Cancer cells and viruses share common glycoepitopes: exciting opportunities toward combined treatments

Aberrant glycosylation patterns of glycoproteins and glycolipids have long been recognized as one the major hallmarks of cancer cells that has led to numerous glycoconjugate vaccine attempts. These abnormal glycosylation profiles mostly originate from the lack of key glycosyltransferases activities,...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	René Roy [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2024

Schlagwörter:	O-glycans vaccines cancer viruses glycobiology glycoepitopes

Übergeordnetes Werk:	In: Frontiers in Immunology - Frontiers Media S.A., 2011, 15(2024)
Übergeordnetes Werk:	volume:15 ; year:2024

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fimmu.2024.1292588

Katalog-ID:	DOAJ101450966

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allfieldsSound	10.3389/fimmu.2024.1292588 doi (DE-627)DOAJ101450966 (DE-599)DOAJebfd6b9a0a664eaa824981387ce7e2c0 DE-627 ger DE-627 rakwb eng RC581-607 René Roy verfasserin aut Cancer cells and viruses share common glycoepitopes: exciting opportunities toward combined treatments 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Aberrant glycosylation patterns of glycoproteins and glycolipids have long been recognized as one the major hallmarks of cancer cells that has led to numerous glycoconjugate vaccine attempts. These abnormal glycosylation profiles mostly originate from the lack of key glycosyltransferases activities, mutations, over expressions, or modifications of the requisite chaperone for functional folding. Due to their relative structural simplicity, O-linked glycans of the altered mucin family of glycoproteins have been particularly attractive in the design of tumor associated carbohydrate-based vaccines. Several such glycoconjugate vaccine formulations have generated potent monoclonal anti-carbohydrate antibodies useful as diagnostic and immunotherapies in the fight against cancer. Paradoxically, glycoproteins related to enveloped viruses also express analogous N- and O-linked glycosylation patterns. However, due to the fact that viruses are not equipped with the appropriate glycosyl enzyme machinery, they need to hijack that of the infected host cells. Although the resulting N-linked glycans are very similar to those of normal cells, some of their O-linked glycan patterns often share the common structural simplicity to those identified on tumor cells. Consequently, given that both cancer cells and viral glycoproteins share both common N- and O-linked glycoepitopes, glycoconjugate vaccines could be highly attractive to generate potent immune responses to target both conditions. O-glycans vaccines cancer viruses glycobiology glycoepitopes Immunologic diseases. Allergy In Frontiers in Immunology Frontiers Media S.A., 2011 15(2024) (DE-627)657998354 (DE-600)2606827-8 16643224 nnns volume:15 year:2024 https://doi.org/10.3389/fimmu.2024.1292588 kostenfrei https://doaj.org/article/ebfd6b9a0a664eaa824981387ce7e2c0 kostenfrei https://www.frontiersin.org/articles/10.3389/fimmu.2024.1292588/full kostenfrei https://doaj.org/toc/1664-3224 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 15 2024
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callnumber-first	R - Medicine
author	René Roy
spellingShingle	René Roy misc RC581-607 misc O-glycans misc vaccines misc cancer misc viruses misc glycobiology misc glycoepitopes misc Immunologic diseases. Allergy Cancer cells and viruses share common glycoepitopes: exciting opportunities toward combined treatments
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topic_title	RC581-607 Cancer cells and viruses share common glycoepitopes: exciting opportunities toward combined treatments O-glycans vaccines cancer viruses glycobiology glycoepitopes
topic	misc RC581-607 misc O-glycans misc vaccines misc cancer misc viruses misc glycobiology misc glycoepitopes misc Immunologic diseases. Allergy
topic_unstemmed	misc RC581-607 misc O-glycans misc vaccines misc cancer misc viruses misc glycobiology misc glycoepitopes misc Immunologic diseases. Allergy
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title	Cancer cells and viruses share common glycoepitopes: exciting opportunities toward combined treatments
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title_full	Cancer cells and viruses share common glycoepitopes: exciting opportunities toward combined treatments
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title_sort	cancer cells and viruses share common glycoepitopes: exciting opportunities toward combined treatments
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title_auth	Cancer cells and viruses share common glycoepitopes: exciting opportunities toward combined treatments
