{"title":"Characterization of bacterial glycolipids in Pediococcus pentosaceus for fermented soybean paste (miso) and Tetragenococcus halophilus for soy sauce, in comparison with those in Lactobacillus, Streptococcus and Staphylococcus species.","authors":"Masao Iwamori, Kyoko Tanaka","doi":"10.1007/s10719-025-10190-1","DOIUrl":"https://doi.org/10.1007/s10719-025-10190-1","url":null,"abstract":"<p><p>Gram-positive bacterial biomembranes are composed of phosphatidyl glycerol (PG), cardiolipin (CL), and dihexaosyl diglycerides (DH-DG) as the major lipid constituents. The carbohydrate structures of DH-DG are specific to the particular bacterial species and we previously revealed them to have immunologically active properties. To characterize the species-structure relationship of glycolipids in Gram-positive bacteria, the structures of DH-DG in Pediococcus pentosaceus (PP) for producing fermented soybean paste (miso) and Tetragenococcus halophilus (TH) for soy sauce were determined in comparison with those in Lactobacillus, Streptococcus and Staphylococcus species. They were shown to be Glcα1-2Glcα1-3'DG (kojibiosyl DG) with 18:1(oleic acid) and 18:1 as the fatty acids for PP, and that with 16:0 (palmitic acid) and 18:1 for TH, and their carbohydrate structures were identical to that in Streptococcus salivarius, a symbiotic bacterium in the human oral cavity. Additionally, both bacteria contained an acidic glycolipid, in which glycerol phosphate was attached to the 6-position of the nonreducing terminal Glc residue of DH-DG. TLC immunostaining with human sera revealed antibodies to Galα1-2Glcα1-3'DG (LacDH-DG) from Lactobacillus species and Glcβ1-6Glcβ1-3'DG (StaDH-DG) from Staphylococcus species, but not to Glcα1-2Glcα1-3'DG (StrDH-DG) from Streptococcus species, in 2 out of 20 human sera. Given that one serum sample with anti-StaDH-DG antibodies was from a patient who had suffered from food poisoning due to Staphylococcus aureus 6 months previously, the antibodies to bacterial DH-DG were thought to have arisen via bacterial infection.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144636796","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Dorina Dobi, Alessandro Rimessi, Nicoletta Loberto, Laura Mauri, Rosaria Bassi, Elena Chiricozzi, Debora Olioso, Giulia Pellielo, Paolo Pinton, Valentino Bezzerri, Giulio Cabrini, Giuseppe Lippi, Anna Tamanini, Giulia Lunghi, Massimo Aureli
{"title":"Effects of GM1 ganglioside and its derivatives on ETI-rescued F508del-CFTR maturation and host-pathogen interactions in cystic fibrosis bronchial cells.","authors":"Dorina Dobi, Alessandro Rimessi, Nicoletta Loberto, Laura Mauri, Rosaria Bassi, Elena Chiricozzi, Debora Olioso, Giulia Pellielo, Paolo Pinton, Valentino Bezzerri, Giulio Cabrini, Giuseppe Lippi, Anna Tamanini, Giulia Lunghi, Massimo Aureli","doi":"10.1007/s10719-025-10191-0","DOIUrl":"https://doi.org/10.1007/s10719-025-10191-0","url":null,"abstract":"<p><p>Cystic Fibrosis (CF), a life-threatening hereditary disease, arises from mutations in the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) gene, which encodes a chloride-conducting channel widely expressed in epithelial cells. The most common mutation, F508del, causes CFTR misfolding, premature degradation, and impaired mucociliary clearance, leading to recurrent respiratory infections and inflammation. The triple combination therapy with Elexacaftor, Tezacaftor, and Ivacaftor (ETI) has revolutionized CF management by partially restoring mutated CFTR function. However, enhancing CFTR rescue and stabilizing host immune responses remain critical challenges. In airway epithelial cells, CFTR interacts with proteins and lipids in macromolecular complexes that influence its stability. Among these, the ganglioside GM1 plays a key role in modulating plasma membrane protein dynamics, including CFTR. This study investigates the effects of exogenous GM1 supplementation as an adjuvant to ETI treatment. Our results demonstrate that GM1 enhances F508del-CFTR maturation and stability, even under Pseudomonas aeruginosa infection, which typically suppresses CFTR expression and function. Furthermore, GM1 restores xenophagic activity in bronchial epithelial cells, improving host defence mechanisms against the bacteria. These findings underscore the therapeutic potential of GM1 and its analogues in optimizing the plasma membrane environment for CFTR correction, suggesting that by enhancing the efficacy of CFTR modulators, GM1 could pave the way for innovative approaches to improve CF management.