Purification of an atypical bovine interferon induced in response to heat shock in bovine cultured cells. Characterization in comparison with the classical alpha, beta and gamma interferon.

ABSTRACT

Heat-shock induced factor (HSIF) was excreted by bovine MDBK cells during their recovery period after a heat shock. This factor has the capacity to induce 2',5' oligoadenylate synthetase activity, an enzyme generally by interferon treatment (J Biol Chem (1987) 262, 4806-4811). We have observed that an antiviral state was also produced in response to heat shock. HSIF was purified 10,000-fold and different techniques showed a copurification of both activities. Certain properties of HSIF were established, such as its molecular mass (45 kDa) and isoelectric point (6.8). This cytokine was acid-sensitive as IFN gamma (type II) and temperature labile contrarily to alpha, beta and gamma bovine IFN. Immunoprecipitation and comparative chromatography on lectines or polynucleotides established that HSIF was structurally different from the three classes of bovine IFN. Moreover, two-dimensional electrophoresis and comparative analysis of [35S] methionine-labeled proteins induced by HSIF alpha, beta or gamma bovine IFN showed that HSIF induces a specific set of proteins. Taken together, all these results strongly suggest that HSIF is a new atypical bovine interferon induced in response to heat shock.