Sphingomyelinase D from venoms of Loxosceles spiders

Evolutionary insights from cDNA sequences and gene structure

Greta J. Binford, Matthew Hj Cordes, Michael A. Wells

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

Loxosceles spider venoms cause dermonecrosis in mammalian tissues. The toxin sphingomyelinase D (SMaseD) is a sufficient causative agent in lesion formation and is only known in these spiders and a few pathogenic bacteria. Similarities between spider and bacterial SMaseD in molecular weights, pIs and N-terminal amino acid sequence suggest an evolutionary relationship between these molecules. We report three cDNA sequences from venom-expressed mRNAs, analyses of amino acid sequences, and partial characterization of gene structure of SMaseD homologs from Loxosceles arizonica with the goal of better understanding the evolution of this toxin. Sequence analyses indicate SMaseD is a single domain protein and a divergent member of the ubitiquous, broadly conserved glycerophosphoryl diester phosphodiesterase family (GDPD). Bacterial SMaseDs are not identifiable as homologs of spider SMaseD or GDPD family members. Amino acid sequence similarities do not afford clear distinction between independent origin of toxic SMaseD activity in spiders and bacteria and origin in one lineage by ancient horizontal transfer from the other. The SMaseD genes span at least 6500 bp and contain at least 5 introns. Together, these data indicate L. arizonica SMaseD has been evolving within a eukaryotic genome for a long time ruling out origin by recent transfer from bacteria.

Original languageEnglish (US)
Pages (from-to)547-560
Number of pages14
JournalToxicon
Volume45
Issue number5
DOIs
StatePublished - Apr 2005

Fingerprint

Spider Venoms
Complementary DNA
Genes
Spiders
Bacteria
Phosphoric Diester Hydrolases
Amino Acids
Amino Acid Sequence
loxosceles venom
sphingomyelin phosphodiesterase D
Poisons
Protein Sequence Analysis
Venoms
Introns
Sequence Analysis
Molecular Weight
Molecular weight
Genome
Tissue
Messenger RNA

Keywords

  • Concerted evolution
  • Corynebacteria
  • Horizontal transfer
  • Loxosceles
  • Venom

ASJC Scopus subject areas

  • Toxicology

Cite this

Sphingomyelinase D from venoms of Loxosceles spiders : Evolutionary insights from cDNA sequences and gene structure. / Binford, Greta J.; Cordes, Matthew Hj; Wells, Michael A.

In: Toxicon, Vol. 45, No. 5, 04.2005, p. 547-560.

Research output: Contribution to journalArticle

@article{8dd180e04c4648a98434d30a70220738,
title = "Sphingomyelinase D from venoms of Loxosceles spiders: Evolutionary insights from cDNA sequences and gene structure",
abstract = "Loxosceles spider venoms cause dermonecrosis in mammalian tissues. The toxin sphingomyelinase D (SMaseD) is a sufficient causative agent in lesion formation and is only known in these spiders and a few pathogenic bacteria. Similarities between spider and bacterial SMaseD in molecular weights, pIs and N-terminal amino acid sequence suggest an evolutionary relationship between these molecules. We report three cDNA sequences from venom-expressed mRNAs, analyses of amino acid sequences, and partial characterization of gene structure of SMaseD homologs from Loxosceles arizonica with the goal of better understanding the evolution of this toxin. Sequence analyses indicate SMaseD is a single domain protein and a divergent member of the ubitiquous, broadly conserved glycerophosphoryl diester phosphodiesterase family (GDPD). Bacterial SMaseDs are not identifiable as homologs of spider SMaseD or GDPD family members. Amino acid sequence similarities do not afford clear distinction between independent origin of toxic SMaseD activity in spiders and bacteria and origin in one lineage by ancient horizontal transfer from the other. The SMaseD genes span at least 6500 bp and contain at least 5 introns. Together, these data indicate L. arizonica SMaseD has been evolving within a eukaryotic genome for a long time ruling out origin by recent transfer from bacteria.",
keywords = "Concerted evolution, Corynebacteria, Horizontal transfer, Loxosceles, Venom",
author = "Binford, {Greta J.} and Cordes, {Matthew Hj} and Wells, {Michael A.}",
year = "2005",
month = "4",
doi = "10.1016/j.toxicon.2004.11.011",
language = "English (US)",
volume = "45",
pages = "547--560",
journal = "Toxicon",
issn = "0041-0101",
publisher = "Elsevier Limited",
number = "5",

