Mucin-type O-glycosylation and its potential use in drug and vaccine development - PubMed (original) (raw)
Review
. 2008 Mar;1780(3):546-63.
doi: 10.1016/j.bbagen.2007.09.010. Epub 2007 Sep 25.
Affiliations
- PMID: 17988798
- DOI: 10.1016/j.bbagen.2007.09.010
Review
Mucin-type O-glycosylation and its potential use in drug and vaccine development
Mads Agervig Tarp et al. Biochim Biophys Acta. 2008 Mar.
Abstract
Mucin-type O-glycans are found on mucins as well as many other glycoproteins. The initiation step in synthesis is catalyzed by a large family of polypeptide GalNAc-transferases attaching the first carbohydrate residue, GalNAc, to selected serine and threonine residues in proteins. During the last decade an increasing number of GalNAc-transferase isoforms have been cloned and their substrate-specificities partly characterized. These differences in substrate specificities have been exploited for in vitro site-directed O-glycosylation. In GlycoPEGylation, polyehylene glycol (PEG) is transferred to recombinant therapeutics to specific acceptor sites directed by GalNAc-transferases. GalNAc-transferases have also been used to control density of glycosylation in the development of glycopeptide-based cancer vaccines. The membrane-associated mucin-1 (MUC1) has long been considered a target for immunotherapeutic and immunodiagnostic measures, since it is highly overexpressed and aberrantly O-glycosylated in most adenocarcinomas, including breast, ovarian, and pancreatic cancers. By using vaccines mimicking the glycosylation pattern of cancer-cells, it is possible to overcome tolerance in transgenic animals expressing the human MUC1 protein as a self-antigen providing important clues for an improved MUC1 vaccine design. The present review will highlight some of the potential applications of site-directed O-glycosylation.
Similar articles
- Unexpected tolerance of glycosylation by UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase revealed by electron capture dissociation mass spectrometry: carbohydrate as potential protective groups.
Yoshimura Y, Matsushita T, Fujitani N, Takegawa Y, Fujihira H, Naruchi K, Gao XD, Manri N, Sakamoto T, Kato K, Hinou H, Nishimura S. Yoshimura Y, et al. Biochemistry. 2010 Jul 20;49(28):5929-41. doi: 10.1021/bi100623g. Biochemistry. 2010. PMID: 20540529 - An efficient approach for the characterization of mucin-type glycopeptides: the effect of O-glycosylation on the conformation of synthetic mucin peptides.
Hashimoto R, Fujitani N, Takegawa Y, Kurogochi M, Matsushita T, Naruchi K, Ohyabu N, Hinou H, Gao XD, Manri N, Satake H, Kaneko A, Sakamoto T, Nishimura S. Hashimoto R, et al. Chemistry. 2011 Feb 18;17(8):2393-404. doi: 10.1002/chem.201002754. Epub 2011 Jan 24. Chemistry. 2011. PMID: 21264968 - The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation.
Wandall HH, Irazoqui F, Tarp MA, Bennett EP, Mandel U, Takeuchi H, Kato K, Irimura T, Suryanarayanan G, Hollingsworth MA, Clausen H. Wandall HH, et al. Glycobiology. 2007 Apr;17(4):374-87. doi: 10.1093/glycob/cwl082. Epub 2007 Jan 10. Glycobiology. 2007. PMID: 17215257 - Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family.
Bennett EP, Mandel U, Clausen H, Gerken TA, Fritz TA, Tabak LA. Bennett EP, et al. Glycobiology. 2012 Jun;22(6):736-56. doi: 10.1093/glycob/cwr182. Epub 2011 Dec 18. Glycobiology. 2012. PMID: 22183981 Free PMC article. Review. - O-glycosylation of the mucin type.
Hanisch FG. Hanisch FG. Biol Chem. 2001 Feb;382(2):143-9. doi: 10.1515/BC.2001.022. Biol Chem. 2001. PMID: 11308013 Review.
Cited by
- Characterization of cancer associated mucin type O-glycans using the exchange sialylation properties of mammalian sialyltransferase ST3Gal-II.
Chandrasekaran EV, Xue J, Xia J, Locke RD, Patil SA, Neelamegham S, Matta KL. Chandrasekaran EV, et al. J Proteome Res. 2012 Apr 6;11(4):2609-18. doi: 10.1021/pr201108q. Epub 2012 Feb 29. J Proteome Res. 2012. PMID: 22329400 Free PMC article. - Chemoenzymatic Methods for the Synthesis of Glycoproteins.
Li C, Wang LX. Li C, et al. Chem Rev. 2018 Sep 12;118(17):8359-8413. doi: 10.1021/acs.chemrev.8b00238. Epub 2018 Aug 24. Chem Rev. 2018. PMID: 30141327 Free PMC article. Review. - Sweet and sour: the impact of differential glycosylation in cancer cells undergoing epithelial-mesenchymal transition.
Freire-de-Lima L. Freire-de-Lima L. Front Oncol. 2014 Mar 25;4:59. doi: 10.3389/fonc.2014.00059. eCollection 2014. Front Oncol. 2014. PMID: 24724053 Free PMC article. Review. - Classification of Tandem Mass Spectra for Identification of N- and O-linked Glycopeptides.
Toghi Eshghi S, Yang W, Hu Y, Shah P, Sun S, Li X, Zhang H. Toghi Eshghi S, et al. Sci Rep. 2016 Nov 21;6:37189. doi: 10.1038/srep37189. Sci Rep. 2016. PMID: 27869200 Free PMC article. - Structure-guided engineering of the affinity and specificity of CARs against Tn-glycopeptides.
Sharma P, Marada VVVR, Cai Q, Kizerwetter M, He Y, Wolf SP, Schreiber K, Clausen H, Schreiber H, Kranz DM. Sharma P, et al. Proc Natl Acad Sci U S A. 2020 Jun 30;117(26):15148-15159. doi: 10.1073/pnas.1920662117. Epub 2020 Jun 15. Proc Natl Acad Sci U S A. 2020. PMID: 32541028 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous