Recent Advances in Trypanosomatid Research: Genome Organization, Expression, Metabolism, Taxonomy and Evolution
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The Morphology, Ultrastructure and Molecular Phylogeny of a New Freshwater Heterolobose Amoeba Parafumarolamoeba Stagnalis N. Sp
diversity Article The Morphology, Ultrastructure and Molecular Phylogeny of a New Freshwater Heterolobose Amoeba Parafumarolamoeba stagnalis n. sp. (Vahlkampfiidae; Heterolobosea) Anastasia S. Borodina 1,2, Alexander P. Mylnikov 1,†, Jan Janouškovec 3 , Patrick J. Keeling 4 and Denis V. Tikhonenkov 1,5,* 1 Papanin Institute for Biology of Inland Waters, Russian Academy of Sciences, 152742 Borok, Russia; [email protected] 2 Department of Zoology and Parasitology, Voronezh State University, Universitetskaya Ploshad 1, 394036 Voronezh, Russia 3 Centre Algatech, Laboratory of Photosynthesis, Institute of Microbiology, Czech Academy of Sciences, Opatovický Mlýn, 37981 Tˇreboˇn,Czech Republic; [email protected] 4 Department of Botany, University of British Columbia, 6270 University Boulevard, Vancouver, BC V6T1Z4, Canada; [email protected] 5 AquaBioSafe Laboratory, University of Tyumen, 625003 Tyumen, Russia * Correspondence: [email protected]; Tel.: +7-485-472-4533 † Alexander P. Mylnikov is deceased. http://zoobank.org/References/e543a49a-16c1-4b7c-afdb-0bc56b632ef0 Abstract: Heterolobose amoebae are important members of marine, freshwater, and soil microbial Citation: Borodina, A.S.; Mylnikov, communities, but their diversity remains under-explored. We studied the diversity of Vahlkampfiidae A.P.; Janouškovec, J.; Keeling, P.J.; to improve our understanding of heterolobosean relationships and their representation in aquatic Tikhonenkov, D.V. The Morphology, benthos. Using light and electron microscopy, and molecular phylogenies based on the SSU rRNA Ultrastructure and Molecular and ITS loci, we describe the fine morphology and evolutionary relationships of a new heterolobosean Phylogeny of a New Freshwater Parafumarolamoeba stagnalis n. sp. from a small pond in European Russia. Cells of P. stagnalis possess Heterolobose Amoeba a clearly distinguishable anterior hyaline pseudopodium, eruptive movement, several thin and Parafumarolamoeba stagnalis n. -
An Atpase Domain Common to Prokaryotic Cell Cycle Proteins
Proc. Natl. Acad. Sci. USA Vol. 89, pp. 7290-7294, August 1992 Biochemistry An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp7O heat shock proteins (structural comparison/property pattern/remote homology) PEER BORK, CHRIS SANDER, AND ALFONSO VALENCIA European Molecular Biology Laboratory, D-6900 Heidelberg, Federal Republic of Germany Communicated by Russell F. Doolittle, March 6, 1992 ABSTRACT The functionally diverse actin, hexokinase, and hsp7O protein families have in common an ATPase domain of known three-dimensional structure. Optimal superposition ofthe three structures and alignment ofmany sequences in each of the three families has revealed a set of common conserved residues, distributed in five sequence motifs, which are in- volved in ATP binding and in a putative interdomain hinge. From the multiple sequence aliment in these motifs a pattern of amino acid properties required at each position is defined. The discriminatory power of the pattern is in part due to the use of several known three-dimensional structures and many sequences and in part to the "property" method ofgeneralizing from observed amino acid frequencies to amino acid fitness at each sequence position. A sequence data base search with the pattern significantly matches sugar kinases, such as fuco-, glucono-, xylulo-, ribulo-, and glycerokinase, as well as the prokaryotic cell cycle proteins MreB, FtsA, and StbA. These are predicted to have subdomains with the same tertiary structure as the ATPase subdomains Ia and Ha of hexokinase, actin, and Hsc7O, a very similar ATP binding pocket, and the capacity for interdomain hinge motion accompanying func- tional state changes. -
