Purification and characterization of a novel glycoprotein from Streptomyces sp. ZX01.

A novel glycoprotein GP-1 with antiviral activity against plant virus was isolated from the fermentation broth of the actinomycete Streptomyces sp. ZX01. MALDI-TOF-MS proved that molecular weight of GP-1 approximately was 8.5 kDa. GP-1 was a heat-sensitive glycoprotein with decreasing antiviral activity after treated from 80 °C to 100 °C for 30 min. GP-1 contained 40.23% carbohydrate with N-linked and O-linked glycan. FT-IR and NMR spectra proved that GP-1 contained protein and carbohydrate portions with α-D-(1,6)-glucose residues. Circular dichroism revealed that GP-1 was a glycoprotein with a large unordered content. Moreover, protein sequencing was predicted by using MALDI-TOF-MS and Mascot search. These results suggested that glycoprotein GP-1 could be used as a novel natural antiviral agent in agricultural industry.