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144636797","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Progress in research on DDOST dysregulation in related diseases.","authors":"Haoan Sun, Chunbao Xie","doi":"10.1007/s10719-025-10188-9","DOIUrl":"https://doi.org/10.1007/s10719-025-10188-9","url":null,"abstract":"<p><p>DDOST is an important subunit of N-glycosylated oligosaccharyltransferase and is closely related to protein N-glycosylation. Some studies have reported that abnormal expression of DDOST is associated with congenital disorders of glycosylation, solid tumours and other diseases. To better understand the progress of research on DDOST in diseases, we herein provide a comprehensive review of the basic functions of DDOST, interactions molecules, DDOST-congenital disorders of glycosylation (DDOST-CDG) and solid tumours. Our review findings will lay a foundation for researchers to better understand the functions of DDOST and to investigate its specific mechanisms of action.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144539989","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Makoto Kurihara, Yukinobu Goso, Rei Kawashima, Takafumi Ichikawa, Kazuhiko Ishihara
{"title":"Analysis of site-dependent mucins in rat intestinal mucosa using anti-glycan monoclonal antibodies.","authors":"Makoto Kurihara, Yukinobu Goso, Rei Kawashima, Takafumi Ichikawa, Kazuhiko Ishihara","doi":"10.1007/s10719-025-10187-w","DOIUrl":"https://doi.org/10.1007/s10719-025-10187-w","url":null,"abstract":"<p><p>Intestinal gel-forming mucins are high-molecular weight glycoproteins, and their glycan moieties vary depending on the intestinal site. Although the means of analyzing mucin glycans are limited, monoclonal antibodies are expected to be a powerful analysis tool. In this study, 12 monoclonal antibodies were generated using rat intestinal mucin as the immunogen, and the epitopes of the antibodies were studied. The analyses using resins with the glycans of blood group-associated antigens and neoglycolipids synthesized from mucin glycans revealed that most antibodies recognize glycans. Furthermore, some recognize blood group-related antigens on glycans, whereas others recognize immaturely synthesized mucin-type glycans. Immunostaining of the rat jejunum, ileum, proximal colon, and distal colon with antibodies produced a site-dependent staining intestinal image. Affinity chromatography using an antibody-conjugated column was utilized to fractionate rat small intestinal mucins. Mucins with various glycan compositions were produced, suggesting the possibility of obtaining site-specific mucins. The site-specific mucins with various glycan compositions result in site-specific glycan functions, and the antibodies developed in this study could be useful tools for their analysis.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-06-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144527580","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Maurice Michel, Benoit Stijlemans, Dana Michel, Monika Garg, Andreas Geissner, Peter H Seeberger, Daniel Varón Silva
{"title":"Detection of antibodies against the African parasite Trypanosoma brucei using synthetic glycosylphosphatidylinositol oligosaccharide fragments.","authors":"Maurice Michel, Benoit Stijlemans, Dana Michel, Monika Garg, Andreas Geissner, Peter H Seeberger, Daniel Varón Silva","doi":"10.1007/s10719-025-10186-x","DOIUrl":"https://doi.org/10.1007/s10719-025-10186-x","url":null,"abstract":"","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144475024","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Giulia Lunghi, Carola Pedroli, Ilaria Tagliabue, Dorina Dobi, Maria Grazia Ciampa, Laura Mauri, Laura Rouvière, Alexandre Henriques, Noelle Callizot, Sandro Sonnino, Elena Chiricozzi, Maria Fazzari
{"title":"GM1 oligosaccharide-mediated rescue in GBA-linked Parkinson's disease via modulation of lysosomal and mitochondrial dysfunctions.","authors":"Giulia Lunghi, Carola Pedroli, Ilaria Tagliabue, Dorina Dobi, Maria Grazia Ciampa, Laura Mauri, Laura Rouvière, Alexandre Henriques, Noelle Callizot, Sandro Sonnino, Elena Chiricozzi, Maria Fazzari","doi":"10.1007/s10719-025-10185-y","DOIUrl":"https://doi.org/10.1007/s10719-025-10185-y","url":null,"abstract":"<p><p>Mutations in the glucocerebrosidase GBA gene, encoding the lysosomal enzyme β-glucocerebrosidase, represent the most frequent genetic risk factor for Parkinson's disease, leading to lysosomal dysfunction, α-synuclein aggregation, and mitochondrial impairment. In this study, we investigated the therapeutic potential of GM1 ganglioside and its oligosaccharide portion (OligoGM1) in a cellular model of GBA-associated Parkinson's disease, using SH-SY5Y neuroblastoma cells carrying the L444P GBA mutation. We observed that both GM1 and OligoGM1 reduced α-synuclein accumulation and improved cell viability. Notably, only OligoGM1 attenuated lysosomal overload and restored mitophagy. Additionally, OligoGM1 significantly prevented 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced toxicity, including lysosomal dysfunction, reactive oxidative species-overproduction, and mitochondrial energy failure, whereas GM1 failed to provide protection. These findings highlight the selective and multifaceted neuroprotective actions of OligoGM1 under both genetic conditions and environmental stress. Due to its small, hydrophilic nature and capacity to cross the blood-brain barrier, OligoGM1 emerges as a promising therapeutic candidate for GBA-related and potentially idiopathic forms of Parkinson's Disease.