WASP-3b: a strongly irradiated transiting gas-giant planet

We report the discovery of WASP-3b, the third transiting exoplanet to be discovered by the WASP and SOPHIE collaboration. WASP-3b transits its host star USNO-B1.01256-0285133 every 1.846834 +/- 0.000002 d. Our high-precision radial velocity measurements present a variation with amplitude characteristic of a planetary-mass companion and in phase with the light curve. Adaptive optics imaging shows no evidence for nearby stellar companions, and line-bisector analysis excludes faint, unresolved binarity and stellar activity as the cause of the radial velocity variations. We make a preliminary spectroscopic analysis of the host star and find it to have Teff = 6400 +/- 100K and log g = 4.25 +/- 0.05 which suggests it is most likely an unevolved main-sequence star of spectral type F7-8V. Our simultaneous modelling of the transit photometry and reflex motion of the host leads us to derive a mass of 1.76+0.08-0.14 MJ and radius 1.31+0.07-0.14 RJ for WASP-3b. The proximity and relative temperature of the host star suggests that WASP-3b is one of the hottest exoplanets known, and thus has the potential to place stringent constraints on exoplanet atmospheric models.

Discovery of Spatial Periodicities in a Coronal Loop Using Automated Edge-Tracking Algorithms

A new method for automated coronal loop tracking, in both spatial and temporal domains, is presented. Applying this technique to TRACE data, obtained using the 171 angstrom filter on 1998 July 14, we detect a coronal loop undergoing a 270 s kink-mode oscillation, as previously found by Aschwanden et al. However, we also detect flare-induced, and previously unnoticed, spatial periodicities on a scale of 3500 km, which occur along the coronal loop edge. Furthermore, we establish a reduction in oscillatory power for these spatial periodicities of 45% over a 222 s interval. We relate the reduction in detected oscillatory power to the physical damping of these loop-top oscillations.

Crystallization and preliminary X-ray diffraction analysis of naphthalene dioxygenase from Rhodococcus sp strain NCIMB 12038

The three-component naphthalene dioxygenase (NDO) enzyme system carries out the first step in the aerobic degradation of naphthalene to (+)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene by Rhodococcus sp. strain NCIMB 12038. The terminal oxygenase component (naphthalene 1,2-dioxygenase) that catalyzes this reaction belongs to the aromatic ring hydroxylating dioxygenase family and has been crystallized. These enzymes utilize a mononuclear nonheme iron centre to catalyze the addition of dioxygen to their respective substrates. In this reaction, two electrons, two protons and a dioxygen molecule are consumed. The Rhodococcus enzyme has only 33 and 29% sequence identity to the corresponding alpha- and beta-subunits of the NDO system of Pseudomonas putida NCIMB 9816-4, for which the tertiary structure has been reported. In order to determine the three-dimensional structure of the Rhodococcus NDO, diffraction-quality crystals have been prepared by the hanging-drop method. The crystals belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 87.5, b = 144, c = 185.6 Angstrom, alpha = beta = gamma = 90degrees, and diffract to 2.3 Angstrom resolution.

Inter-phyla studies on neuropeptides: the potential for broad-spectrum anthelmintic and/or endectocide discovery

Flatworm, nematode and arthropod parasites have proven their ability to develop resistance to currently available chemotherapeutics. The heavy reliance on chemotherapy and the ability of target species to develop resistance has prompted the search for novel drug targets. In view of its importance to parasite/pest survival, the neuromusculature of parasitic helminths and pest arthropod species remains an attractive target for the discovery Of novel endectocide targets. Exploitation of the neuropeptidergic system in helminths and arthropods has been hampered by a limited Understanding of the functional roles of individual peptides and the structure of endogenous targets, such as receptors. Basic research into these systems has the potential to facilitate target characterization and its offshoots (screen development and drug identification). Of particular interest to parasitologists is the fact that selected neuropeptide families are common to metazoan pest species (nematodes, platyhelminths and arthropods) and fulfil specific roles in the modulation of muscle function in each of the three phyla. This article reviews the inter-phyla activity of two peptide families, the FMRFamide-like peptides and allatostatins, on motor function in helminths and arthropods and discusses the potential of neuropeptide signalling as a target system that could uncover novel endectocidal agents.

Isolation and preliminary biological assessment of AADGAPLIRFamide and SVPGVLRFamide from Caenorhabditis elegans

To date, 9 FMRFamide-related peptides (FaRPs) have been structurally characterised from Caenorhabditis elegans. Radioimmunometrical screening of an ethanolic extract of C. elegans revealed the presence of two additional FaRPs that were purified by reverse-phase HPLC and subjected to Edman degradation analysis and gas-phase sequencing. Unequivocal primary structures for the two FaRPs were determined as Ala-Ala-Asp-Gly-Ala-Pro-Leu-Ile-Arg-Phe-NH2 and Ser-Val-Pro-Gly-Val-Leu-Arg-Phe-NH2. Using MALDI-TOF mass. spectrometry, the molecular masses of the peptides were found to be 1032 Da (MH) and 875 Da (MH)(+), respectively. Two copies of AADGAPLIRFamide are predicted to be encoded on the precursor gene termed flp-13, while one copy of SVPGVLRFamide is located on flp-18. Synthetic replicates of the peptides were tested on Ascaris suum somatic muscle to assess bioactivity. ADDGAPLIRFamide had inhibitory effects on A. suum muscle strips, which occurred over a range of concentrations from a threshold for activity of 10 nM to 10 muM. SVPGVLRFamide was excitatory on A. suum somatic musculature from a threshold concentration for activity of 1 nM to 10 muM. The inhibitory and excitatory effects of AADGAPLIRFamide and SVPGVLRFamide, respectively, were the same for dorsal and ventral muscle strips as well as innervated and denervated preparations, suggesting that these physiological effects are not nerve cord dependent. Addition of ADDGAPLIRFamide (10 muM) to muscle strips preincubated in high-K+ and -Ca2+-free medium resulted in a normal inhibitory response. Peptide addition to muscle strips preincubated in Cl--free medium showed no inhibitory response, suggesting that the inhibitory response of the peptide may be chloride mediated. A normal excitatory response was noted following the addition of 10 muM SVPGVLRFamide to muscle strips preincubated in high-K+, Ca2+- and Cl--free media. (C) 2001 Academic Press.