRESUMO
Chimeras consisting of the homologous skeletal dihydropyridine receptor (DHPR) beta1a subunit and the heterologous cardiac/brain beta2a subunit were used to determine which regions of beta1a were responsible for the skeletal-type excitation-contraction (EC) coupling phenotype. Chimeras were transiently transfected in beta1 knockout myotubes and then voltage-clamped with simultaneous measurement of confocal fluo-4 fluorescence. All chimeras expressed a similar density of DHPR charge movements, indicating that the membrane density of DHPR voltage sensors was not a confounding factor in these studies. The data indicates that a beta1a-specific domain present in the carboxyl terminus, namely the D5 region comprising the last 47 residues (beta1a 478-524), is essential for expression of skeletal-type EC coupling. Furthermore, the location of beta1aD5 immediately downstream from conserved domain D4 is also critical. In contrast, chimeras in which beta1aD5 was swapped by the D5 region of beta2a expressed Ca(2+) transients triggered by the Ca(2+) current, or none at all. A hydrophobic heptad repeat is present in domain D5 of beta1a (L478, V485, V492). To determine the role of this motif, residues in the heptad repeat were mutated to alanines. The triple mutant beta1a(L478A/V485A/V492A) recovered weak skeletal-type EC coupling (DeltaF/F(max) = 0.4 +/- 0.1 vs. 2.7 +/- 0.5 for wild-type beta1a). However, a triple mutant with alanine substitutions at positions out of phase with the heptad repeat, beta1a(S481A/L488A/S495A), was normal (DeltaF/F(max) = 2.1 +/- 0.4). In summary, the presence of the beta1a-specific D5 domain, in its correct position after conserved domain D4, is essential for skeletal-type EC coupling. Furthermore, a heptad repeat in beta1aD5 controls the EC coupling activity. The carboxyl terminal heptad repeat of beta1a might be involved in protein-protein interactions with ryanodine receptor type 1 required for DHPR to ryanodine receptor type 1 signal transmission.
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Canais de Cálcio Tipo L/química , Canais de Cálcio Tipo L/metabolismo , Sinalização do Cálcio/fisiologia , Potenciais da Membrana/fisiologia , Contração Muscular/fisiologia , Fibras Musculares Esqueléticas/fisiologia , Músculo Esquelético/fisiologia , Animais , Células Cultivadas , Camundongos , Mutagênese Sítio-Dirigida , Engenharia de Proteínas , Estrutura Terciária de Proteína , Subunidades Proteicas/química , Subunidades Proteicas/metabolismo , Proteínas Recombinantes/metabolismo , Relação Estrutura-AtividadeRESUMO
Molecular understanding of the mechanism of excitation-contraction (EC) coupling in skeletal muscle has been made possible by cultured myotube models lacking specific dihydropyridine receptor (DHPR) subunits and ryanodine receptor type 1 (RyR1) isoforms. Transient expression of missing cDNAs in mutant myotubes leads to a rapid recovery, within days, of various Ca2+ current and EC coupling phenotypes. These myotube models have thus permitted structure-function analysis of EC coupling domains present in the DHPR controlling the opening of RyR1. The purpose of this brief review is to highlight advances made by this laboratory towards understanding the contribution of domains present in alpha1S and beta1a subunits of the skeletal DHPR to EC coupling signaling. Our main contention is that domains of the alpha1S II-III loop are necessary but not sufficient to recapitulate skeletal-type EC coupling. Rather, the structural unit that controls the EC coupling signal appears to be the alpha1S/beta1a pair.
