Identification of a major surface protein on Neospora caninum tachyzoites.

Hemphill, Andrew; Gottstein, Bruno (1996). Identification of a major surface protein on Neospora caninum tachyzoites. Parasitology research, 82(6), pp. 497-504. Springer-Verlag 10.1007/s004360050152

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Neospora caninum is a recently identified coccidian parasite that is closely related to Toxoplasma gondii. Molecules associated with the surface of N. caninum tachyzoites are likely to be involved in the process of adhesion and invasion of host cells. They probably also participate in the interaction of the parasite with the immune system, and they could play an important role in the pathogenesis of the parasite. To identify such surface molecules, we performed subcellular fractionation studies of isolated N. caninum tachyzoites. Employing the nonionic detergent Triton-X-114, we prepared a membrane fraction. Immunoblot analysis of this fraction using polyclonal antisera directed against tachyzoites of N. caninum and T. gondii resulted in the identification of a protein of approximately 43 kDa (Nc-p43). This molecule was present in two isolates of Neospora (Nc-1 and Liverpool) but was absent in Toxoplasma (RH-strain) tachyzoites. Further immunofluorescence and immunogold transmission electron microscopy (TEM) studies using affinity-purified anti-Nc-p43 antibodies demonstrated the presence of this molecule on the surface of N. caninum tachyzoites.

Item Type:

Journal Article (Original Article)

Division/Institute:

05 Veterinary Medicine > Department of Infectious Diseases and Pathobiology (DIP) > Institute of Parasitology
05 Veterinary Medicine > Department of Infectious Diseases and Pathobiology (DIP)

UniBE Contributor:

Hemphill, Andrew and Gottstein, Bruno

Subjects:

600 Technology > 630 Agriculture
600 Technology > 610 Medicine & health

ISSN:

0932-0113

Publisher:

Springer-Verlag

Language:

English

Submitter:

Bruno Gottstein

Date Deposited:

18 Jul 2018 14:15

Last Modified:

18 Jul 2018 16:25

Publisher DOI:

10.1007/s004360050152

PubMed ID:

8832729

BORIS DOI:

10.7892/boris.118699

URI:

https://boris.unibe.ch/id/eprint/118699

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