Non-Homologous Isofunctional Enzymes: a Systematic Analysis Of
Omelchenko et al. Biology Direct 2010, 5:31 http://www.biology-direct.com/content/5/1/31 RESEARCH Open Access Non-homologousResearch isofunctional enzymes: A systematic analysis of alternative solutions in enzyme evolution Marina V Omelchenko, Michael Y Galperin*, Yuri I Wolf and Eugene V Koonin Abstract Background: Evolutionarily unrelated proteins that catalyze the same biochemical reactions are often referred to as analogous - as opposed to homologous - enzymes. The existence of numerous alternative, non-homologous enzyme isoforms presents an interesting evolutionary problem; it also complicates genome-based reconstruction of the metabolic pathways in a variety of organisms. In 1998, a systematic search for analogous enzymes resulted in the identification of 105 Enzyme Commission (EC) numbers that included two or more proteins without detectable sequence similarity to each other, including 34 EC nodes where proteins were known (or predicted) to have distinct structural folds, indicating independent evolutionary origins. In the past 12 years, many putative non-homologous isofunctional enzymes were identified in newly sequenced genomes. In addition, efforts in structural genomics resulted in a vastly improved structural coverage of proteomes, providing for definitive assessment of (non)homologous relationships between proteins. Results: We report the results of a comprehensive search for non-homologous isofunctional enzymes (NISE) that yielded 185 EC nodes with two or more experimentally characterized - or predicted - structurally unrelated proteins. Of these NISE sets, only 74 were from the original 1998 list. Structural assignments of the NISE show over-representation of proteins with the TIM barrel fold and the nucleotide-binding Rossmann fold. From the functional perspective, the set of NISE is enriched in hydrolases, particularly carbohydrate hydrolases, and in enzymes involved in defense against oxidative stress. -
Identification and Phylogenetic Analysis of Heme Synthesis Genes in Trypanosomatids and Their Bacterial Endosymbionts
Identification and Phylogenetic Analysis of Heme Synthesis Genes in Trypanosomatids and Their Bacterial Endosymbionts Joa˜o M. P. Alves1*, Logan Voegtly1, Andrey V. Matveyev1, Ana M. Lara1, Fla´via Maia da Silva2, Myrna G. Serrano1, Gregory A. Buck1, Marta M. G. Teixeira2, Erney P. Camargo2 1 Department of Microbiology and Immunology and the Center for the Study of Biological Complexity, Virginia Commonwealth University, Richmond, Virginia, United States of America, 2 Department of Parasitology, ICB, University of Sa˜o Paulo, Sa˜o Paulo, Brazil Abstract It has been known for decades that some insect-infecting trypanosomatids can survive in culture without heme supplementation while others cannot, and that this capability is associated with the presence of a betaproteobacterial endosymbiont in the flagellate’s cytoplasm. However, the specific mechanisms involved in this process remained obscure. In this work, we sequence and phylogenetically analyze the heme pathway genes from the symbionts and from their hosts, as well as from a number of heme synthesis-deficient Kinetoplastida. Our results show that the enzymes responsible for synthesis of heme are encoded on the symbiont genomes and produced in close cooperation with the flagellate host. Our evidence suggests that this synergistic relationship is the end result of a history of extensive gene loss and multiple lateral gene transfer events in different branches of the phylogeny of the Trypanosomatidae. Citation: Alves JMP, Voegtly L, Matveyev AV, Lara AM, da Silva FM, et al. (2011) Identification and Phylogenetic Analysis of Heme Synthesis Genes in Trypanosomatids and Their Bacterial Endosymbionts. PLoS ONE 6(8): e23518. doi:10.1371/journal.pone.0023518 Editor: Purification Lopez-Garcia, Universite´ Paris Sud, France Received May 20, 2011; Accepted July 19, 2011; Published August 10, 2011 Copyright: ß 2011 Alves et al. -
