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• W2073194787 abstract "Human parainfluenza virus types 1 (hPIV-1), 2, and 3 represent significant respiratory pathogens for which no antiviral treatment is currently available. To characterize the biochemical functions of the hPIV-1 hemagglutinin–neuraminidase (HN) glycoprotein, a potential target for antiviral therapy, we cloned and expressed a soluble portion of hPIV-1 HN (amino acid residues 137–575), lacking the N-terminal hydrophobic membrane anchorage region, in insect cells using the baculovirus secretion expression system. The expressed HN protein was purified through cation-exchange chromatography followed by metal affinity chromatography, using the 6×His epitope introduced at the carboxyl terminus of the recombinant protein. N-terminal amino acid sequence analysis of purified HN indicated that the honeybee melittin secretion signal peptide was correctly removed during post-translational processing. Further characterization revealed that the purified HN protein was N-glycosylated and exhibited neuraminidase activity whose characteristics resembled those of the native HN protein of hPIV-1 virions. The establishment of this expression and purification system has allowed us to further explore the biochemical characteristics of paramyxovirus HN and to obtain material that could be suitable for X-ray crystallography studies." @default.
• W2073194787 created "2016-06-24" @default.
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• W2073194787 date "2001-10-01" @default.
• W2073194787 modified "2023-10-18" @default.
• W2073194787 title "Expression and characterization of soluble human parainfluenza virus type 1 hemagglutinin–neuraminidase glycoprotein" @default.
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• W2073194787 doi "https://doi.org/10.1016/s0166-0934(01)00355-x" @default.
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