Heterologous expression of Babesia bovis vaccine candidate MSA-2c in Tetrahymena thermophila

MONTES, GUADALUPE; EUGENIA ELGUERO; CLARA B. NUDEL; CHRISTENSEN MONICA; LEONHARD SCHNITTGER; ALEJANDRO D. NUSBLAT

Mar del Plata

Congreso; LI Reunion Anual 2015; 2015

Sociedad Argentina de Investigacion Bioquimica y Biologia Molecular

Tetrahymena thermophila is a non-pathogenic protozoa used for the expression of recombinant proteins. Several glycosylphosphatidylinositol (GPI) anchors proteins have been expressed successfully in the surface of this ciliate. Some examples are the circumsporozoite protein (CSP) of Plasmodium falciparum and the immobilization antigen of Ichthyophthirius multifiliis, which are used as vaccine candidates for malaria and white dot disease respectively.Babesia bovis is a tick-transmitted hemoprotozooan that causes infection diseases in vertebrate hosts. It is responsible for the mortality of cattles, leading to significant economic losses. Up to date, no effective recombinant vaccines are available.The GPI protein MSA2c of B. bovis represents a prominent vaccine candidate that was chosen to be expressed in T. thermophila for the preparation of subunit vaccines. We could achieve episomal expression of MSA2c in whole cell of T. thermophila and also in enrich GPI fraction.Preliminary analysis, based on a detergent phase-partitioning procedure followed by HPLC-MS, has confirmed the expression of MSA2c as an endogenous GPI protein of 35 kda member of the SerH family. This result demonstrated that T. thermophila expresses successfully heterologous GPI proteins and supported the idea that it can be used as a platform to produce recombinant surface antigens.