Insect cells are used routinely to express recombinant mammalian glycoproteins. However, insect protein glycosylation pathways are not well understood and appear to differ from those of mammalian cells. One way to more clearly evaluate the protein glycosylation potential of insect cells is to use the Drosophila melanogaster genome to identify genes that might encode relevant functions. These genes can then be expressed and the functions of the gene products directly evaluated by biochemical assays. In this study, we used this approach to determine the function of a putative Drosophila nucleotide sugar transporter gene. The results showed that this gene encodes a protein that can transport UDP-galactose, but not CMP-sialic acid. Thus, Drosophila encodes at least some of the infrastructure needed to produce glycoproteins with complex glycans, but this particular gene product does not directly support glycoprotein sialylation. These findings are relevant to insect cell biology and to an informed consideration of insect cell expression systems as tools for recombinant glycoprotein production.
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http://dx.doi.org/10.1016/s1046-5928(02)00550-8 | DOI Listing |
Front Immunol
December 2024
Medical Genetic Institute of Henan Province, Henan Key Laboratory of Genetic Diseases and Functional Genomics, National Health Commission Key Laboratory of Birth Defects Prevention, Henan Provincial People's Hospital, People's Hospital of Zhengzhou University, Zhengzhou University, Zhengzhou, Henan, China.
Sialylation is a typical final step of glycosylation, which is a prevalent post-translational modification of proteins. Sialoglycans, the products of sialylation, are located on the outmost of cells and participate in pivotal biological processes. They have been identified as glyco-immune checkpoints and are currently under rigorous investigation in the field of tumor research.
View Article and Find Full Text PDFFront Pharmacol
December 2024
Department of Pharmacy, The First Affiliated Hospital of Chongqing Medical University, Chongqing, China.
Introduction: In the last decades, the recombinant tissue plasminogen activator alteplase has been the standard fibrinolytic treatment of acute myocardial infarction, pulmonary embolism, and acute ischemic stroke. An optimized version of alteplase, tenecteplase, has been developed by exchanging six amino acids to increase half-life, achieve higher fibrin selectivity and increase resistance to plasminogen activator inhibitor-1. Meanwhile, several products containing tenecteplase exist.
View Article and Find Full Text PDFFood Chem X
January 2025
Department of Nutrition, University of Nevada, Reno, Reno, NV 89557, USA.
The glycomes of bovine whey, egg white, pea, and soy protein isolates are described here. -glycans from four protein isolates were analyzed by HILIC high performance liquid chromatography and quadrupole time-of-flight tandem mass spectrometry (HILIC-FLD-QTOF-MS/MS). In total, 33 glycans from bovine whey and egg white and 10 -glycans from soy and pea glycoproteins were identified.
View Article and Find Full Text PDFVirulence
December 2025
College of Veterinary Medicine, Northeast Agricultural University, Harbin, PR China.
Porcine deltacoronavirus (PDCoV) is increasingly prevalent in newborn piglets with diarrhea. With the development of research on the virus and the feasibility of PDCoV cross-species transmission, the biosafety and the development of pig industry have been greatly affected. In this study, a PDCoV strain CH/LNFX/2022 was isolated from diarrheal newborn piglets at a farm in China.
View Article and Find Full Text PDFOrg Biomol Chem
January 2025
School of Pharmaceutical Science and Technology, Hangzhou Institute of Advanced Study, Hangzhou 310024, China.
Glycosite-specific antibody-drug conjugates (gsADCs), which carry cytotoxic payloads at the conserved -glycosylation site, N297, of an IgG, have emerged as a promising ADC format with better therapeutic index. Conjugating the payloads aldehyde-based chemistry is more friendly to IgGs, and has been widely investigated. However, the efficiency of introducing an aldehyde tag at the N297 site is poor due to the complicated procedures required, such as the multiple-enzyme-catalyzed IgG glycoengineering process and the successive oxidation step, which always results in heterogeneous products and poor stability.
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