Molecular diversity of spider venom

  title={Molecular diversity of spider venom},
  author={Alexander A. Vassilevski and Sergey A Kozlov and Eugene V. Grishin},
  journal={Biochemistry (Moscow)},
Spider venom, a factor that has played a decisive role in the evolution of one of the most successful groups of living organisms, is reviewed. Unique molecular diversity of venom components including substances of variable structure (from simple low molecular weight compounds to large multidomain proteins) with different functions is considered. Special attention is given to the structure, properties, and biosynthesis of toxins of polypeptide nature. 

Structural features of cysteine-rich polypeptides from sea anemone venoms

The known polypeptide toxins from the sea anemone venoms are considered in this review primarily in terms of their classification according to structural features, and the most outstanding functional features ofpolypeptides within each class were analyzed.

Main Components of Spider Venoms

The venoms from many mygalomorph species, containing several mini-proteins, a variety of low molecular mass compounds and enzymes, represent a very well-functioning and reliable mixture and may be seen as the basic form of spider venoms.

Applications of Spider Venom in Medical Science and Agriculture

The potential applications of spider venom as analgesics, anti-fungal, anti,parasitic and anti-bacterial agent, and bio-insecticides are encompassed.

Anticancer, antimicrobial, and analgesic activities of spider venoms.

This review will highlight the structures, activities and the possible mechanisms of action of spider venoms and their components against cancer, microbial infections, and pain.

Spider-Venom Peptides as Therapeutics

The structure and pharmacology of spider-venom peptides that are being used as leads for the development of therapeutics against a wide range of pathophysiological conditions including cardiovascular disorders, chronic pain, inflammation, and erectile dysfunction are reviewed.

Structural venomics: evolution of a complex chemical arsenal by massive duplication and neofunctionalization of a single ancestral fold

It is demonstrated that the lethal Australian funnel-web spider produces 33 superfamilies of venom peptides and proteins, more than described for any other arachnid, and that 15 of the 26 DRP superfam families form an ultra-stable inhibitor cystine knot motif.

Spider Venom Peptides for Gene Therapy of Chlamydia Infection

The venom of the ant spider Lachesana tarabaevi contains a wide variety of antimicrobial peptides, and six of them were tested for their ability to suppress Chlamydia trachomatis infection.

Spider venomics: implications for drug discovery.

This review describes recent advances in spider- venom-based drug discovery pipelines and discusses spider-venom-derived peptides that are currently under investigation for treatment of a diverse range of pathologies including pain, stroke and cancer.

Spider's venom phospholipases D: A structural review.




Polypeptide neurotoxins from spider venoms.

  • E. Grishin
  • Biology, Chemistry
    European journal of biochemistry
  • 1999
The structural and functional properties of spider polypeptide toxins are reviewed and high molecular mass toxic proteins was found in the venom of the spider genus Latrodectus, causing a massive transmitter release from a diversity of nerve endings.

Molecular diversification in spider venoms: A web of combinatorial peptide libraries

Gene duplication and focal hypermutation appear to be common mechanisms to venomous mollusks and spiders, leading to the pharmacologically complex cocktails used for predation and defense.

Pharmacology and biochemistry of spider venoms.

  • L. RashW. Hodgson
  • Biology, Chemistry
    Toxicon : official journal of the International Society on Toxinology
  • 2002

Therapeutic potential of venom peptides

The pharmacology of venom peptides is surveyed and their therapeutic prospects are assessed for the treatment of pain, diabetes, multiple sclerosis and cardiovascular diseases are assessed.

A rational nomenclature for naming peptide toxins from spiders and other venomous animals.

The anticoagulant action of phospholipase A from Eresus niger spider venom.

  • P. UsmanovF. Nuritova
  • Chemistry, Biology
    Toxicon : official journal of the International Society on Toxinology
  • 1994

Evolution of an Arsenal

Investigation of the timing of toxin recruitment events across the entire advanced snake radiation indicates that the evolution of advanced venom systems in three front-fanged lineages is associated with recruitment of new toxin types or explosive diversification of existing toxin types.