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In this quantitative proteomics study we determined the variety and relative abundance of toxins present in enriched preparations of two nematocyst types isolated from the primary tentacles of the adult medusa stage of the hydrozoan Olindias sambaquiensis. The two nematocyst types were microbasic mastigophores and microbasic euryteles, and these were recovered from the macerated tentacle tissues by using a differential centrifugation approach. Soluble protein extracts from these nematocysts were tagged with tandem mass tag isobaric labels and putative toxins identified using tandem mass spectrometry coupled with a stringent bioinformatics annotation pipeline. Astonishingly, the venom composition of the two capsule types was nearly identical, and there was also little difference in the comparative abundance of toxins between the two nematocyst preparations. This homogeneity suggested that the same toxin complement was present regardless of the penetrative ability of the nematocyst type. Predicted toxin protein families that constituted the venom closely matched those of the toxic proteome of O. sambaquiensis published four years previously, suggesting that venom composition in this species changes little over time. Retaining an array of different nematocyst types to deliver a single venom, rather than sustaining the high metabolic cost necessary to maintain a dynamically evolving venom, may be more advantageous, given the vastly different interspecific interactions that adult medusa encounter in coastal zones., Introduction Venoms are composed of an assortment of peptides and proteins colloquially known as 'toxins.' Toxins are biosynthesized within specialized glands that are connected to dedicated anatomical structures, such as [...]

Antarctica poses numerous challenges to life such as cold shock, low nutrient concentrations, and periodic desiccation over a wide range of extreme temperatures. Cyanobacteria survive this harsh environment having evolved adaptive metabolic plasticity to become the dominant primary producers. The type strain cyanobacterium Halotia branconii CENA392 was isolated from an Antarctic intertidal seashore. The complete circular genome of this strain is presented herein, which was assembled using long‐sequence reads. The genome encoded some stress‐related genes associated with low‐temperature adaptation and biosynthesis of mycosporine‐like amino acid (MAA) photoprotective compounds. Empirical experimentation demonstrated constitutive production of the MAA porphyra‐334 and total carotenoids without exposure to low temperatures or ultraviolet radiation stress. Phylogenetic analysis provided insights on taxonomic placement and evolutionary history of some annotated genes. These data exemplify the importance of generating complete quality genome sequences of microorganisms isolated from extreme intertidal environments, facilitating in‐depth evaluation of ecological and taxonomic inferences. [ABSTRACT FROM AUTHOR]

Although most Myxozoa species of the genera Ceratomyxa and Ellipsomyxa have been described in marine hosts worldwide, an increasing diversity has been reported infecting South American freshwater fish, mainly in Amazonian waters. The present study deals with two species of myxozoan ceratomyxids parasitizing the gallbladder of Amazonian ornamental cichlids fish: Ceratomyxa amazonensis is identified from a new host—Geophagus altifrons; while Ellipsomyxa santarenensis n. sp. is described infecting Satanoperca jurupari. Morphological (light microscopy and transmission electron microscopy), molecular (small ribosomal subunit DNA—SSU-rDNA sequencing) and phylogenetic analyses were used to characterize both species. Ceratomyxa amazonensis showed a prevalence of 64.2%, with plasmodia showing a vermiform shape and motility. For E. santarenensis n. sp., the prevalence was 33.3%. Ultrastructural analysis revealed that the vermiform C. amazonensis plasmodia were composed of an outer cytoplasmic region and a large vacuole occupying the inner area. In E. santarenensis n. sp., cytoplasmic expansions were observed in pseudoplasmodia originating pseudopodia. SSU rDNA sequencing-based genetic distance analysis revealed a very small difference between C. amazonensis, parasite of G. altifrons, and C. amazonensis, parasite of S. discus—host of the original description, thus showing that they are the same species occurring in a new host. For Ellipsomyxa santarenensis n. sp., molecular data revealed a difference of 1.6% for Ellipsomyxa amazonensis and Ellipsomyxa paraensis. The phylogenetic analysis revealed the grouping of E. santarenensis n. sp. together with the other freshwater Ellipsomyxa species of the Amazonian region, and associated with the morphological data, it was possible to identify it as a new taxon within the genus Ellipsomyxa. [ABSTRACT FROM AUTHOR]

Asparaginases (ASNases) are a large and structurally diverse group of enzymes ubiquitous amongst archaea, bacteria and eukaryotes, that catalyze hydrolysis of asparagine to aspartate and ammonia. Bacterial ASNases are important biopharmaceuticals for the treatment of acute lymphoblastic leukemia, although some patients experience adverse allergic side effects during treatment with these protein therapeutics. ASNases are currently divided into three families: plant‐type ASNases, Rhizobium etli‐type ASNases and bacterial‐type ASNases. This system is outdated as both bacterial‐type and plant‐type families also include archaeal, bacterial and eukaryotic enzymes, each with their own distinct characteristics. Herein, phylogenetic studies allied to tertiary structural analyses are described with the aim of proposing a revised and more robust classification system that considers the biochemical diversity of ASNases. Accordingly, based on distinct peptide domains, phylogenetic data, structural analysis and functional characteristics, we recommend that ASNases now be divided into three new distinct classes containing subgroups according to structural and functional aspects. Using this new classification scheme, 25 ASNases were identified as candidates for future new lead discovery. [ABSTRACT FROM AUTHOR]

An element of aromatic polyketide synthases (PKS), previously called 'chain-length factor' (CLF), has been shown to be a factor needed for polyketide chain initiation. This factor has decarboxylase activity towards malonyl-acyl carrier protein. The discovery of the common function of CLF and KSQ, a domain of previously unknown function which acts like CLF, as chain initiation factors supplies a further significant mechanistic connection between type I and type II PKSs and between PKSs and fatty-acid synthases.