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PubMed2006

Morphological and molecular characterization of a new microsporidian (Protozoa: Microsporidia) isolated from Spodoptera litura (Fabricius) (Lepidoptera: Noctuidae).

A microsporidium was isolated from larvae of Spodoptera litura (Fabricius) collected from Tamil Nadu, India. This microsporidian species is monomorphic, disporous and develops in direct contact with the cytoplasm of the host cell. The nuclear configuration of merogonic and sporogonic stages was diplokaryotic. The merogonic proliferative stage was unusual that normal development with 1, 2 and 4 binucleated forms were common, while large multinucleate meronts containing 8 and 12 small compact horseshoe-like diplokaryotic nuclei were also observed. The fresh spores were typically ovocylindrical in shape, with a mean size of 3.91 x 1.91 microm and the polar filament length was approximately 90 microm. Infection was systemic with mature spores produced in the midgut, nervous tissue, muscles, labial glands, gonads, tracheae, epidermis, Malpighian tubules and, most extensively, fat body tissues. The new isolate was highly pathogenic to S. litura larvae. Host specificity tests performed on 37 non-target hosts of 5 different insect orders revealed that the new isolate is pathogenic only to lepidopteran insects. We sequenced the 16S small subunit rRNA (SSU rRNA) gene of the isolate and compared it with 72 non-redundant microsporidian sequences from the GenBank. Based on the light microscopic studies and phylogenetic analyses, the new isolate is assigned to the genus Nosema. Significant differences in the SSU rRNA sequence were identified when compared with the type species Nosema bombycis and other closely related species viz., Nosema spodopterae. Structural differences were also observed in the 16S SSU rRNA between the new isolate and the two above-mentioned microsporidian pathogens. We conclude that the microsporidian isolate reported here is distinctly different from the other known species and is likely to be a new species.

Animals↗
PubMed1997

Comparative sequence analysis of 5.8S rRNA genes and internal transcribed spacer (ITS) regions of trichomonadid protozoa.

The taxonomic situation in the genus Tritrichomonas is the subject of controversial discussion: potentially T. foetus and T. suis, the tritrichomonads from cattle and swine, respectively, could belong to the same species. In order to shed some light on this question, a molecular biological analysis was performed. The 5.8S rRNA gene and the flanking internal transcribed spacer regions (ITS1 and ITS2) of 12 different isolates of 3 Tritrichomonas species T. foetus, T. suis and T. mobilensis were enzymatically amplified by PCR and subcloned. Also, the corresponding regions of the trichomonads Trichomonas vaginalis, T. tenax, T. gallinae and Pentatrichomonas hominis were included in this study. Sequence analysis of cloned fragments was used to compare the parasite isolates. The genus Tritrichomonas exhibited an extremely high degree of homogeneity. All T. foetus and T. suis isolates had identical sequences, and only 1 substitution was found in the ITS2 region of T. mobilensis. In contrast, the genus Trichomonas shared more diversity. The results obtained in this study support a possible future revision of the taxonomic classification of tritrichomonads.

Animals↗
PubMed2000

Population biology of Eimeria (Protozoa: Apicomplexa) in Apodemus sylvaticus: a capture/recapture study.

The first long-term (27 month) survey of single species of Eimeria occurring in a population of Apodemus sylvaticus in the UK showed that Eimeria apionodes, E. hungaryensis and E. uptoni occurred throughout the period whilst E. sp. E. was only found during 4 months. In first-captured animals, overall prevalence of Eimeria spp. was 73%: a figure higher than previously published, but possibly an underestimate. Multiple infections (2 or 3 species) occurred in 34% of first-capture infected animals, but without significant associations. There were no significant differences of prevalence rates between the sexes, nor between adults and juveniles, except for E. uptoni which was more common in juveniles than in adults. E. hungaryensis and E. uptoni probably occurred as near-continuous infections whilst E. apionodes occurred more intermittently but with no long-term total immunity. Monthly prevalence data indicated ongoing trends over the 27 months. Prevalences of E. apionodes indicated an annual cycle, lowest in January-May and with a peak in October-November, correlating positively with both the number of animals and the percentage of juveniles in the host population and also with the environmental relative humidity. There was no consistent pattern for E. uptoni and an annual cycle for E. hungaryensis was not apparent.

Age Factors↗
PubMed1989

Glucosylation of glycoproteins by mammalian, plant, fungal, and trypanosomatid protozoa microsomal membranes.