The Intestinal Protozoa
The Intestinal Protozoa A. Introduction 1. The Phylum Protozoa is classified into four major subdivisions according to the methods of locomotion and reproduction. a. The amoebae (Superclass Sarcodina, Class Rhizopodea move by means of pseudopodia and reproduce exclusively by asexual binary division. b. The flagellates (Superclass Mastigophora, Class Zoomasitgophorea) typically move by long, whiplike flagella and reproduce by binary fission. c. The ciliates (Subphylum Ciliophora, Class Ciliata) are propelled by rows of cilia that beat with a synchronized wavelike motion. d. The sporozoans (Subphylum Sporozoa) lack specialized organelles of motility but have a unique type of life cycle, alternating between sexual and asexual reproductive cycles (alternation of generations). e. Number of species - there are about 45,000 protozoan species; around 8000 are parasitic, and around 25 species are important to humans. 2. Diagnosis - must learn to differentiate between the harmless and the medically important. This is most often based upon the morphology of respective organisms. 3. Transmission - mostly person-to-person, via fecal-oral route; fecally contaminated food or water important (organisms remain viable for around 30 days in cool moist environment with few bacteria; other means of transmission include sexual, insects, animals (zoonoses). B. Structures 1. trophozoite - the motile vegetative stage; multiplies via binary fission; colonizes host. 2. cyst - the inactive, non-motile, infective stage; survives the environment due to the presence of a cyst wall. 3. nuclear structure - important in the identification of organisms and species differentiation. 4. diagnostic features a. size - helpful in identifying organisms; must have calibrated objectives on the microscope in order to measure accurately. -
Primary Amoebic Meningoencephalitis Due to Naegleria Fowleri
56 Case report Primary amoebic meningoencephalitis due to Naegleria fowleri A. Angrup, L. Chandel, A. Sood, K. Thakur, S. C. Jaryal Department of Microbiology,Dr. Rajendra Prasad Government Medical College, Kangra at Tanda, Himachal Pradesh, Pin Code- 176001, India. Correspondence to: Dr. Archana Angrup, Department of Microbiology, Dr. Rajendra Prasad Government Medical College, Kangra, Tanda, Himachal Pradesh, Pin Code-176001, India. Phone no. 09418119222, Facsimile: 01892-267115 Email: [email protected] Abstract The genus Naegleria comprises of free living ameboflagellates found in soil and fresh water. More than 30 species have been isolated but only N. fowleri has been associated with human disease. N. fowleri causes primary amoebic meningoencephalitis (PAM), an acute, often fulminant infection of CNS. Here we report a rare and first case of PAM in an immunocompetent elderly patient from this part of the country. Amoeboid and flagellate forms of N. fowleri were detected in the direct microscopic examination of CSF and confirmed by flagellation test in distilled water, demonstrating plaques /clear areas on 1.5% non nutrient agar and its survival at 42°C. Keywords: Meningitis, Naegleria fowleri, primary amoebic meningoencephalitis Introduction of our knowledge, in India, only eight cases have been reported so far .1, 5-8 Infection of the central nervous system (CNS) in human We hereby report a rare case of PAM in elderly beings with free living amoebae is uncommon. Among the immunocompetent patient from the hilly state of Himachal many different genera of amoebae, Naegleria spp, Pradesh (H.P) in Northern India. Acanthamoeba spp and Balamuthia spp are primarily pathogenic to the CNS. -