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144215652","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Polina Obukhova, Nadezhda Shilova, Galina Pazynina, Svetlana Tsygankova, Inna Popova, Jacques Le Pendu, Nicolai Bovin
{"title":"Anti-GalNAcα (anti-Tn) antibody repertoire differs between individuals with blood groups A and B.","authors":"Polina Obukhova, Nadezhda Shilova, Galina Pazynina, Svetlana Tsygankova, Inna Popova, Jacques Le Pendu, Nicolai Bovin","doi":"10.1007/s10719-025-10184-z","DOIUrl":"https://doi.org/10.1007/s10719-025-10184-z","url":null,"abstract":"<p><p>Recently, Breiman et al. (2021) reported that the level of anti-Tn in the blood of healthy donors and COVID-19 patients is significantly lower in individuals of blood group A than B. This prompted us to look for qualitative differences in the repertoire of anti-Tn like specificity in individuals of different blood groups (BG). To this end, we isolated antibodies from the pooled sera of BG A and BG B healthy donors using GalNAcα-sepharose, followed by Printed Glycan Array analysis. As expected, antibodies affinity isolated from BG A donors completely lack species directed to canonical (GalNAcα-transferase dependent) A-glycans, such as A (types 1, 2 and 4), GalNAcα1-3(Fucα1-2)Gal, GalNAcα1-3Galβ1-4GlcNAc (linear A), and ALe<sup>Y</sup>. Unexpectedly, GalNAcα1-4Galβ1-4GlcNAc, glycan with an unnatural 1-4 bond fell into the same group, i.e., antibodies to it were found only in BG B donors. Other unexpected results include the following: (1) for GalNAcα1-OCH<sub>2</sub>CH(COOH)NH<sub>2</sub> (GalNAcα-OSer, immobilized by NH<sub>2</sub> group) the opposite result was observed, i.e. affinity isolated anti-Tn antibodies of BG A donors demonstrated significantly higher titer than of BG B; (2) in BG A donors, the level of antibodies to GalNGcα1-3GalNAcα (i.e. disaccharide in N-glycolyl form) is close to background, while there is a significant level of these antibodies in the BG B donors. Since antiglycan antibodies are known to play both a protective role in antimicrobial immunity and to promote infectivity, the knowledge gained about the difference in the specificity profiles of anti-Tn antibodies signals the need to take blood group into account in developing therapeutic strategies.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-04-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143997497","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Glycoconjugate JournalPub Date : 2025-04-01Epub Date: 2025-03-25DOI: 10.1007/s10719-025-10182-1
Heba A Hassan
{"title":"Exploring the impact of advanced glycation end products on diabetic salivary gland dysfunctions.","authors":"Heba A Hassan","doi":"10.1007/s10719-025-10182-1","DOIUrl":"10.1007/s10719-025-10182-1","url":null,"abstract":"<p><p>The role of Advanced Glycation End Products (AGEs) in the pathophysiology of salivary gland dysfunction in diabetes has not been fully addressed. In this work, we discuss the pathophysiological mechanisms of salivary gland dysfunctions in diabetes, focusing on the role of AGEs. Hyperglycemia induces the generation and accumulation of AGEs, induces oxidative stress, and activates the receptor for AGEs (RAGE), with detrimental effects on the salivary glands and the submandibular autonomic innervation. Structural and ultrastructural alterations have been described in the three major salivary glands, and hypo-salivation development has been linked to early autonomic neuropathy. Poor metabolic control aggravates the salivary flow rate via injury to the autonomic nerve fiber bundles or direct damage to the secretory acinar cells of the glands. Chronic hyperglycemia, the most crucial feature of diabetes, leads to the generation and accumulation of advanced glycation end products (AGEs). The interest in the role of AGEs in the pathogenesis of diabetic complications has grown exponentially, and AGEs have been implicated as a primary culprit in the pathophysiology of diabetes and its various complications, including neuropathy, nephropathy, retinopathy, vasculopathy, and cardiomyopathy.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":"97-106"},"PeriodicalIF":2.7,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143709557","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Glycoconjugate JournalPub Date : 2025-04-01Epub Date: 2025-02-19DOI: 10.1007/s10719-025-10179-w
