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At least 1,459 records · Page 81Linked to original sources
PubMed1999

The relationship of Hammondia hammondi and Sarcocystis mucosa to other heteroxenous cyst-forming coccidia as inferred by phylogenetic analysis of the 18S SSU ribosomal DNA sequence.

The complete sequence of the 18S small subunit (SSU) ribosomal DNA of Hammondia hammondi and Sarcocystis mucosa was obtained and compared to SSU rDNA sequences of Neospora caninum, Toxoplasma gondii, Besnoitia besnoiti, 2 species of Frenkelia, 3 species of Isospora, and 13 species of Sarcocystis. Analyses showed that H. hammondi and T. gondii are monophyletic and that these taxa shared a common ancestor with N. caninum and B. besnoiti. The weight of evidence shows that S. mucosa, S. neurona, and Frenkelia species form a clade thereby supporting the conclusion that Sarcocystis is paraphyletic.

Animals↗
PubMed1999

Discrimination between two Perkinsus spp. isolated from the softshell clam, Mya arenaria, by sequence analysis of two internal transcribed spacer regions and the 5.8S ribosomal RNA gene.

The internal transcribed spacer (ITS-1 and ITS-2) regions and the 5.8S ribosomal RNA gene of 2 Perkinsus spp. (G117 and H49) originating from the softshell clam, Mya arenaria, of the Chesapeake Bay were cloned and sequenced to obtain evidence for their genetic divergence. A high level of heterogeneity in both regions, probably resulting from deletions, insertions, and base substitutions, was evident from alignments of the sequences of the 2 isolates with published sequences of other Perkinsus spp. The isolate G117 and other Perkinsus spp. were highly divergent (13-26% and 19-20% sequence divergence in ITS-1 and ITS-2, respectively). These regions in the isolate H49 and Perkinsus marinus were similar (99.07% and 99% for ITS-1 and ITS-2, respectively). Evidence obtained from a phylogenetic analysis using the aligned sequences suggests that G117 and H49 belong to 2 distinct species of Perkinsus. The isolate G117 possibly belongs to an as yet undescribed species of Perkinsus, and H49 belongs to the species P. marinus. The conclusions drawn from the genetic analysis of H49 and G117 are supported by previously reported morphological characteristics (McLaughlin & Faisal, 1998b). Isolates H49 and G117 originated from the same molluscan species demonstrating that at least 2 different species of Perkinsus can co-exist in 1 host.

Animals↗
PubMed2004

Studying the cell biology of apicomplexan parasites using fluorescent proteins.

The ability to transfect Apicomplexan parasites has revolutionized the study of this important group of pathogens. The function of specific genes can be explored by disruption of the locus or more subtly by introduction of altered or tagged versions. Using the transgenic reporter gene green fluorescent protein (GFP), cell biological processes can now be studied in living parasites and in real time. We review recent advances made using GFP-based experiments in the understanding of protein trafficking, organelle biogenesis, and cell division in Toxoplasma gondii and Plasmodium falciparum. A technical section provides a collection of basic experimental protocols for fluorescent protein expression in T. gondii. The combination of the in vivo marker GFP with an increasingly diverse genetic toolbox for T. gondii opens many exciting experimental opportunities, and emerging applications of GFP in genetic and pharmacological screens are discussed.

Animals↗
PubMed1981

In vitro activity of 2-alkyl-3-hydroxy-1,4-naphthoquinones against Theileria parva.

A variety of naphthoquinones have veen prepared and evaluated in vitro against the causative agent of the cattle disease East Coast Fever-Theileria parva infection. It is concluded from structure-activity studies that a 2-hydroxyl moiety es essential for high activity. The most active compounds tested were 2-hydroxy-3-alkyl-1,4-naphthoquinones in which the alkyl moiety was cyclohexyl, cyclohexylcyclohexyl, tridecyl, or tetradecyl.

Animals↗
PubMed2006

Binding and interaction of dinitroanilines with apicomplexan and kinetoplastid alpha-tubulin.

Despite years of use as commercial herbicides, it is still unclear how dinitroanilines interact with tubulin, how they cause microtubule disassembly, and why they are selectively active against plant and protozoan tubulin. In this work, through a series of computational studies, a common binding site of oryzalin, trifluralin, and GB-II-5 on apicomplexan and kinetoplastid alpha-tubulin is proposed. Furthermore, to investigate how dinitroanilines affect tubulin dynamics, molecular dynamics simulations of Leishmania alpha-tubulin with and without a bound dinitroaniline are performed. The results obtained provide insight into the molecular mechanism by which these compounds interact with tubulin and function to prevent microtubule assembly. Finally, to aid in the design of effective parasitic microtubule inhibitors, several novel dinitroaniline analogues are evaluated. The location of the binding site and the relative binding affinities of the dinitroanilines all agree well with experimental data.

Aniline Compounds↗
PubMed2003

Toxoplasma gondii: perfecting an intracellular life style.

Toxoplasma gondii is a widespread protozoan parasite that infects all nucleated cell types of warm-blooded vertebrates. Parasite motility is regulated by polymerization of new actin filaments that provide a substrate for the small myosin TgMyoA. Interaction between the cytoplasmic tails of parasite adhesins and the actin-binding protein aldolase links these cell surface proteins with the cytoskeleton. Translocation of adhesins coupled to extracellular receptors allows the parasite to glide across the substrate. This conserved system is important for active penetration into host cells and tissue migration by T. gondii. Entry into the host cell is accompanied by dramatic remodeling of the intracellular vacuole that the parasite resides in. This compartment resists fusion with host cell endocytic organelles, yet recruits mitochondria and endoplasmic reticulum in order to gain access to host cell nutrients. The combined abilities to actively penetrate host cells and control the fate of the parasite-containing vacuole contributes to the remarkable success of T. gondii as an intracellular parasite.

Animals↗