Oocyst production, late-stage merogony, gametogony, and cross-transmission studies of Eimeria bubonis (Protozoa: Eimeriidae) of the great horned owl, Bubo virginianus

1982 ◽  
Vol 60 (10) ◽  
pp. 2279-2283 ◽  
Author(s):  
Richard J. Cawthorn ◽  
P. H. G. Stockdale

The study was designed to examine oocyst production, endogenous development and host specificity of Eimeria bubonis (Protozoa: Eimeriidae). Three great horned owls were administered 1.0 × 104 sporulated oocysts of E. bubonis orally. Three more great horned owls were each fed two mice which had been previously intubated with sporulated oocysts of E. bubonis. Feces were examined daily after flotation and oocyst production was estimated. One great horned owl was administered 2.25 × 105 sporulated oocysts of E. bubonis, killed 5.5 days later and examined histologically. Domestic chicks were administered oocysts of E. bubonis and their feces examined as above. Mice were administered sporulated oocysts of E. bubonis and then killed sequentially. Tissues of chickens and mice were examined histologically. The prepatent period of E. bubonis in great horned owls was 5.0–6.0 days; the patent period was as short as 4–6 days. Maximal oocyst production occurred 6–7 days after infection. Endogenous development occurred distal to nuclei of villar epithelial cells in the anterior half of the small intestine. E. bubonis was not transmissible to chickens. Pyogranulomas developed and persisted 12 weeks in mice administered E. bubonis; however, there were no stages of E. bubonis infective to great horned owls.

1982 ◽  
Vol 60 (2) ◽  
pp. 152-157 ◽  
Author(s):  
Richard J. Cawthorn ◽  
P. H. G. Stockdale

The purpose of the study was to describe some parameters of oocyst production in direct and indirect transmission studies, endogenous development, and attempts at cross transmission of Caryospora bubonis (Protozoa: Eimeriidae) of great horned owls, Bubo virginianus (Gmelin). Three great horned owls were given sporulated oocysts of C. bubonis orally. Three more great horned owls were each fed two mice which had been given sporulated oocysts of C. bubonis orally, 4 weeks previously. Feces were examined daily by flotation and daily oocyst production was estimated. One great horned owl was given sporulated oocysts of C. bubonis and killed 12 days after infection when oocysts were first detected in feces. Tissues were examined histologically. Two long-eared owls (Asio otus (Pontoppidan)) and one short-eared owl (Asio flammeus (L.)) and domestic chicks (Gallus domesticus L.) were given sporulated oocysts of C. bubonis orally and their feces examined as above. Mice were given varying doses of sporulated oocysts of C. bubonis orally and killed sequentially after infection. Tissues of mice and chickens were examined histologically.The prepatent period was 12 days, the patent period was 4–11 days long and maximal oocyst production occurred from 12 to 17 days after direct infection of great horned owls with C. bubonis. The prepatent period was shortened by 48 h in owls indirectly infected with C. bubonis in mice. Endogenous development occurred in the posterior third of the small intestine. Caryospora bubonis was not transmitted to other species of birds.


1984 ◽  
Vol 62 (2) ◽  
pp. 217-225 ◽  
Author(s):  
Richard J. Cawthorn ◽  
Alvin A. Gajadhar ◽  
Ronald J. Brooks

Sarcocystis rauschorum sp. n. (Protozoa: Sarcocystidae) is heteroxenous, with varying lemmings (Dicrostonyx richardsoni) as expermental intermediate hosts and snowy owls (Nyctea scandiaca) as natural and experimental definitive hosts. Free sporocysts of a Sarcocystis-like organism (11.6 × 9.2 μm with a diffuse residuum of numerous small refractile granules) from intestinal scrapings of a naturally infected snowy owl were orally administered to laboratory-reared varying lemmings. Meronts were present 7 days post inoculation (DPI) in hepatocytes. Cysts of S. rauschorum sp. n. developed in striated muscle and contained metrocytes (4.6 × 3.8 μm) 14 DPI; bradyzoites (6 × 2 μm) were present at least as early as 28 DPI. Cysts at 84 DPI were not macroscopic (greatest diameter 80.9 μm, least diameter 70.9 μm) with walls 0.35–0.70 μm thick. Laboratory-reared rats (Rattus norvegicus), house mice (Mus musculus), white-footed mice (Peromyscus leucopus), red-backed voles (Clethrionomys gapped), and brown lemmings (Lemmus sibiricus) were not suitable intermediate hosts. Carcasses of varying lemmings containing cysts (57 and 84 DPI) of S. rauschorum sp. n. were fed to three Sarcocystis-free snowy owls. The prepatent period was 7 days and the patent period 12 – 19 days. Sporogony occurred in the lamina propria throughout the length of the small intestine. Free sporocysts (10.4 × 8.2 μm with a compact residuum of numerous small refractile granules) from experimentally infected owls were infective for varying lemmings.


