scholarly journals Diverse Cone-Snail Species Harbor Closely Related Streptomyces Species with Conserved Chemical and Genetic Profiles, Including Polycyclic Tetramic Acid Macrolactams

2017 ◽  
Vol 8 ◽  
Author(s):  
Michelle Quezada ◽  
Cuauhtemoc Licona-Cassani ◽  
Pablo Cruz-Morales ◽  
Angela A. Salim ◽  
Esteban Marcellin ◽  
...  
Marine Drugs ◽  
2020 ◽  
Vol 18 (9) ◽  
pp. 464
Author(s):  
Xinjia Li ◽  
Wanyi Chen ◽  
Dongting Zhangsun ◽  
Sulan Luo

The venom of various Conus species is composed of a rich variety of unique bioactive peptides, commonly referred to as conotoxins (conopeptides). Most conopeptides have specific receptors or ion channels as physiologically relevant targets. In this paper, high-throughput transcriptome sequencing was performed to analyze putative conotoxin transcripts from the venom duct of a vermivorous cone snail species, Conus litteratus native to the South China Sea. A total of 128 putative conotoxins were identified, most of them belonging to 22 known superfamilies, with 43 conotoxins being regarded as belonging to new superfamilies. Notably, the M superfamily was the most abundant in conotoxins among the known superfamilies. A total of 15 known cysteine frameworks were also described. The largest proportion of cysteine frameworks were VI/VII (C-C-CC-C-C), IX (C-C-C-C-C-C) and XIV (C-C-C-C). In addition, five novel cysteine patterns were also discovered. Simple sequence repeat detection results showed that di-nucleotide was the major type of repetition, and the codon usage bias results indicated that the codon usage bias of the conotoxin genes was weak, but the M, O1, O2 superfamilies differed in codon preference. Gene cloning indicated that there was no intron in conotoxins of the B1- or J superfamily, one intron with 1273–1339 bp existed in a mature region of the F superfamily, which is different from the previously reported gene structure of conotoxins from other superfamilies. This study will enhance our understanding of conotoxin diversity, and the new conotoxins discovered in this paper will provide more potential candidates for the development of pharmacological probes and marine peptide drugs.


Marine Drugs ◽  
2020 ◽  
Vol 18 (3) ◽  
pp. 135 ◽  
Author(s):  
Xiujie Liu ◽  
Ge Yao ◽  
Kang Wang ◽  
Yanli Liu ◽  
Xiukun Wan ◽  
...  

Conotoxin-Ac1 and its variant conotoxin-Ac1-O6P, were isolated from the venom duct of Conus achatinus, a fish-hunting cone snail species collected in the Sea of Hainan, China. Conotoxin-Ac1 is linear peptide that contain 15 amino acids. In the present study, we synthesized and structurally and functionally characterized conotoxin-Ac1 as well as 19 variants. Electrophysiological results showed that conotoxin-Ac1 inhibited N-methyl-D-aspartate receptor subunit 2B (NR2B) with an IC50 of 8.22 ± 0.022 μM. Further structure-activity studies of conotoxin-Ac demonstrated that polar amino acid residues were important for modulating its active, and the replacement of N1, O9, E10, and S12 by Ala resulted in a significant decrease in potency to NR2B. °Furthermore, conotoxin-Ac1 and conotoxin-Ac1-O6P were tested in hot-plate and tail-flick assays to measure the potential analgesic activity to an acute thermal stimulus in a dose-dependent manner. Subsequently, the analgesic activity of conotoxin-Ac1 mutants was analyzed by the hot-plate method. The results show that N1, Y2, Y3, E10, N11, S12, and T15 play an important role in the analgesic activity of conotoxin-Ac1. N1 and S12 have significant effects on conotoxin-Ac1 in inhibiting NR2B and analgesic activity. In conclusion, we have discovered that conotoxin-Ac1 is an inhibitor of NMDAR and displays antinociceptive activity.


Author(s):  
Moustafa Sarhan ◽  
Mohammed Abdel-Wahab ◽  
Hamdy Aly ◽  
Maged Fouda

2018 ◽  
Vol 92 (5) ◽  
pp. 804-837 ◽  
Author(s):  
Jonathan R. Hendricks

AbstractExtant members of the neogastropod family Conidae (cone snails) are renowned for their often dazzling shell coloration patterns and venomous feeding habits. Many cone snail species have also been described from the fossil record, but to date have been little used to understand the evolutionary history of extant clades. The cone snail fauna of the Miocene Gatun Formation of Colón Province, Panama is especially important for understanding the temporal and biogeographic history of tropical American Conidae. Intensive, focused collecting from an exposure of the lower Gatun Formation (deposited ca. 11–10 Ma) resulted in the discovery of nearly 900 specimens of Conidae. Remarkably, many of these well-preserved specimens exhibit revealed coloration patterns when exposed to ultraviolet light. The fluorescing coloration patterns were used in conjunction with other features of shell morphology to differentiate species and, in most cases, evaluate their potential relationships to members of the extant tropical American fauna. Nine species are fully described from this locality, one of which is recognized as new:Conus(Stephanoconus)woodringin. sp. At least one, and perhaps more, additional Conidae species are also present at the study locality. The diversity of this Conidae fauna is considered moderate relative to other recently analyzed tropical American fossil assemblages. The phylogenetic diversity of the assemblage, however, is noteworthy: six of the ten species can be confidently assigned to six different clades of extant Conidae, providing potentially useful calibration points for future phylogenetic studies.http://zoobank.org/8fe00c31-8f3f-4514-85af-29068e468cd3


2017 ◽  
Vol 114 (17) ◽  
pp. E3507-E3515 ◽  
Author(s):  
Catharina Reimers ◽  
Cheng-Han Lee ◽  
Hubert Kalbacher ◽  
Yuemin Tian ◽  
Chih-Hsien Hung ◽  
...  