Effect of a Commercial Disinfectant CLORICAN® on Acanthamoeba Spp
Article Effect of a Commercial Disinfectant CLORICAN® on Acanthamoeba spp. and Naegleria fowleri Viability Ines Sifaoui 1,2,3,*,†, Aitor Rizo-Liendo 1,2,3,†, María Reyes-Batlle 1,2,3, Iñigo Arberas-Jiménez 1,2,3, Rubén L. Rodríguez-Expósito 1,2,3 , José E. Piñero 1,2,3,* and Jacob Lorenzo-Morales 1,2,3,* 1 Instituto Universitario de Enfermedades Tropicales y Salud Pública de Canarias, Universidad de La Laguna (ULL), 38206 Tenerife, Spain; [email protected] (A.R.-L.); [email protected] (M.R.-B.); [email protected] (I.A.-J.); [email protected] (R.L.R.-E.) 2 Departamento de Obstetricia, Ginecología, Pediatría, Medicina Preventiva y Salud Pública, Toxicología, Medicina Legal y Forense y Parasitología, Universidad De La Laguna, La Laguna, Tenerife, 38203 Islas Canarias, Spain 3 Red de Investigación Cooperativa en Enfermedades Tropicales (RICET), Universidad de Salamanca, 37008 Salamanca, Spain * Correspondence: [email protected] (I.S.); [email protected] (J.E.P.); [email protected] (J.L.-M.) † Contributed equally to this work. Abstract: Swimming pool water treatment by chemicals is an essential step to avoid microbial proliferation and infections namely caused by free living amoeba such as, for example, primary amebic meningoencephalitis and Acanthamoeba keratitis. In the present study, a commercial reactive, CLORICAN, based on chlorine dioxide, was evaluated against Acanthamoeba spp. and Naegleria fowleri. We observed that CLORICAN could eliminate in a short period of incubation time both amoebae. Citation: Sifaoui, I.; Rizo-Liendo, A.; Reyes-Batlle, M.; Arberas-Jiménez, I.; Furthermore, Naegleria fowleri’s trophozoites were more sensitive than those of Acanthamoeba spp. -
Table 6. Putative Genes Involved in the Utilization of Carbohydrates in G
Table 6. Putative genes involved in the utilization of carbohydrates in G. thermodenitrificans NG80-2 genome Carbohydrates* Enzymes Gene ID Glycerol Glycerol Kinase GT1216 Glycerol-3-phosphate dehydrogenase, aerobic GT2089 NAD(P)H-dependent glycerol-3-phosphate dehydrogenase GT2153 Enolase GT3003 2,3-bisphosphoglycerate-independentphosphoglycerate mutase GT3004 Triosephosphate isomerase GT3005 3-phosphoglycerate kinase GT3006 Glyceraldehyde-3-phosphate dehydrogenase GT3007 Phosphoglycerate mutase GT1326 Pyruvate kinase GT2663 L-Arabinose L-arabinose isomerase GT1795 L-ribulokinase GT1796 L-ribulose 5-phosphate 4-epimerase GT1797 D-Ribose Ribokinase GT3174 Transketolase GT1187 Ribose 5-phosphate epimerase GT3316 D-Xylose Xylose kinase GT1756 Xylose isomerase GT1757 D-Galactose Galactokinase GT2086 Galactose-1-phosphate uridyltransferase GT2084 UDP-glucose 4-epimerase GT2085 Carbohydrates* Enzymes Gene ID D-Fructose 1-phosphofructokinase GT1727 Fructose-1,6-bisphosphate aldolase GT1805 Fructose-1,6-bisphosphate aldolase type II GT3331 Triosephosphate isomerase GT3005 D-Mannose Mannnose-6 phospate isomelase GT3398 6-phospho-1-fructokinase GT2664 D-Mannitol Mannitol-1-phosphate dehydrogenase GT1844 N-Acetylglucosamine N-acetylglucosamine-6-phosphate deacetylase GT2205 N-acetylglucosamine-6-phosphate isomerase GT2204 D-Maltose Alpha-1,4-glucosidase GT0528, GT1643 Sucrose Sucrose phosphorylase GT3215 D-Trehalose Alpha-glucosidase GT1643 Glucose kinase GT2381 Inositol Myo-inositol catabolism protein iolC;5-dehydro-2- GT1807 deoxygluconokinase -