Parasitology ◽  
1989 ◽  
Vol 98 (3) ◽  
pp. 329-336 ◽  
Author(s):  
F. Nowell ◽  
S. Higgs

SUMMARYCharacteristics of four species of Eimeria isolated from Apodemus sylvaticus are described. From oocyst morphology, three are identified as E. apionodes, E. hungaryensis and E. uptoni, the fourth being unnamed. Cloning demonstrated that oocysts of E. hungaryensis were polymorphic. Previous literature relating to the taxonomy is discussed and discrepancies outlined. Species isolated from A. sylvaticus were not transmissible to Clethrionomys glareolus, but both E. hungaryensis and E. apionodes have been passaged through immunosuppressed laboratory mice, the former species more than 16 times. In both A. sylvaticus and immunosuppressed laboratory mice, endogenous development of E. hungaryensis occurred mainly in enterocytes near the tips of the villi in the first half of the small intestine, with a few parasites in the rest of the small intestine and into the large intestine. The pre-patent period was 2 days in both hosts but oocyst output was higher in the natural hosts. E. apionodes parasitized enterocytes on the sides or at the base of the villi, mainly in the last 90% of the small intestine with a few parasites in the large intestine. The pre-patent period was 7 days. Parasites, probably E. hungaryensis and E. apionodes, were also isolated from A. flavicollis.


Author(s):  
A. J. Tousimis

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.


Author(s):  
D.S. Friend ◽  
N. Ghildyal ◽  
M.F. Gurish ◽  
K.F. Austen ◽  
R.L. Stevens

Trichinella spiralis induces a profound mastocytosis and eosinophilia in the small intestine of the infected mouse. Mouse mast cells (MC) store in their granules various combinations of at least five chymotryptic chymases [designated mouse MC protease (mMCP) 1 to 5], two tryptic proteases designated mMCP-6 and mMCP-7 and an exopeptidase, carboxypeptidase A (mMC-CPA). Using antipeptide, protease -specific antibodies to these MC granule proteases, immunohistochemistry was done to determine the distribution, number and protease phenotype of the MCs in the small intestine and spleen 10 to >60 days after Trichinella infection of BALB/c and C3H mice. TEM was performed to evaluate the granule morphology of the MCs between intestinal epithelial cells and in the lamina propria (mucosal MCs) and in the submucosa, muscle and serosa of the intestine (submucosal MCs).As noted in the table below, the number of submucosal MCs remained constant throughout the study. In contrast, on day 14, the number of MCs in the mucosa increased ~25 fold. Increased numbers of MCs were observed between epithelial cells in the mucosal crypts, in the lamina propria and to a lesser extent, between epithelial cells of the intestinal villi.


2006 ◽  
Vol 50 (2) ◽  
pp. 198-200
Author(s):  
Juliana Fariña ◽  
M. Concepción Millana ◽  
M<sup>a</sup> Jesús Fernández-Aceñero ◽  
Vanessa Campo-Ruiz

1989 ◽  
Vol 109 (3) ◽  
pp. 1057-1069 ◽  
Author(s):  
A Marxer ◽  
B Stieger ◽  
A Quaroni ◽  
M Kashgarian ◽  
H P Hauri

The previously produced monoclonal antibody IEC 1/48 against cultured rat intestinal crypt cells (Quaroni, A., and K. J. Isselbacher. 1981. J. Natl. Cancer Inst. 67:1353-1362) was extensively characterized and found to be directed against the beta subunit of (Na+ + K+)-ATPase as assessed by immunological and enzymatic criteria. Under nondenaturing conditions the antibody precipitated the alpha-beta enzyme complex (98,000 and 48,000 Mr). This probe, together with the monoclonal antibody C 62.4 against the alpha subunit (Kashgarian, M., D. Biemesderfer, M. Caplan, and B. Forbush. 1985. Kidney Int. 28:899-913), was used to localize (Na+ + K+)-ATPase in epithelial cells along the rat intestinal tract by immunofluorescence and immunoelectron microscopy. Both antibodies exclusively labeled the basolateral membrane of small intestine and proximal colon epithelial cells. However, in the distal colon, IEC 1/48, but not C 62.4, also labeled the brush border membrane. The cross-reacting beta-subunit-like antigen on the apical cell pole was tightly associated with isolated brush borders but was apparently devoid of (Na+ + K+)-ATPase activity. Subcellular fractionation of colonocytes in conjunction with limited proteolysis and surface radioiodination of intestinal segments suggested that the cross-reacting antigen in the brush border may be very similar to the beta subunit. The results support the notion that in the small intestine and proximal colon the enzyme subunits are exclusively targeted to the basolateral membrane while in the distal colon nonassembled beta subunit or a beta-subunit-like protein is also transported to the apical cell pole.


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