}

TY - JOUR

T1 - Sphingomyelinase D from venoms of Loxosceles spiders

T2 - Evolutionary insights from cDNA sequences and gene structure

AU - Binford, Greta J.

AU - Cordes, Matthew Hj

AU - Wells, Michael A.

PY - 2005/4

Y1 - 2005/4

N2 - Loxosceles spider venoms cause dermonecrosis in mammalian tissues. The toxin sphingomyelinase D (SMaseD) is a sufficient causative agent in lesion formation and is only known in these spiders and a few pathogenic bacteria. Similarities between spider and bacterial SMaseD in molecular weights, pIs and N-terminal amino acid sequence suggest an evolutionary relationship between these molecules. We report three cDNA sequences from venom-expressed mRNAs, analyses of amino acid sequences, and partial characterization of gene structure of SMaseD homologs from Loxosceles arizonica with the goal of better understanding the evolution of this toxin. Sequence analyses indicate SMaseD is a single domain protein and a divergent member of the ubitiquous, broadly conserved glycerophosphoryl diester phosphodiesterase family (GDPD). Bacterial SMaseDs are not identifiable as homologs of spider SMaseD or GDPD family members. Amino acid sequence similarities do not afford clear distinction between independent origin of toxic SMaseD activity in spiders and bacteria and origin in one lineage by ancient horizontal transfer from the other. The SMaseD genes span at least 6500 bp and contain at least 5 introns. Together, these data indicate L. arizonica SMaseD has been evolving within a eukaryotic genome for a long time ruling out origin by recent transfer from bacteria.

AB - Loxosceles spider venoms cause dermonecrosis in mammalian tissues. The toxin sphingomyelinase D (SMaseD) is a sufficient causative agent in lesion formation and is only known in these spiders and a few pathogenic bacteria. Similarities between spider and bacterial SMaseD in molecular weights, pIs and N-terminal amino acid sequence suggest an evolutionary relationship between these molecules. We report three cDNA sequences from venom-expressed mRNAs, analyses of amino acid sequences, and partial characterization of gene structure of SMaseD homologs from Loxosceles arizonica with the goal of better understanding the evolution of this toxin. Sequence analyses indicate SMaseD is a single domain protein and a divergent member of the ubitiquous, broadly conserved glycerophosphoryl diester phosphodiesterase family (GDPD). Bacterial SMaseDs are not identifiable as homologs of spider SMaseD or GDPD family members. Amino acid sequence similarities do not afford clear distinction between independent origin of toxic SMaseD activity in spiders and bacteria and origin in one lineage by ancient horizontal transfer from the other. The SMaseD genes span at least 6500 bp and contain at least 5 introns. Together, these data indicate L. arizonica SMaseD has been evolving within a eukaryotic genome for a long time ruling out origin by recent transfer from bacteria.

KW - Concerted evolution

KW - Corynebacteria

KW - Horizontal transfer

KW - Loxosceles

KW - Venom

UR - http://www.scopus.com/inward/record.url?scp=15044352365&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=15044352365&partnerID=8YFLogxK

U2 - 10.1016/j.toxicon.2004.11.011

DO - 10.1016/j.toxicon.2004.11.011

M3 - Article

VL - 45

SP - 547

EP - 560

JO - Toxicon

JF - Toxicon

SN - 0041-0101

IS - 5

ER -