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Canais de Cálcio Tipo L/fisiologia , Contração Muscular/fisiologia , Músculo Esquelético/fisiologia , Animais , Canais de Cálcio Tipo L/genética , DNA Complementar/análise , Eletrofisiologia , Microscopia Confocal , Modelos Biológicos , Fibras Musculares Esqueléticas/fisiologia , Canal de Liberação de Cálcio do Receptor de Rianodina/metabolismoRESUMO
We investigated the contribution of the carboxyl terminus region of the beta1a subunit of the skeletal dihydropyridine receptor (DHPR) to the mechanism of excitation-contraction (EC) coupling. cDNA-transfected beta1 KO myotubes were voltage clamped, and Ca(2+) transients were analyzed by confocal fluo-4 fluorescence. A chimera with an amino terminus half of beta2a and a carboxyl terminus half of beta1a (beta2a 1-287/beta1a 325-524) recapitulates skeletal-type EC coupling quantitatively and was used to generate truncated variants lacking 7 to 60 residues from the beta1a-specific carboxyl terminus (Delta7, Delta21, Delta29, Delta35, and Delta60). Ca(2+) transients recovered by the control chimera have a sigmoidal Ca(2+) fluorescence (DeltaF/F) versus voltage curve with saturation at potentials more positive than +30 mV, independent of external Ca(2+) and stimulus duration. In contrast, the amplitude of Ca(2+) transients expressed by the truncated variants varied with the duration of the pulse, and for Delta29, Delta35, and Delta60, also varied with external Ca(2+) concentration. For Delta7 and Delta21, a 50-ms depolarization produced a sigmoidal DeltaF/F versus voltage curve with a lower than control maximum fluorescence. Moreover, for Delta29, Delta35, and Delta60, a 200-ms depolarization increased the maximum fluorescence and changed the shape of the DeltaF/F versus voltage curve, from sigmoidal to bell-shaped, with a maximum at approximately +30 mV. The change in voltage dependence, together with the external Ca(2+) dependence and additional controls with ryanodine, indicated a loss of skeletal-type EC coupling and the emergence of an EC coupling component triggered by the Ca(2+) current. Analyses of d(DeltaF/F)/dt showed that the rate of cytosolic Ca(2+) increase during the Ca(2+) transient was fivefold faster for the control chimera than for the severely truncated variants (Delta29, Delta35, and Delta60) and was consistent with the kinetics of the DHPR Ca(2+) current. In summary, absence of the beta1a-specific carboxyl terminus (last 29 to 60 residues of the control chimera) results in a loss of the fast component of the Ca(2+) transient, bending of the DeltaF/F versus voltage curve, and emergence of EC coupling triggered by the Ca(2+) current. The studies underscore the essential role of the carboxyl terminus region of the DHPR beta1a subunit in fast voltage dependent EC coupling in skeletal myotubes.
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Canais de Cálcio Tipo L/química , Canais de Cálcio Tipo L/fisiologia , Cálcio/metabolismo , Contração Muscular/fisiologia , Fibras Musculares Esqueléticas/fisiologia , Animais , Cálcio/farmacologia , Canais de Cálcio/química , Canais de Cálcio/genética , Canais de Cálcio/metabolismo , Canais de Cálcio Tipo L/genética , Dióxido de Carbono/química , Dióxido de Carbono/fisiologia , Células Cultivadas , Clonagem Molecular , Membro Posterior/embriologia , Membro Posterior/fisiologia , Potenciais da Membrana/efeitos dos fármacos , Potenciais da Membrana/fisiologia , Contração Muscular/genética , Fibras Musculares Esqueléticas/química , Mutagênese Sítio-Dirigida , Conformação Proteica , Subunidades Proteicas/química , Subunidades Proteicas/fisiologia , Sensibilidade e Especificidade , Transformação GenéticaRESUMO