An assay for UDP-Glc:glycoprotein glucosyltransferase was developed. Incubation of rat liver microsomes with UDP-[14C]Glc led to the formation of hot trichloroacetic acid insoluble material identified as protein-linked Glc1Man7-9GlcNAc2. Addition of 8 M urea-denatured thyroglobulin to the incubation mixtures stimulated up to 10-12-fold the formation of the same compounds but only in the presence of detergents. Native thyroglobulin was ineffective. Several experiments indicated that the stimulation was due to the transfer of glucose residues from UDP-Glc to high-mannose oligosaccharides in urea-denatured thyroglobulin and that this transfer reaction did not involve dolichol mono- or diphosphate derivatives as intermediates. The glycoprotein glucosylating activity was mainly located in the endoplasmic reticulum and could glucosylate glycopeptides derived from the digestion of thyroglobulin with an unspecific protease. Glucosylation of oligosaccharides in those glycopeptides occurred, however, at a rate at least 2 orders of magnitude slower than that of the same compounds in urea-denatured thyroglobulin. Tryptic digestion of urea-denatured thyroglobulin did not affect its glucosylation rate. The structure of Glc1Man9GlcNAc2 linked to urea-denatured thyroglobulin was identical with that of Glc1Man9GlcNAc2-P-P-dolichol. The assay of UDP-Glc:glycoprotein glucosyltransferase allowed detection of the activity in microsomal membranes in which endogenous acceptors appeared to be absent or almost absent, such as those derived from mung bean, Mucor rouxii, Crithidia fasciculata, and Trypanosoma cruzi cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Acetylglucosaminidase↗
PubMed2001

Marine protozoa produce organic matter with a high affinity for PCBs during grazing.

Processes influencing organic carbon distribution and composition can control the speciation of organic contaminants such as polychlorinated biphenyls (PCBs) and ultimately determine their residence time in aquatic environments. Protozoan grazers are active in the remineralization and recycling of organic material both in the water column and at the sediment-water interface. Thus, they influence the quality and quantity of potential PCB binding substrates in the suspended and dissolved phases of aqueous systems. In this study, common headspace systems were used to compare the chlorobiphenyl-binding affinity of dissolved organic carbon (DOC) in protozoan and bacterial culture filtrates (<0.2 microm) relative to DOC in a seawater control. Culture filtrates from three marine protozoan species were compared-Uronema sp., Cafeteria sp., and Paraphysomonas imperforata. Each protozoan species was fed the same bacterial prey, Halomonas halodurans, which was also used as a bacterial control. Affinities of culture DOC for [14C]3,3',4,4'-tetrachlorobiphenyl (IUPAC 77) were normalized to DOC and surfactant concentrations. Values of DOC equilibrium partition coefficients (K(DOC)) ranged from 10(4.6) in seawater (Vineyard Sound, MA) to 10(5.4) and 10(5.5) in protist cultures, indicating that grazer-modified DOC was a better sorbent for PCBs than DOC in bacterial or seawater controls.

Absorption↗
PubMed2002

Topological organization of DNA molecules in the macronucleus of hypotrichous ciliated protozoa.

The DNA in the macronucleus of a hypotrichous ciliate occurs as millions of short molecules packed into dense chromatin bodies 0.1-2 microm in diameter. We have studied by electron microscopy the organization of DNA molecules in these chromatin bodies of macronuclei lysed in water at pH 9. Proteinase K treatment of lysed macronuclei progressively releases from chromatin bodies many rosettes of DNA molecules bound at one or both ends to a central core of protein. With longer treatment with proteinase K, rosettes disappear, leaving individual free DNA molecules. We propose that, in the native state, both ends of DNA molecules are bound through telomere-binding protein to a central core to form rosettes. Many rosettes, with collapsed DNA loops, aggregate to form a chromatin body. Chromatin bodies are believed to dissociate into individual collapsed rosettes to form the granules in the forward zone of the replication band. In the rear zone of the band, the rosettes dissociate, presumably as a result of release of telomere-binding protein, which is preliminary to the replication of the DNA molecules.

Animals↗
PubMed1997

Conserved features of TBE1 transposons in ciliated protozoa.

The complete sequences of four TBE1 transposons from Oxytricha fallax and O. trifallax are presented and analyzed. Although two TBE1s are 98% identical to each other at the nucleotide level, the remaining two TBE1s are only 90% identical both to each other and to the other two. This large evolutionary divergence allows us to identify conserved TBE1 features. TBE1 transposons are 4.1 kbp long and are flanked by 3 bp target-site repeats. The elements consist of 78 bp inverted terminal repeats, of which the 17 terminal base pairs are Oxytricha telomere repeats; a central conserved section of 550 bp that includes a set of nested direct and inverted sequence repeats; and 3 open reading frames conserved for encoded amino acid sequence. The three open reading frames encode a 22 kDa basic protein of unknown function, a 42 kDa 'D,D35E' transposase, and a 57 kDa chimeric C2H2 zinc finger/protein kinase. The protein kinase domain of the 57 kDa protein is unusual, lacking a conserved ATP-binding motif.

Amino Acid Sequence↗