Transplantation into Jirds as a Method of Assessing the Viability and Reproductive Integrity of Adult Acanthocheilonema viteae from Culture

1991 ◽  
Vol 77 (5) ◽  
pp. 749 ◽  
Author(s):  
Jun Maki ◽  
Paul P. Weinstein
Keyword(s):  
Acanthocheilonema Viteae

Localization, turnover and conservation of gp15/400 in different stages ofBrugia malayi

Parasitology ◽  
1993 ◽  
Vol 107 (4) ◽  
pp. 449-457 ◽  
Author(s):  
M. E. Selkirk ◽  
W. F. Gregory ◽  
R. E. Jenkins ◽  
R. M. Maizels
Keyword(s):  
Protein Complex ◽  
Cdna Probe ◽  
The Body ◽  
Mammalian Host ◽  
Major Protein ◽  
Homologous Genes ◽  
Acanthocheilonema Viteae ◽  
Filarial Nematodes ◽  
The Matrix

SUMMARYThe expression of a protein complex designated gp15/400, previously identified via extrinsic iodination of adultBrugia malayi, was examined by labelling all stages found in the mammalian host and immunoprecipitation with a specific antibody raised to a recombinant protein. In this way, gp15/400 could be detected in L3, L4, adult worms and microfilariae recovered from jirds and labelled with Bolton–Hunter reagent. Metabolic labelling indicated that gp15/400 was released into culture medium when adult worms were maintainedin vitro, but at a rate slower than that of gp29, the major soluble cuticular glycoprotein. Immuno-electron microscopy showed that the protein complex was broadly distributed in different tissues, although it was not detectable in the cuticle of adult worms. Dense labelling was observed in the matrix of the basal laminae bordering the hypodermis, somatic musculature and oesophagus, and lower but significant labelling was seen in the cells overlying these extracellular matrices. Hybridization of genomic DNA with a cDNA probe encoding gp15/400 indicated that homologous genes were present inDirofilaria immitisandAcanthocheilonema viteae. The failure to detect related genes in non-filarial nematodes was presumed to be due to divergence beyond the practical limits of detection by nucleic acid probes, as antibody reagents showed that the protein cross-reacted immunologically with ABA-1, a major protein allergen from the body fluid ofAscaris.

Expression of the filarial nematode phosphorylcholine-containing glycoprotein, ES62, is stage specific

Parasitology ◽  
2002 ◽  
Vol 125 (2) ◽  
pp. 155-164 ◽  
Author(s):  
G. STEPEK ◽  
M. AUCHIE ◽  
R. TATE ◽  
K. WATSON ◽  
D. G. RUSSELL ◽  
...  
Keyword(s):  
Transcriptional Control ◽  
Close Relation ◽  
Onchocerca Volvulus ◽  
Filarial Nematode ◽  
Cdna Libraries ◽  
Homologous Sequences ◽  
Acanthocheilonema Viteae ◽  
Filarial Nematodes ◽  
Species Specific ◽  
Control Of Expression

ES62, an immunomodulatory phosphorylcholine-containing glycoprotein secreted by the rodent filarial nematode Acanthocheilonema viteae, has previously been shown to be produced by L4 larvae and adult worms only. However, homologous sequences to ES62 have recently been found in L1 and L3 cDNA libraries of certain human filarial nematodes. Therefore, the various stages of A. viteae were re-examined and it was again found that only the post-L3 stages secreted ES62. Synthesis but not secretion by earlier stages was ruled out by examination of the protein content of whole worm extracts and by immunoelectron microscopy. However, examination by PCR of the mRNA for ES62 revealed that it was found in the L1 and L3 larvae. This may explain why homologous sequences to ES62 have been found in Brugia malayi and Onchocerca volvulus larval cDNA libraries. It also suggests that filarial nematodes, in general, may secrete ES62. To obtain evidence for this, we investigated production by Brugia pahangi, a close relation of B. malayi. We found that ES62 was indeed secreted but, as with A. viteae, only by the post-L3 stages, although again the mRNA for ES62 could be detected in the earlier stages. Overall our results suggest that production of ES62 is not species specific, that it is indeed stage specific, and that this may be due to post-transcriptional control of expression.