The beta-subunit of the dihydropyridine receptor (DHPR) enhances the Ca(2+) channel and voltage-sensing functions of the DHPR. In skeletal myotubes, there is additional modulation of DHPR functions imposed by the presence of ryanodine receptor type-1 (RyR1). Here, we examined the participation of the beta-subunit in the expression of L-type Ca(2+) current and charge movements in RyR1 knock-out (KO), beta1 KO, and double beta1/RyR1 KO myotubes generated by mating heterozygous beta1 KO and RyR1 KO mice. Primary myotube cultures of each genotype were transfected with various beta-isoforms and then whole-cell voltage-clamped for measurements of Ca(2+) and gating currents. Overexpression of the endogenous skeletal beta1a isoform resulted in a low-density Ca(2+) current either in RyR1 KO (36 +/- 9 pS/pF) or in beta1/RyR1 KO (34 +/- 7 pS/pF) myotubes. However, the heterologous beta2a variant with a double cysteine motif in the N-terminus (C3, C4), recovered a Ca(2+) current that was entirely wild-type in density in RyR1 KO (195 +/- 16 pS/pF) and was significantly enhanced in double beta1/RyR1 KO (115 +/- 18 pS/pF) myotubes. Other variants tested from the four beta gene families (beta1a, beta1b, beta1c, beta3, and beta4) were unable to enhance Ca(2+) current expression in RyR1 KO myotubes. In contrast, intramembrane charge movements in beta2a-expressing beta1a/RyR1 KO myotubes were significantly lower than in beta1a-expressing beta1a/RyR1 KO myotubes, and the same tendency was observed in the RyR1 KO myotube. Thus, beta2a had a preferential ability to recover Ca(2+) current, whereas beta1a had a preferential ability to rescue charge movements. Elimination of the double cysteine motif (beta2a C3,4S) eliminated the RyR1-independent Ca(2+) current expression. Furthermore, Ca(2+) current enhancement was observed with a beta2a variant lacking the double cysteine motif and fused to the surface membrane glycoprotein CD8. Thus, tethering the beta2a variant to the myotube surface activated the DHPR Ca(2+) current and bypassed the requirement for RyR1. The data suggest that the Ca(2+) current expressed by the native skeletal DHPR complex has an inherently low density due to inhibitory interactions within the DHPR and that the beta1a-subunit is critically involved in process.
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Canais de Cálcio Tipo L/fisiologia , Canais de Cálcio/fisiologia , Fibras Musculares Esqueléticas/fisiologia , Subunidades Proteicas/fisiologia , Canal de Liberação de Cálcio do Receptor de Rianodina/deficiência , Animais , Cálcio/metabolismo , Canais de Cálcio Tipo L/química , Células Cultivadas , Condutividade Elétrica , Potenciais da Membrana/fisiologia , Camundongos , Camundongos Knockout , Fibras Musculares Esqueléticas/química , Mutagênese Sítio-Dirigida , Estrutura Terciária de Proteína , Subunidades Proteicas/química , Proteínas Recombinantes , Canal de Liberação de Cálcio do Receptor de Rianodina/fisiologia , Sensibilidade e Especificidade , TransfecçãoRESUMO
A fundamental problem of plant science is to understand the biochemical basis of plant/pathogen interactions. The foliar disease tan spot of wheat (Triticum aestivum), caused by Pyrenophora tritici-repentis, involves Ptr ToxA, a proteinaceous host-selective toxin that causes host cell death. The fungal gene ToxA encodes a 17.2-kD pre-pro-protein that is processed to produce the mature 13.2-kD toxin. Amino acids 140 to 142 of the pre-pro-protein form an arginyl-glycyl-aspartic (RGD) sequence, a motif involved in the binding of some animal proteins and pathogens to transmembrane receptor proteins called integrins. Integrin-like proteins have been identified in plants recently, but their role in plant biology is unclear. Our model for Ptr ToxA action predicts that toxin interacts with a putative host receptor through the RGD motif. Mutant clones of a ToxA cDNA, created by polymerase chain reaction such that the RGD in the pro-toxin was changed to arginyl-alanyl-aspartic or to arginyl-glycyl-glutamic, were expressed in Escherichia coli. Extracts containing mutated forms of toxin failed to cause host cell death, but extracts from E. coli expressing both a wild-type pro-protein cDNA and a control mutation away from RGD were active in cell death development. In competition experiments, 2 mM RGD tripeptide reduced the level of electrolyte leakage from wheat leaves by 63% when co-infiltrated with purified Ptr ToxA (15 microg mL(-1)) obtained from the fungus, but the control peptide arginyl-glycyl-glutamyl-serine provided no protection. These experiments indicate that the RGD motif of Ptr ToxA is involved with toxin action, possibly by interacting with a putative integrin-like receptor in the host.