A Global Analysis of Enzyme Compartmentalization to Glycosomes
pathogens Article A Global Analysis of Enzyme Compartmentalization to Glycosomes Hina Durrani 1, Marshall Hampton 2 , Jon N. Rumbley 3 and Sara L. Zimmer 1,* 1 Department of Biomedical Sciences, University of Minnesota Medical School, Duluth Campus, Duluth, MN 55812, USA; [email protected] 2 Mathematics & Statistics Department, University of Minnesota Duluth, Duluth, MN 55812, USA; [email protected] 3 College of Pharmacy, University of Minnesota, Duluth Campus, Duluth, MN 55812, USA; [email protected] * Correspondence: [email protected] Received: 25 March 2020; Accepted: 9 April 2020; Published: 12 April 2020 Abstract: In kinetoplastids, the first seven steps of glycolysis are compartmentalized into a glycosome along with parts of other metabolic pathways. This organelle shares a common ancestor with the better-understood eukaryotic peroxisome. Much of our understanding of the emergence, evolution, and maintenance of glycosomes is limited to explorations of the dixenous parasites, including the enzymatic contents of the organelle. Our objective was to determine the extent that we could leverage existing studies in model kinetoplastids to determine the composition of glycosomes in species lacking evidence of experimental localization. These include diverse monoxenous species and dixenous species with very different hosts. For many of these, genome or transcriptome sequences are available. Our approach initiated with a meta-analysis of existing studies to generate a subset of enzymes with highest evidence of glycosome localization. From this dataset we extracted the best possible glycosome signal peptide identification scheme for in silico identification of glycosomal proteins from any kinetoplastid species. Validation suggested that a high glycosome localization score from our algorithm would be indicative of a glycosomal protein. -
The Amoeboid Parabasalid Flagellate Gigantomonas Herculeaof
Acta Protozool. (2005) 44: 189 - 199 The Amoeboid Parabasalid Flagellate Gigantomonas herculea of the African Termite Hodotermes mossambicus Reinvestigated Using Immunological and Ultrastructural Techniques Guy BRUGEROLLE Biologie des Protistes, UMR 6023, CNRS and Université Blaise Pascal de Clermont-Ferrand, Aubière Cedex, France Summary. The amoeboid form of Gigantomonas herculea (Dogiel 1916, Kirby 1946), a symbiotic flagellate of the grass-eating subterranean termite Hodotermes mossambicus from East Africa, is observed by light, immunofluorescence and transmission electron microscopy. Amoeboid cells display a hyaline margin and a central granular area containing the nucleus, the internalized flagellar apparatus, and organelles such as Golgi bodies, hydrogenosomes, and food vacuoles with bacteria or wood particles. Immunofluorescence microscopy using monoclonal antibodies raised against Trichomonas vaginalis cytoskeleton, such as the anti-tubulin IG10, reveals the three long anteriorly-directed flagella, and the axostyle folded into the cytoplasm. A second antibody, 4E5, decorates the conspicuous crescent-shaped structure or cresta bordered by the adhering recurrent flagellum. Transmission electron micrographs show a microfibrillar network in the cytoplasmic margin and internal bundles of microfilaments similar to those of lobose amoebae that are indicative of cytoplasmic streaming. They also confirm the internalization of the flagella. The arrangement of basal bodies and fibre appendages, and the axostyle composed of a rolled sheet of microtubules are very close to that of the devescovinids Foaina and Devescovina. The very large microfibrillar cresta supporting an enlarged recurrent flagellum resembles that of Macrotrichomonas. The parabasal apparatus attached to the basal bodies is small in comparison to the cell size; this is probably related to the presence of many Golgi bodies supported by a striated fibre that are spread throughout the central cytoplasm in a similar way to Placojoenia and Mixotricha. -