Acid-sensing ion channels (ASICs) are proton-gated Na+ channels that are expressed throughout the nervous system. ASICs have been implicated in several neuronal disorders, like ischemic stroke, neuronal inflammation, and pathological pain. Several toxins from venomous animals have been identified that target ASICs with high specificity and potency. These toxins are extremely useful in providing protein pharmacophores and to characterize function and structure of ASICs. Marine cone snails contain a high diversity of toxins in their venom such as conotoxins, which are short polypeptides stabilized by disulfide bonds, and conopeptides, which have no or only one disulfide bond. Whereas conotoxins selectively target specific neuronal proteins, mainly ion channels, the targets of conopeptides are less well known. Here, we perform an in vitro screen of venoms from 18 cone snail species to identify toxins targeting ASICs. We identified a small conopeptide of only four amino acids from the venom of Conus textile that strongly potentiated currents of ASIC3, which has a specific role in the pain pathway. This peptide, RPRFamide, belongs to the subgroup of cono-RFamides. Electrophysiological characterization of isolated dorsal root ganglion (DRG) neurons revealed that RPRFamide increases their excitability. Moreover, injection of the peptide into the gastrocnemius muscle strongly enhanced acid-induced muscle pain in mice that was abolished by genetic inactivation of ASIC3. In summary, we identified a conopeptide that targets the nociceptor-specific ion channel ASIC3.


Toxicon ◽  
2013 ◽  
Vol 65 ◽  
pp. 59-67 ◽  
Author(s):  
Carolina Möller ◽  
Nicole Vanderweit ◽  
José Bubis ◽  
Frank Marí

2016 ◽  
Vol 16 (2) ◽  
pp. 763-772 ◽  
Author(s):  
Marimuthu Vijayasarathy ◽  
Soorej M. Basheer ◽  
Jayaseelan Benjamin Franklin ◽  
Padmanabhan Balaram

2017 ◽  
Vol 83 (23) ◽  
Author(s):  
Joshua P. Torres ◽  
Maria Diarey Tianero ◽  
Jose Miguel D. Robes ◽  
Jason C. Kwan ◽  
Jason S. Biggs ◽  
...  

ABSTRACT Cone snails are biomedically important sources of peptide drugs, but it is not known whether snail-associated bacteria affect venom chemistry. To begin to answer this question, we performed 16S rRNA gene amplicon sequencing of eight cone snail species, comparing their microbiomes with each other and with those from a variety of other marine invertebrates. We show that the cone snail microbiome is distinct from those in other marine invertebrates and conserved in specimens from around the world, including the Philippines, Guam, California, and Florida. We found that all venom ducts examined contain diverse 16S rRNA gene sequences bearing closest similarity to Stenotrophomonas bacteria. These sequences represent specific symbionts that live in the lumen of the venom duct, where bioactive venom peptides are synthesized. IMPORTANCE In animals, symbiotic bacteria contribute critically to metabolism. Cone snails are renowned for the production of venoms that are used as medicines and as probes for biological study. In principle, symbiotic bacterial metabolism could either degrade or synthesize active venom components, and previous publications show that bacteria do indeed contribute small molecules to some venoms. Therefore, understanding symbiosis in cone snails will contribute to further drug discovery efforts. Here, we describe an unexpected, specific symbiosis between bacteria and cone snails from around the world.


2007 ◽  
Vol 404 (3) ◽  
pp. 413-419 ◽  
Author(s):  
Carolina Möller ◽  
Frank Marí

Vasopressins and oxytocins are homologous, ubiquitous and multifunctional peptides present in animals. Conopressins are vasopressin/oxytocin-related peptides that have been found in the venom of cone snails, a genus of marine predatory molluscs that envenom their prey with a complex mixture of neuroactive peptides. In the present paper, we report the purification and characterization of a unique conopressin isolated from the venom of Conus villepinii, a vermivorous cone snail species from the western Atlantic Ocean. This novel peptide, designated γ-conopressin-vil, has the sequence CLIQDCPγG* (γ is γ-carboxyglutamate and * is C-terminal amidation). The unique feature of this vasopressin/oxytocin-like peptide is that the eighth residue is γ-carboxyglutamate instead of a neutral or basic residue; therefore it could not be directly classified into either the vasopressin or the oxytocin peptide families. Nano-NMR spectroscopy of the peptide isolated directly from the cone snails revealed that the native γ-conopressin-vil undergoes structural changes in the presence of calcium. This suggests that the peptide binds calcium, and the calcium-binding process is mediated by the γ-carboxyglutamate residue. However, the negatively charged residues in the sequence of γ-conopressin-vil may mediate calcium binding by a novel mechanism not observed in other peptides of this family.


Author(s):  
Vidyasagar G M ◽  
Shankaravva B ◽  
R Begum ◽  
Imrose ◽  
Sagar R ◽  
...  

Microorganisms like fungi, actinomycetes and bacteria are considered nanofactories and are helpful in the production of nanoparticles useful in the welfare of human beings. In the present study, we investigated the production of silver nanoparticles from Streptomyces species JF714876. Extracellular synthesis of silver nanoparticles by Streptomyces species was carried out using two different media. Silver nanoparticles were examined using UV-visible, IR and atomic force microscopy. The size of silver nanoparticles was in the range of 80-100 nm. Antimicrobial activity of silver nanoparticle against bacteria such as E. coli, S. aureus, and dermatophytes like T. rubrum and T. tonsurans was determined. Thus, this study suggests that the Streptomyces sp. JF741876 can produce silver ions that can be used as an antimicrobial substance.


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