Hemchandra Deka, Arabinda Ghosh, Debabrat Baishya
{"title":"Computational insights into DC-SIGN's enhanced recognition of mannotriose CPS units via Ca<sup>2+</sup> ion cross-talk.","authors":"Hemchandra Deka, Arabinda Ghosh, Debabrat Baishya","doi":"10.1007/s10719-025-10179-w","DOIUrl":"10.1007/s10719-025-10179-w","url":null,"abstract":"<p><p>The Carbohydrate Recognition Domain (CRD) of immune system's c-type lectin receptors (CLRs) preferentially interacts with the Capsular Polysaccharides (CPS) units. Implicit Ca<sup>2+</sup> ions are crucial to CRD function. Increment of the ionic concentration explicitly affects the CPS recognition by CRD many-fold. DC-SIGN is one such CLR that acts for the differential recognition of the microbial CPS. The CPS mannotriose had the lowest binding energy (ΔG -4.7 kcal/mol) and the maximum affinity for DC-SIGN with implicit Ca<sup>2+</sup> ion. In the present investigation the ligand affinity increases with the rise of Ca<sup>2+</sup> concentration up to 1.5 M. Again, within the CRD the residues viz; Glutamate (347), Proline (348), and Asparagine (349) (EPN) were reported previously as essential for CPS unit coordination. Our analysis demonstrated that besides the EPN residues, CPS unit interacts with the neighboring Asparagine (350), Glutamate (354) and Asparagine (355) residues. Thus, these residues were replaced one at a time with Alanine (a charge neutral residue) to test their effect on the contact event. The CRD loses its affinity for recognition on the N350A, E354A, and D355A substitutions. Thus, this heterogeneity of CRD recognition towards Carbohydrate provides fresh information about the immune system's theragnostic function. This new understanding of Ca<sup>2+</sup>-induced recognition may help design new theragnostic applications that boost our immune defenses against pathogenic evasion.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":"61-76"},"PeriodicalIF":2.7,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143448914","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Plant glycosides and glycosidases: classification, sources, and therapeutic insights in current medicine.","authors":"Kumaresan Kowsalya, Nandakumar Vidya, Jayachandran Halka, Jaganathan Sakthi Yazhini Preetha, Muthukrishnan Saradhadevi, Jesudass Joseph Sahayarayan, Packiaraj Gurusaravanan, Muthukrishnan Arun","doi":"10.1007/s10719-025-10180-3","DOIUrl":"10.1007/s10719-025-10180-3","url":null,"abstract":"<p><p>Plant glycosides have a broad spectrum of pharmaceutical activities primarily due to the glycosidic residues present in their structure. Especially, the therapeutic glycosides can be classified into many compounds based on the sugar moiety, chains/ saccharide units, glycosidic linkages, and aglycones. Among many classes, the widely used pharmacological classification is based on the aglycones linked to the glycoside molecule. Based on these non-sugar moiety (aglycones), plant glycosides are further classified into twelve different types of glycosides along with the recent discovery of novel (cannabinoid) glycosides. They are called alcoholic, anthraquinone, coumarin, chromone, cyanogenic, flavonoid, phenolic, cardiac, saponin, thio, steviol, iridoid, and cannabinoid glycosides. Each of the plant glycosides has been discussed in this paper with, origin, structure, and abundant presence in a specific family of plants. Besides, the therapeutic roles of these plant glycosides are further described in detail to validate their efficacies in the human health care system. On the other hand, glycosides are inactive until enzymatic hydrolysis releases their active aglycone, enabling targeted drug delivery. This process enhances aglycone solubility and stability, improving bioavailability and therapeutic efficacy. They target specific receptors or enzymes, minimizing off-target effects and enhancing pharmacological outcomes. Derived from plants, glycosides offer diverse chemical structures for drug development. They are integral to traditional medicine and modern pharmaceuticals, utilized in therapies ranging from cardiology to antimicrobial treatments.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":"107-124"},"PeriodicalIF":2.7,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143482972","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}