Different derivatives of bovine herpesvirus 1 (BHV-1) glycoprotein B (gB) ectodomain were expressed in a novel heat-shock expression system. The putative ectodomain, gBt, and the N-terminal subunit, gBb, were of the expected molecular weight and were secreted. Their production were heat-inducible and the purified proteins were able to elicit antibody responses in mice of a comparable level as induced by authentic gB. The truncated C-terminal subunit, gBct, was retained in the endoplasmic reticulum. Our studies suggest that the gBb subunit may play a major role in constituting the overall configuration of gB and is required for the intracellular transport of gB.
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Li, Y., Van Drunen Littel-Van den Hurk, S., Liang, X. et al. Production and characterization of bovine herpesvirus 1 glycoprotein B ectodomain derivatives in an hsp70A gene promoter-based expression system. Archives of Virology 141, 2019–2029 (1996). https://doi.org/10.1007/BF01718212
- Molecular Weight
- Infectious Disease
- Endoplasmic Reticulum
- Antibody Response
- Expression System