The mitochondrial genome of the venomous cone snail conus consors

Cone snails are venomous predatory marine neogastropods that belong to the species-rich superfamily of the Conoidea. So far, the mitochondrial genomes of two cone snail species (Conus textile and Conus borgesi) have been described, and these feed on snails and worms, respectively. Here, we report the mitochondrial genome sequence of the fish-hunting cone snail Conus consors and describe a novel putative control region (CR) which seems to be absent in the mitochondrial DNA (mtDNA) of other cone snail species. This possible CR spans about 700 base pairs (bp) and is located between the genes encoding the transfer RNA for phenylalanine (tRNA-Phe, trnF) and cytochrome c oxidase subunit III (cox3). The novel putative CR contains several sequence motifs that suggest a role in mitochondrial replication and transcription

The relationships of the enigmatic gastropod Tritonoharpa (Neogastropoda): New data on early neogastropod evolution?

In this paper, the relationships of Tritonoharpa Dall, 1908, within Neogastropoda are discussed. Tritonoharpa is indeed similar to Colubraria in the morphology of its head-foot, pallial complex, reproductive and excretory systems, in the presence of an extremely long and coiled proboscis, and a very large stomach. However, it differs from Colubraria in the rest of its foregut anatomy, revealing a cancellariid affinity, and a typical nematoglossan radula. The molecular data confirms Beu and Maxwell's placement of Tritonoharpa in the Cancellariidae, close to Plesiotriton. It is also suggested that cancellariids may be the sister-group to the rest of neogastropods. Tritonoharpa has a rather large and well developed midgut gland, resembling the gland of Leiblein. As previously studied cancellarioideans have been shown to lack a well differentiated gland of Leiblein, the present study raises some interesting questions about the evolution of the foregut in Neogastropoda. In fact, if this glandular structure were confirmed as a true homologue of the gland of Leiblein, and the cancellarioideans proved to be the sister group to the remaining neogastropods, the possession of the gland should be considered a synapomorphy of the Neogastropoda

Celulární automat a CML systémy

The main aim of this thesis is the study of cellular automata and discrete dynamical systems on a lattice. Both tools, cellular automata as well as dynamical systems on a lattice are introduced and elementary properties described. The relation between cellular automata and dynamical system on lattice is derived. The main goal of the thesis is also the use of the cellular automata as that mathematical tool of evolution visualization of discrete dynamical systems. The theory of cellular automata is applied to the discrete dynamical systems on a lattice Laplacian type and implemented in Java language.Hlavním cílem práce je studium vztahu celulárních automatů a diskrétních dynamických systémů na mřížce. Oba nástroje, jak celulární automat tak dynamický systém na mřížce, jsou zavedeny a jejich základní vlastnosti popsány. Vztah mezi celulárními automaty a dynamickými systémy na mřížce je podrobně popsán. Hlavním cílem práce je dále použití nástroje celulárního automatu jako matematického vizualizačního prostředku evoluce diskrétních dynamických systémů. Teorie celulárních automatů je použita na dynamické systémy na mřížce Lamplaceova typu a implementována v prostředí Java.470 - Katedra aplikované matematikyvelmi dobř

Conopeptides from Cape Verde Conus crotchii

Marine Cone snails of the genus Conus contain complex peptide toxins in their venom. Living in tropical habitats, they usually use the powerful venom for self-defense and prey capture. Here, we study Conus crotchii venom duct using a peptide mass-matching approach. The C. crotchii was collected on the Cape Verde archipelago in the Boa Vista Island. The venom was analyzed using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). About 488 molecular masses between 700 Da and 3000 Da were searched bymatching with known peptide sequences from UniProtKB protein sequence database. Through this method we were able to identify 12 conopeptides. For validation we considered the error between the experimental molecular mass (monoisotopic) and the calculated mass of less than 0.5 Da. All conopeptides detected belong to the A-, O1-, O2-, O3-, T- and D-superfamilies, which can block Ca2+ channels, inhibit K+ channels and act on nicotinic acetylcholine receptors (nAChRs). Only a few of the detected peptides have a 100% UniProtKB database similarity, suggesting that several of them could be newly discovered marine drugs

Biotoxicity in Marine Organisms

The results from the screening of 118 marine organisms (corals, alcyoniarians, mollusks, echinoderms, flagellates) found in the coastal waters of India for their toxicity on fish and mice fingerlings as well as their hemolytic activities are presented

Novel conopeptides of largely unexplored Indo Pacific <i>Conus</i> sp.

