Molecular data reveal cryptic speciation and host specificity in Toxascaris leonina (Nematoda: Ascarididae).
Animals
Cyclooxygenase 1
/ genetics
DNA Barcoding, Taxonomic
DNA, Intergenic
/ genetics
Dogs
/ parasitology
Felidae
/ parasitology
Foxes
/ parasitology
Genetic Speciation
Host Specificity
/ genetics
NADH Dehydrogenase
/ genetics
Phylogeny
Toxascariasis
/ parasitology
Toxascaris
/ classification
Wolves
/ parasitology
Barcode gap
Cryptic-species
ITS1
Toxascaris leonina
cox1
nad1
Journal
Veterinary parasitology
ISSN: 1873-2550
Titre abrégé: Vet Parasitol
Pays: Netherlands
ID NLM: 7602745
Informations de publication
Date de publication:
Feb 2019
Feb 2019
Historique:
received:
10
10
2018
revised:
04
01
2019
accepted:
05
01
2019
entrez:
10
2
2019
pubmed:
10
2
2019
medline:
12
4
2019
Statut:
ppublish
Résumé
Toxascaris leonina (Ascarididae) is a cosmopolitan and polyxenical parasite whose host are canids and felids. To date, molecular phylogenetic studies included toxascarid representatives collected only from dogs or felids, therefore the intra-species differences between T. leonina collected from different host species has not been noticed. In this paper, we test the hypothesis of cryptic speciation in the T. leonina complex based on extended sequence data (ITS1, nad1, cox1) and individuals collected from dogs, felids and foxes. Phylogenetic analysis clustered T. leonina representatives into three well-supported clades depending on their host species, i.e. dogs and wolves, wild felids and foxes. Both genetic distances and the barcoding-gap analysis strongly support the species status of populations inhabiting different hosts. The results suggest additional genetic separation in felids. However, to determine the actual size of the Toxascaris complex, it would be necessary to analyse individuals collected from other canid and felid Toxascaris leonina host species.
Identifiants
pubmed: 30736952
pii: S0304-4017(19)30020-2
doi: 10.1016/j.vetpar.2019.01.002
pii:
doi:
Substances chimiques
DNA, Intergenic
0
Cyclooxygenase 1
EC 1.14.99.1
NADH Dehydrogenase
EC 1.6.99.3
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
80-83Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.