Abstract

This review gives an overview on the development of research on spider venoms with a focus on structure and function of venom components and techniques of analysis. Major venom component groups are small molecular mass compounds, antimicrobial (also called cytolytic, or cationic) peptides (only in some spider families), cysteine-rich (neurotoxic) peptides, and enzymes and proteins. Cysteine-rich peptides are reviewed with respect to various structural motifs, their targets (ion channels, membrane receptors), nomenclature, and molecular binding. We further describe the latest findings concerning the maturation of antimicrobial, and cysteine-rich peptides that are in most known cases expressed as propeptide-containing precursors. Today, venom research, increasingly employs transcriptomic and mass spectrometric techniques. Pros and cons of venom gland transcriptome analysis with Sanger, 454, and Illumina sequencing are discussed and an overview on so far published transcriptome studies is given. In this respect, we also discuss the only recently described cross contamination arising from multiplexing in Illumina sequencing and its possible impacts on venom studies. High throughput mass spectrometric analysis of venom proteomes (bottom-up, top-down) are reviewed.

Highlights

  • Many animal lineages independently developed toxic secretions

  • These adapters can lead to extension of library fragments with the wrong index adapter, an effect which is bigger if cluster generation is achieved via ExAmp chemistry used for patterned flow cells, as used for HiSeqX, HiSeq

  • inductive coupled plasma (ICP)-MS based quantification of venom proteins may provide a promising tool for further venomic studies, but it reveals a major challenge ahead because the full separation of proteoforms prior to mass spectrometry is a prerequisite for ICP-MS based quantification [277]

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Summary

Introduction

Many animal lineages independently developed toxic secretions Such secretions can be either deployed through direct contact or ingestion (poison), or through a wound by stingers, teeth, fangs, harpoons, or other specialized tools (venoms) [1]. Potential threats to primates is seen as the main reason for the long-lasting fascination of humans towards venomous animals [5]. Humans started to use animal venoms for their benefit. Venom components are increasingly used in research of their biological targets (e.g., ion channels) [11], and venoms of imminent danger to humans are studied for development of envenoming therapies [12]. Venoms of animals preying on insects are studied for development of insecticides [13]. Spider venom has for a long time received only small attention due to its limited impact on human health. We review the state of the art of the composition of spider venoms and the currently available methods to analyze it

Spider Venom
Small Molecular Mass Compounds
Antimicrobial Peptides
Cysteine-Rich Peptides
Structural Motifs
Targets of Neurotoxic Peptides
Nomenclature of Toxins
Molecular Binding of Neurotoxins
Modular
Enzymes and Proteins
Spider Venom Peptide Precursors and Their Maturing
Comparison of Protease Cleavage Motifs to Motifs of Other Organisms
Cleavage for Heterodimerization of Spider Toxins
Concluding Remarks on Venom Components and Their Toxic Action
Analysis of Venom Components
Venom Gland Transcriptome Analysis
Sequencing Method
47 Isolation of Sequences Based on
Identification of Toxin-Like Transcripts
Recent Developments in Sequencing Techniques
Cross Contamination among Multiplexed Samples in Illumina Sequencing
High Throughput Mass Spectrometric Analysis of the Venom Proteoms
Bottom-Up Proteomics
Top-Down Proteomics
Annotation of Spider Venom Toxins
Concluding Remarks on the Analysis of Venom Components
Findings
Freeman
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