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Veterinary parasitology2008; 154(1-2); 82-93; doi: 10.1016/j.vetpar.2007.12.037

Identification of a LIM domain-containing gene in the Cyathostominae.

Abstract: The Cyathostominae are a complex group of nematodes and are the primary parasitic pathogens of horses. Little is known of their basic biology. As part of an investigation into mechanisms involved in reactivation of mucosal larval stages, we identified a gene encoding a predicted LIM domain-containing protein (Cy-LIM-1). LIM domains are cysteine- and histidine-rich motifs that are thought to direct protein-protein interactions. Proteins that contain these domains have a wide range of functions including gene regulation, cell fate determination and cytoskeleton organization. The Cy-lim-1 mRNA was identified as an abundant transcript following differential display-arbitrary primed reverse transcriptase-polymerase chain reaction amplification of RNA from faecal fourth stage larvae (FL4), which had been obtained from the diarrhoea of clinical cases of larval cyathostominosis. Detailed analysis showed that Cy-lim-1 was transcribed in FL4 and in other developmental stages; however there were differences in transcription of alternatively spliced variants amongst the stages. The predicted peptide sequence of Cy-lim-1 showed high identity to two LIM domain-containing proteins from Caenorhabditis elegans. RT-PCR analysis of these Cy-lim-1 homologues in C. elegans indicated that the two genes, which are described as separate entities in GenBank, are likely to compose a single gene of which alternative splice variants are transcribed. The LIM proteins from the cyathostomins and C. elegans were classified as LIM-only (LMO) proteins and, along with LMO proteins identified in sequence databases of other nematodes, comprise a group of LIM proteins distinct to those defined in other organisms.
Publication Date: 2008-03-04 PubMed ID: 18406533DOI: 10.1016/j.vetpar.2007.12.037Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The study identifies a gene in nematodes (a type of worm) that is thought to be involved in a variety of biological functions like regulating genes, determining cell fate, and organizing the cell structure. This gene is abundant in a particular developmental stage of the worm that has been identified as a key parasite affecting horses.

Study Overview and Purpose

  • This research focuses on Cyathostominae, a type of nematode or worm that is a significant parasite in horses. The specific biology and understanding of these nematodes is currently limited.
  • The purpose of this study was to investigate the mechanisms involved in the reactivation of larval stages in the mucus linings, especially the fourth stage larvae (FL4) often found in horse diarrhoea during clinical cases of larval cyathostominosis, a dangerous equine disease.

Key Findings

  • The researchers identified a gene encoding a LIM domain-containing protein, termed Cy-LIM-1. LIM domains are rich in cysteine and histidine and thought to direct protein-protein interactions. These proteins have numerous functions ranging from gene regulation to determinations of cell fate and organization of the cell’s structural framework or cytoskeleton.
  • The Cy-lim-1 mRNA was found to be an abundant transcript following a sophisticated RNA amplification process from fecal fourth stage larvae (FL4).
  • Detailed examination revealed that Cy-lim-1 was transcribed in FL4 and other developmental stages, but there were variations in transcription of alternatively spliced variants, meaning different forms of the gene were expressed at different stages.

Comparative Analysis

  • The predicted sequence of Cy-lim-1 showed high similarity to two LIM domain-containing proteins in the nematode species Caenorhabditis elegans. Reverse transcriptase PCR analysis of these Cy-lim-1 homologues in C. elegans suggested that the two genes, currently separately documented in genetic databases, may actually represent a single gene from which alternative splice variants are transcribed.
  • The LIM proteins from the cyathostomins and C. elegans were grouped as LIM-only (LMO) proteins and are a class of LIM proteins distinct from those found in other organisms.

Research Significance

  • This identification of Cy-lim-1 gene in a nematode species that infect horses could help to get a better understanding of the biology of these parasites.
  • Further research on how this gene functions in the nematodes’ life cycle, and how it reactivates the larvae in horses, could lead to improved treatments for common parasitic infections in horses.

Cite This Article

APA
Matthews JB, Johnson DR, Lazari O, Craig R, Matthews KR. (2008). Identification of a LIM domain-containing gene in the Cyathostominae. Vet Parasitol, 154(1-2), 82-93. https://doi.org/10.1016/j.vetpar.2007.12.037

Publication

ISSN: 0304-4017
NlmUniqueID: 7602745
Country: Netherlands
Language: English
Volume: 154
Issue: 1-2
Pages: 82-93

Researcher Affiliations

Matthews, Jacqueline B
  • Division of Parasitology, Moredun Research Institute, Midlothian, Scotland EH26 0PZ, UK. jacqui.matthews@moredun.ac.uk
Johnson, Deborah R
    Lazari, Ovadia
      Craig, Randa
        Matthews, Keith R

          MeSH Terms

          • Amino Acid Sequence
          • Animals
          • DNA, Complementary / genetics
          • DNA, Helminth / genetics
          • DNA-Binding Proteins / chemistry
          • DNA-Binding Proteins / genetics
          • DNA-Binding Proteins / metabolism
          • Genes, Helminth
          • Helminth Proteins / genetics
          • Helminth Proteins / metabolism
          • Homeodomain Proteins / chemistry
          • Homeodomain Proteins / genetics
          • Homeodomain Proteins / metabolism
          • Models, Molecular
          • Molecular Sequence Data
          • Nematoda / genetics
          • Protein Conformation
          • Transcription, Genetic

          Citations

          This article has been cited 1 times.
          1. Sang M, Ma L, Sang M, Zhou X, Gao W, Geng C. LIM-domain-only proteins: multifunctional nuclear transcription coregulators that interacts with diverse proteins. Mol Biol Rep 2014 Feb;41(2):1067-73.
            doi: 10.1007/s11033-013-2952-1pubmed: 24379077google scholar: lookup