I am trying to express a membrane receptor of entamoeba origin in Sf9 cells. I will be using the HBM signal peptide for targeting my protein in the insect cells. the HBM is generally cleaved after the last Ala residue. But in some research articles i found that people are adding an aspartic acid residue after the HBM signal peptide and then the protein of interest.No aspartate residue is present in the HBM protein after the signal sequence. I donot understand the reason of adding the Asp residue. Can somebody please help?
Dear Shilpa Sarkar,
I stumble on your question just now. I’m not sure whether you already solved the ‘mystery’ behind your question already but as stated in the following reference:
https://www.researchgate.net/publication/14910675_High-level_expression_and_purification_of_secreted_forms_of_herpes_simplex_virus_type_1_glycoprotein_gD_synthesized_by_baculovirus-infected_insect_cells
“Note that in each case, cloning into the BamHI site of pVT-Bac should cause two extra amino acids (aspartic acid and proline) to be present at the N terminus.
In other words your observation that an additional aspartic acid is present that do not belong to the BHM sequence is most likely simply a consequence of the mutation set-up (replacing a native sequence for a BHM sequence).
FYI.
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