Cargando…

Comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites

BACKGROUND: The phylum Apicomplexa is an early-branching eukaryotic lineage that contains a number of important human and animal pathogens. Their complex life cycles and unique cytoskeletal features distinguish them from other model eukaryotes. Apicomplexans rely on actin-based motility for cell inv...

Descripción completa

Detalles Bibliográficos
Autores principales: Gordon, Jennifer L, Sibley, L David
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1334187/
https://www.ncbi.nlm.nih.gov/pubmed/16343347
http://dx.doi.org/10.1186/1471-2164-6-179
_version_ 1782126559756288000
author Gordon, Jennifer L
Sibley, L David
author_facet Gordon, Jennifer L
Sibley, L David
author_sort Gordon, Jennifer L
collection PubMed
description BACKGROUND: The phylum Apicomplexa is an early-branching eukaryotic lineage that contains a number of important human and animal pathogens. Their complex life cycles and unique cytoskeletal features distinguish them from other model eukaryotes. Apicomplexans rely on actin-based motility for cell invasion, yet the regulation of this system remains largely unknown. Consequently, we focused our efforts on identifying actin-related proteins in the recently completed genomes of Toxoplasma gondii, Plasmodium spp., Cryptosporidium spp., and Theileria spp. RESULTS: Comparative genomic and phylogenetic studies of apicomplexan genomes reveals that most contain only a single conventional actin and yet they each have 8–10 additional actin-related proteins. Among these are a highly conserved Arp1 protein (likely part of a conserved dynactin complex), and Arp4 and Arp6 homologues (subunits of the chromatin-remodeling machinery). In contrast, apicomplexans lack canonical Arp2 or Arp3 proteins, suggesting they lost the Arp2/3 actin polymerization complex on their evolutionary path towards intracellular parasitism. Seven of these actin-like proteins (ALPs) are novel to apicomplexans. They show no phylogenetic associations to the known Arp groups and likely serve functions specific to this important group of intracellular parasites. CONCLUSION: The large diversity of actin-like proteins in apicomplexans suggests that the actin protein family has diverged to fulfill various roles in the unique biology of intracellular parasites. Conserved Arps likely participate in vesicular transport and gene expression, while apicomplexan-specific ALPs may control unique biological traits such as actin-based gliding motility.
format Text
id pubmed-1334187
institution National Center for Biotechnology Information
language English
publishDate 2005
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-13341872006-01-19 Comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites Gordon, Jennifer L Sibley, L David BMC Genomics Research Article BACKGROUND: The phylum Apicomplexa is an early-branching eukaryotic lineage that contains a number of important human and animal pathogens. Their complex life cycles and unique cytoskeletal features distinguish them from other model eukaryotes. Apicomplexans rely on actin-based motility for cell invasion, yet the regulation of this system remains largely unknown. Consequently, we focused our efforts on identifying actin-related proteins in the recently completed genomes of Toxoplasma gondii, Plasmodium spp., Cryptosporidium spp., and Theileria spp. RESULTS: Comparative genomic and phylogenetic studies of apicomplexan genomes reveals that most contain only a single conventional actin and yet they each have 8–10 additional actin-related proteins. Among these are a highly conserved Arp1 protein (likely part of a conserved dynactin complex), and Arp4 and Arp6 homologues (subunits of the chromatin-remodeling machinery). In contrast, apicomplexans lack canonical Arp2 or Arp3 proteins, suggesting they lost the Arp2/3 actin polymerization complex on their evolutionary path towards intracellular parasitism. Seven of these actin-like proteins (ALPs) are novel to apicomplexans. They show no phylogenetic associations to the known Arp groups and likely serve functions specific to this important group of intracellular parasites. CONCLUSION: The large diversity of actin-like proteins in apicomplexans suggests that the actin protein family has diverged to fulfill various roles in the unique biology of intracellular parasites. Conserved Arps likely participate in vesicular transport and gene expression, while apicomplexan-specific ALPs may control unique biological traits such as actin-based gliding motility. BioMed Central 2005-12-12 /pmc/articles/PMC1334187/ /pubmed/16343347 http://dx.doi.org/10.1186/1471-2164-6-179 Text en Copyright © 2005 Gordon and Sibley; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Gordon, Jennifer L
Sibley, L David
Comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites
title Comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites
title_full Comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites
title_fullStr Comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites
title_full_unstemmed Comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites
title_short Comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites
title_sort comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1334187/
https://www.ncbi.nlm.nih.gov/pubmed/16343347
http://dx.doi.org/10.1186/1471-2164-6-179
work_keys_str_mv AT gordonjenniferl comparativegenomeanalysisrevealsaconservedfamilyofactinlikeproteinsinapicomplexanparasites
AT sibleyldavid comparativegenomeanalysisrevealsaconservedfamilyofactinlikeproteinsinapicomplexanparasites