Biomaterial Database

Peptides associated with monensin resistance in sporozoites of Eimeria tenella (Coccidia). 1994

G Zhu, and J K Johnson, and L R McDougald

Department of Poultry Science, University of Georgia, Athens 30602.

Resistance to monensin in the sporozoites of a laboratory strain (WIS) of Eimeria tenella was amplified by treating free sporozoites with increased monensin levels in vitro, followed by propagation of these treated sporozoites in chickens. The parent strain of WIS and its subsequent lines developed from the treatment of monensin at 1, 5, or 25 micrograms/ml were designated as WIS(0), WIS(1), WIS(5), or WIS(25), respectively. The penetration rate of sporozoites into primary chicken kidney cell cultures showed that the sensitivity of sporozoites to the treatment of monensin at 1 and 5 micrograms/ml was significantly reduced in the WIS(25) line in comparison with the WIS(0) line. When native polyacrylamide gel electrophoresis (PAGE) was conducted, a change in the relative mobility of a protein band was found in the protein samples of these coccidial lines. Sodium dodecyl sulfate PAGE revealed that 2 peptides with molecular weights of approximately 50.0 and 31.4 kDa were present in the sporozoites of resistant lines but undetectable in their WIS-parent sporozoites. Derivation of the resistant lines from a drug-sensitive parent line gave strong support to a link between the appearance of the peptides and resistance to ionophores in this strain of E. tenella.

UI	MeSH Term	Description	Entries
D008985	Monensin	An antiprotozoal agent produced by Streptomyces cinnamonensis. It exerts its effect during the development of first-generation trophozoites into first-generation schizonts within the intestinal epithelial cells. It does not interfere with hosts' development of acquired immunity to the majority of coccidial species. Monensin is a sodium and proton selective ionophore and is widely used as such in biochemical studies.	Coban,Monensin Monosodium Salt,Monensin Sodium,Monensin-A-Sodium Complex,Rumensin,Monensin A Sodium Complex
D010455	Peptides	Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides
D004351	Drug Resistance	Diminished or failed response of an organism, disease or tissue to the intended effectiveness of a chemical or drug. It should be differentiated from DRUG TOLERANCE which is the progressive diminution of the susceptibility of a human or animal to the effects of a drug, as a result of continued administration.	Resistance, Drug
D004591	Electrophoresis, Polyacrylamide Gel	Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.	Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D015800	Protozoan Proteins	Proteins found in any species of protozoan.	Proteins, Protozoan
D016786	Eimeria tenella	A species of coccidian protozoa that mainly infects domestic poultry.	Eimeria tenellas,tenella, Eimeria