abstract	Aberrant glycosylation patterns of glycoproteins and glycolipids have long been recognized as one the major hallmarks of cancer cells that has led to numerous glycoconjugate vaccine attempts. These abnormal glycosylation profiles mostly originate from the lack of key glycosyltransferases activities, mutations, over expressions, or modifications of the requisite chaperone for functional folding. Due to their relative structural simplicity, O-linked glycans of the altered mucin family of glycoproteins have been particularly attractive in the design of tumor associated carbohydrate-based vaccines. Several such glycoconjugate vaccine formulations have generated potent monoclonal anti-carbohydrate antibodies useful as diagnostic and immunotherapies in the fight against cancer. Paradoxically, glycoproteins related to enveloped viruses also express analogous N- and O-linked glycosylation patterns. However, due to the fact that viruses are not equipped with the appropriate glycosyl enzyme machinery, they need to hijack that of the infected host cells. Although the resulting N-linked glycans are very similar to those of normal cells, some of their O-linked glycan patterns often share the common structural simplicity to those identified on tumor cells. Consequently, given that both cancer cells and viral glycoproteins share both common N- and O-linked glycoepitopes, glycoconjugate vaccines could be highly attractive to generate potent immune responses to target both conditions.
abstractGer	Aberrant glycosylation patterns of glycoproteins and glycolipids have long been recognized as one the major hallmarks of cancer cells that has led to numerous glycoconjugate vaccine attempts. These abnormal glycosylation profiles mostly originate from the lack of key glycosyltransferases activities, mutations, over expressions, or modifications of the requisite chaperone for functional folding. Due to their relative structural simplicity, O-linked glycans of the altered mucin family of glycoproteins have been particularly attractive in the design of tumor associated carbohydrate-based vaccines. Several such glycoconjugate vaccine formulations have generated potent monoclonal anti-carbohydrate antibodies useful as diagnostic and immunotherapies in the fight against cancer. Paradoxically, glycoproteins related to enveloped viruses also express analogous N- and O-linked glycosylation patterns. However, due to the fact that viruses are not equipped with the appropriate glycosyl enzyme machinery, they need to hijack that of the infected host cells. Although the resulting N-linked glycans are very similar to those of normal cells, some of their O-linked glycan patterns often share the common structural simplicity to those identified on tumor cells. Consequently, given that both cancer cells and viral glycoproteins share both common N- and O-linked glycoepitopes, glycoconjugate vaccines could be highly attractive to generate potent immune responses to target both conditions.
abstract_unstemmed	Aberrant glycosylation patterns of glycoproteins and glycolipids have long been recognized as one the major hallmarks of cancer cells that has led to numerous glycoconjugate vaccine attempts. These abnormal glycosylation profiles mostly originate from the lack of key glycosyltransferases activities, mutations, over expressions, or modifications of the requisite chaperone for functional folding. Due to their relative structural simplicity, O-linked glycans of the altered mucin family of glycoproteins have been particularly attractive in the design of tumor associated carbohydrate-based vaccines. Several such glycoconjugate vaccine formulations have generated potent monoclonal anti-carbohydrate antibodies useful as diagnostic and immunotherapies in the fight against cancer. Paradoxically, glycoproteins related to enveloped viruses also express analogous N- and O-linked glycosylation patterns. However, due to the fact that viruses are not equipped with the appropriate glycosyl enzyme machinery, they need to hijack that of the infected host cells. Although the resulting N-linked glycans are very similar to those of normal cells, some of their O-linked glycan patterns often share the common structural simplicity to those identified on tumor cells. Consequently, given that both cancer cells and viral glycoproteins share both common N- and O-linked glycoepitopes, glycoconjugate vaccines could be highly attractive to generate potent immune responses to target both conditions.
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title_short	Cancer cells and viruses share common glycoepitopes: exciting opportunities toward combined treatments
url	https://doi.org/10.3389/fimmu.2024.1292588 https://doaj.org/article/ebfd6b9a0a664eaa824981387ce7e2c0 https://www.frontiersin.org/articles/10.3389/fimmu.2024.1292588/full https://doaj.org/toc/1664-3224
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