Cone snails are predatory creatures using venom as a weapon for prey capture and defense. Since this venom is neurotoxic, the venom gland is considered as an enormous collection of pharmacologically interesting compounds having a broad spectrum of targets. As such, cone snail peptides represent an interesting treasure for drug development. Here, we report five novel peptides isolated from the venom of Conus longurionis, Conus asiaticus and Conus australis. Lo6/7a and Lo6/7b were retrieved from C. longurionis and have a cysteine framework VI/VII. Lo6/7b has an exceptional amino acid sequence because no similar conopeptide has been described to date (similarity percentage C. asiaticus, has a typical framework III Cys arrangement, classifying the peptide in the M-superfamily. Asi14a, another peptide of C. asiaticus, belongs to framework XIV peptides and has a unique amino acid sequence. Finally, AusB is a novel conopeptide from C. australis. The peptide has only one disulfide bond, but is structurally very different as compared to other disulfide-poor peptides. The peptides were screened on nAChRs, NaV and KV channels depending on their cysteine framework and proposed classification. No targets could be attributed to the peptides, pointing to novel functionalities. Moreover, in the quest of identifying novel pharmacological targets, the peptides were tested for antagonistic activity against a broad panel of Gram-negative and Gram-positive bacteria, as well as two yeast strains

Vertical distribution of molluscs in the intertidal area in and around Mumbai, India

Vertical distribution of intertidal molluscs in and around Mumbai had been studied. Each species has an upper and lower limit of distribution along the vertical intertidal gradient and are concentrated at particular levels or zones where they find optimum living conditions. Zonation of the intertidal area with reference to molluscs at rocky shores of TIFR, Bandstand and NCPA has similarities. However, there is no similarity in zonation among rocky, sandy and muddy shores. Rocky intertidal zones are more diverse and dense in terms of molluscs. The mid and lower littoral zones have rich diversity. The upper littoral zone at some sites, especially Girgaon chowpatty is totally devoid of molluscs due to anthropogenic activities. Gafrarium divaricatum, Nerita oryzarum, N. polita and Neritina crepidularia have established themselves in all three marked zones, indicating their power to adjust with the wide fluctuations in surrounding environmental conditions

The CAP protein superfamily: function in sterol export and fungal virulence

CAP superfamily proteins, also known as sperm-coating proteins, are found in all kingdoms of life and have been implicated in a variety of physiological contexts, including immune defense in plants and mammals, sperm maturation and fertilization, fungal virulence, and toxicity of insect and reptile venoms as well as prostate and brain cancer. CAP family members are mostly secreted glycoproteins that are highly stable in the extracellular fluid. All members of the superfamily share a common CAP domain of approximately 150 amino acids, which adopts a unique α-β-α sandwich fold. The conserved structure suggests that CAP proteins exert fundamentally similar functions. However, the molecular mode of action of this protein family has remained enigmatic. The budding yeast Saccharomyces cerevisiae has three CAP family members designated Pry (pathogen related in yeast), and recent evidence indicates that they act as sterol-binding and export proteins. Expression of the mammalian CAP protein CRISP2, which binds sterols in vitro, complements the sterol export defect of a yeast pry mutant, suggesting that sterol binding and export is conserved among different CAP family members. Collectively, these observations suggest that CAP family members constitute a novel class of secreted extracellular sterol-binding proteins. A ligand-binding activity of the CAP domain could explain many of the biological activities attributed to these proteins. For example, the strong induction of plant pathogenesis-related 1 protein upon exposure to pathogens may serve to inhibit pathogen proliferation by extracting sterols from the pathogen membrane. Similarly, the presence of these proteins in the venom of toxic insects and reptiles or in the secretome of pathogenic fungi might inflict damage by sequestering sterols or related small hydrophobic compounds from the host tissu