CONCOMITANT IMMUNITY IN A RODENT MODEL OF FILARIASIS: THE INFECTION OF MERIONES UNGUICULATUS WITH ACANTHOCHEILONEMA VITEAE

2006 ◽  
Vol 92 (1) ◽  
pp. 41-45 ◽  
Author(s):  
Sethu Rajakumar ◽  
Wilfrid Bleiss ◽  
Susanne Hartmann ◽  
Peter Schierack ◽  
Anorte Marko ◽  
...  
Keyword(s):  
Meriones Unguiculatus ◽  
Rodent Model ◽  
Acanthocheilonema Viteae ◽  
Concomitant Immunity

ES-62, a therapeutic anti-inflammatory agent evolved by the filarial nematode Acanthocheilonema viteae

2014 ◽  
Vol 194 (1-2) ◽  
pp. 1-8 ◽  
Author(s):  
Miguel A. Pineda ◽  
Felicity Lumb ◽  
Margaret M. Harnett ◽  
William Harnett
Keyword(s):  
Filarial Nematode ◽  
Inflammatory Agent ◽  
Acanthocheilonema Viteae ◽  
Anti Inflammatory

Characterization of heterotrimeric G-proteins in adult Acanthocheilonema viteae

1996 ◽  
Vol 320 (2) ◽  
pp. 459-466 ◽  
Author(s):  
GRANT Karen R. ◽  
Margaret M. HARNETT ◽  
Graeme MILLIGAN ◽  
William HARNETT
Keyword(s):  
G Protein ◽  
G Proteins ◽  
Pertussis Toxin ◽  
Eukaryotic Cells ◽  
Heterotrimeric G Proteins ◽  
Protein Subunits ◽  
Acanthocheilonema Viteae ◽  
Affinity Labelling ◽  
Α Subunits

Heterotrimeric G-proteins have been found in eukaryotic cells, from yeast to humans, but have received little attention, to date, with respect to parasitic organisms. We now present the first report of the characterization of heterotrimeric G-proteins expressed in a filarial nematode, Acanthocheilonema viteae. Using a combination of (i) affinity labelling with [α-32P]GTP; (ii) ADP-ribosylation with cholera toxin and pertussis toxin; (iii) Western blotting with a panel of anti-G-protein antibodies; and (iv) reverse transcriptase-PCR with degenerate G-protein oligonucleotide primers followed by hybridization analysis using oligonucleotides specific for individual G-protein subunits, we demonstrate that adult A. viteae expresses homologues of the β1-and/or β2-like subunits and α-subunits of the Gs, Gi, Gq and G12 subfamilies found in mammals. The role which these G-proteins may play in the biology of the organism is discussed.

Glucose transport in Acanthocheilonema viteae

Parasitology ◽  
1990 ◽  
Vol 101 (2) ◽  
pp. 249-255 ◽  
Author(s):  
D. J. Hayes ◽  
D. L. Selwood
Keyword(s):  
Glucose Transport ◽  
Glucose Transporter ◽  
Cytochalasin B ◽  
Glycogen Depletion ◽  
Acanthocheilonema Viteae ◽  
The One

The uptake of glucose by Acanthocheilonema viteae was studied in vitro. The process was selective for the D-isomer and saturatable with a Km of 2 mM. The rate of glucose transport/utilization was inhibited by 2-deoxyglucose, mannose, 5-thioglucose and dipyridamole but, unlike mammalian systems, was not impaired by cytochalasin B, phloretin, phloridzin, 3-O-methylglucose and 4, 6-ethylideneglucose. A potential chemotherapeutic advantage of selectively inhibiting filarial glucose transport exists for the following reasons. (1) The glucose transporter present in A. viteae was shown to be different from the one present in some mammalian systems. (2) Incubation under glucose-free conditions led to glycogen depletion, loss of motility and worm death. (3) Worms maintained in vitro for more than 18 h without glucose did not survive when implanted into gerbils.

scholarly journals Secreted microRNA data from the parasitic filarial nematode Acanthocheilonema viteae

Data in Brief ◽  
2020 ◽  
Vol 29 ◽  
pp. 105334
Author(s):  
Julien Soichot ◽  
Yvette Endriss ◽  
Hanspeter Marti ◽  
Lucienne Tritten
Keyword(s):  
Filarial Nematode ◽  
Acanthocheilonema Viteae
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