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S A Tennyson

Publications and source records attributed to S A Tennyson.

5 recordsLinked to original sources
PubMed2000

Localization and immunogenicity of a low molecular weight antigen of Eimeria tenella.

A low molecular weight (LMW) antigen recognized by a murine monoclonal antibody (C(3)4F(1)) was localized within endogenous stages of Eimeria tenella (USDA strain 80). Using indirect fluorescent antibody assay and immunoelectron microscopy, the LMW antigen was found in: sporozoites, first, second and third generation meronts, gamonts, unsporulated oocysts, and sporocysts. The antigen was observed in the cytoplasm and pellicle of the parasite, and in the parasitophorous vacuole, sporocyst walls and cytoplasm of infected host cells. The immunogenicity of this LMW antigen was assessed by antigen-specific serum antibody responses in chickens orally inoculated with live oocysts or injected intramuscularly with dead sporozoites. LMW antigen-specific serum antibodies were detected using Western blots of E. tenella sporozoites as early as 4 days after sporozoite injection and 6 days after oocyst inoculation. Unusually, the monoclonal antibody C(3)4F(1) reduced the binding of immune chicken serum to the antigen in a competitive antibody binding assay, but not the reverse, suggesting that there is a single, immunodominant epitope on this antigen.

Animals↗
PubMed2000

Partial characterization of a non-proteinaceous, low molecular weight antigen of Eimeria tenella.

A low molecular weight (LMW) antigen of Eimeria tenella, initially identified using a murine monoclonal antibody (mAb C(3)4F(1)) raised against E. tenella sporozoites, was partially characterized using enzymatic degradation. solvent extraction, and immunization into various inbred lines of mice. The LMW antigen could be isolated using Folch extraction (methanol/chloroform/ water) and the epitope recognized by mAb C(3)4F(1) was resistant to degradation by alpha-amylase, pronase, and proteinase K, but was sensitive to sodium m-periodate treatment or digestion using mixed glycosidases (from Turbo cornutus). These observations suggest that the antigenic epitope recognized by mAb C(3)4F(1) is carbohydrate-dependent and, based on our ability to isolate the LMW antigen by Folch extraction, the epitope probably resides on a polar glycolipid. The inability of sporozoite-immunized nude mice to elicit a serum antibody response to this molecule indicates that it acts as a T-dependent antigen. Furthermore, sporozoite-immunized male CBA/N mice (with an X-linked immunodeficiency) also failed to elicit a serum antibody response to this molecule, which is consistent with a carbohydrate antigenic epitope. We propose that this antigenic molecule be designated ET-GL1 to reflect its origin and probable structure (E. tenella glycolipid 1).

Animals↗
PubMed1994

The development of the diaphragm in infants with sudden infant death syndrome.

The morphological development of the skeletal muscle of the diaphragm was studied in normal controls and cases of sudden infant death syndrome (SIDS). Measurements of fiber diameter indicated that the SIDS population had significantly larger diameters for type 1 and type 2 fibers than the control population. The ratio of type 1 to type 2 fibers was found to remain significantly depressed with increasing age in the SIDS population compared with the control population, where it increased linearly to values between 0.8 and 1.2 after 10 months of age. These results suggest an abnormality in the development of the diaphragm of SIDS victims, although its exact nature remains to be determined.

Child, Preschool↗