Trypanosomatids Are Much More Than Just Trypanosomes: Clues from The
Review Trypanosomatids Are Much More than Just Trypanosomes: Clues from the Expanded Family Tree 1,2, 1,3 1,2 4 1,5 Julius Lukeš, * Anzhelika Butenko, Hassan Hashimi, Dmitri A. Maslov, Jan Votýpka, and 1,3 Vyacheslav Yurchenko Trypanosomes and leishmanias are widely known parasites of humans. How- Highlights ever, they are just two out of several phylogenetic lineages that constitute the Dixenous trypanosomatids, such as the human Trypanosoma parasites, family Trypanosomatidae. Although dixeny – the ability to infect two hosts – is a infect both insects and vertebrates. derived trait of vertebrate-infecting parasites, the majority of trypanosomatids Yet phylogenetic analyses have revealed that these are the exception, are monoxenous. Like their common ancestor, the monoxenous Trypanoso- and that insect-infecting monoxenous matidae are mostly parasites or commensals of insects. This review covers lineages are both abundant and recent advances in the study of insect trypanosomatids, highlighting their diverse. diversity as well as genetic, morphological and biochemical complexity, which, Globally, over 10% of true bugs and until recently, was underappreciated. The investigation of insect trypanoso- flies are infected with monoxenous try- matids is providing an important foundation for understanding the origin and panosomatids, whereas other insect groups are infected much less fre- evolution of parasitism, including colonization of vertebrates and the appear- quently. Some trypanosomatids are ance of human pathogens. confined to a single host species, whereas others parasitize a wide spec- trum of hosts. One Host or Two? Lifestyles of the Trypanosomatidae All members of the family Trypanosomatidae are obligatory parasites and include the iconic Many trypanosomatids are themselves pathogens responsible for African sleeping sickness, Chagas’ disease and leishmaniases. -
Predicting the Proteins of Angomonas Deanei, Strigomonas Culicis and Their Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae Family
Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae Family Maria Cristina Machado Motta1, Allan Cezar de Azevedo Martins1, Silvana Sant’Anna de Souza1,2, Carolina Moura Costa Catta-Preta1, Rosane Silva2, Cecilia Coimbra Klein3,4,5, Luiz Gonzaga Paula de Almeida3, Oberdan de Lima Cunha3, Luciane Prioli Ciapina3, Marcelo Brocchi6, Ana Cristina Colabardini7, Bruna de Araujo Lima6, Carlos Renato Machado9,Ce´lia Maria de Almeida Soares10, Christian Macagnan Probst11,12, Claudia Beatriz Afonso de Menezes13, Claudia Elizabeth Thompson3, Daniella Castanheira Bartholomeu14, Daniela Fiori Gradia11, Daniela Parada Pavoni12, Edmundo C. Grisard15, Fabiana Fantinatti-Garboggini13, Fabricio Klerynton Marchini12, Gabriela Fla´via Rodrigues-Luiz14, Glauber Wagner15, Gustavo Henrique Goldman7, Juliana Lopes Rangel Fietto16, Maria Carolina Elias17, Maria Helena S. Goldman18, Marie-France Sagot4,5, Maristela Pereira10, Patrı´cia H. Stoco15, Rondon Pessoa de Mendonc¸a-Neto9, Santuza Maria Ribeiro Teixeira9, Talles Eduardo Ferreira Maciel16, Tiago Antoˆ nio de Oliveira Mendes14, Tura´nP.U¨ rme´nyi2, Wanderley de Souza1, Sergio Schenkman19*, Ana Tereza Ribeiro de Vasconcelos3* 1 Laborato´rio de Ultraestrutura Celular Hertha Meyer, Instituto de Biofı´sica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Rio de Janeiro, Brazil, 2 Laborato´rio de Metabolismo Macromolecular Firmino Torres de Castro, Instituto de Biofı´sica Carlos Chagas Filho,