Abstract
The structure of the ectodomain of the hepatitis C envelope glycoprotein E1 (E1s) was characterised by spectroscopic methods. Monomeric E1s was purified from a mammalian and from a Hansenula polymorpha cell lysate, and cysteine-blocked monomers were reconstituted into stable particles. Particles from yeast E1s and mammalian E1s showed a comparable reactivity in ELISA with sera from human chronic HCV carriers, similar antibody titers in the sera of immunised mice as well as a comparable structure as analyzed by spectroscopic methods (tryptophan fluorescence, circular dichroism, and Fourier transform infrared spectroscopy). The overall secondary structure of E1s was neither influenced by the degree of glycosylation nor by the nature of cysteine modification used during purification. The structural comparability of mammalian- and H. polymorpha-expressed E1s opens new perspectives for further development of E1s-based therapeutics as yeast systems generally allow a more easy scaling up.
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