High impact information on Kinetoplastida

• Parasitic protozoa belonging to the order Kinetoplastida contain trypanothione as their major thiol [1].
• In mitochondria of Kinetoplastida belonging to the suborder Trypanosomatina, the nucleotide sequence of transcripts is post-transcriptionally edited via insertion and deletion of uridylate residues [2].
• Protozoan parasites of the order Kinetoplastida may represent an exception, because pol I can mediate the expression of exogenously introduced protein-coding genes in these single-cell organisms [3].
• Using antibodies specific for J, we have developed sensitive assays to screen for J in a range of organisms and have found that J is not limited to trypanosomes that undergo antigenic variation but is conserved among Kinetoplastida [4].
• Glucose transport in T. cruzi is mediated via a carrier with unique properties when compared with the other glucose transporters already characterized among the Kinetoplastida [5].

Biological context of Kinetoplastida

• Furthermore, a single dynamin family gene is also found in the Leishmania major and Trypanosoma vivax genomes, indicating that this is a conserved feature among the kinetoplastida [6].
• The presented analysis of GAPDH in T. borelli gives further support to the assertion that one isoenzyme, the cytosolic one, was acquired by horizontal gene transfer during the evolution of the Kinetoplastida, in the lineage leading to the suborder Trypanosomatina (Trypanosoma, Leishmania), after the divergence from the Bodonina (Trypanoplasma) [7].
• Conserved sequences in the U2 snRNA-encoding genes of Kinetoplastida do not include the putative branchpoint recognition region [8].
• Trans-splicing, as demonstrated in the Kinetoplastida, is not involved in the formation of the mature alpha-tubulin transcript in T. gondii [9].
• Previous studies suggested a correlation between antigenic variation in Kinetoplastida and the presence of two RNA polymerase (pol) II largest subunit genes in these organisms [10].

Anatomical context of Kinetoplastida

• In other Kinetoplastida, different tandemly arranged genes code for distinct PGK isoenzymes in glycosomes and cytosol [11].
• Absorption of highly reactive G alpha G antibodies with purified murine laminin and nidogen, two basement membrane proteins, almost abolished G alpha G reactivity, suggesting the identity of anti-G alpha G with laminin and nidogen antibodies previously reported as elevated in Kinetoplastida infections [12].
• Penetration of the salivary glands of Rhodnius domesticus Neiva & Pinto, 1923 (Hemiptera: Reduviidae) by Trypanosoma rangeli Tejera, 1920 (Protozoa: Kinetoplastida) [13].

Associations of Kinetoplastida with chemical compounds

• Beta-D-Glucosyl-hydroxymethyluracil, also called base J, is an unusually modified DNA base conserved among Kinetoplastida [14].
• Protozoa of the order Kinetoplastida differ from other organisms in their ability to conjugate glutathione (l-gamma-glutamyl-cysteinyl-glycine) and spermidine to form trypanothione [N(1),N(8)-bis(glutathionyl)spermidine], a metabolite involved in defense against chemical and oxidant stress and other biosynthetic functions [15].
• The overall similarity, as judged by the distribution of enzyme activities, of purine salvage in these three members of the kinetoplastida suggest a broad spectrum of activity for any inhibitor acting in this area; the plethora of alternative salvage pathways, however, suggests that in no case would such inhibition be cidal [16].
• As with the hexose transporters in the other members of Kinetoplastida, the TvHT1-encoded system differs from erythrocyte-type glucose transport by its moderate sensitivity to cytochalasin B and its capacity to transport fructose [17].
• In a Neighbor-Net analysis of sequence similarity with homologues from numerous prokaryotes and eukaryotes, cytosolic phosphoglycerate kinase of E. gracilis showed the highest similarity to cytosolic and glycosomal homologues from the Kinetoplastida [18].

Gene context of Kinetoplastida

• Trypanothione reductase (TR) is a flavoenzyme that has been found only in parasitic protozoa of the order Kinetoplastida [19].
• The parasite protein is the first classical thioredoxin of the order Kinetoplastida characterized so far [20].
• Furthermore, the data clearly suggest that the original GAPDH of the Kinetoplastida has been compartmentalized during evolution [7].
• Tryparedoxins are components of the hydroperoxide detoxification cascades of Kinetoplastida, where they mediate electron transfer between trypanothione and a peroxiredoxin, which reduces hydroperoxides and possibly peroxynitrite [21].
• Glyoxalase II occurs in the mammalian bloodstream and insect procyclic form of T. brucei and is the first glyoxalase II of the order of Kinetoplastida characterized so far [22].

References