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Glycosylation Modification in Immune Diseases
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Glycosylation Modification in Immune Diseases

A special issue of Journal of Clinical Medicine (ISSN 2077-0383). This special issue belongs to the section "Immunology".

Deadline for manuscript submissions: closed (1 June 2021) | Viewed by 19557

Special Issue Editor

Prof. Dr. Friedrich Altmann

E-Mail Website
Guest Editor
Department of Chemistry, University of Natural Resources and Life Sciences Vienna, Vienna, Austria
Interests: immunogenicity of non-human glycans; analytical glycobiology

Special Issue Information

Dear Colleagues,

These days, we are more than aware of the vitally important role of a well-functioning immune system. Humoral and cellular components constantly act and cooperate to detect and remove pathogenic entities from tumor cells to fungi, bacteria and—most obvious at present—viruses. The first line of contact of these unpleasant encounters very often involves carbohydrates. The glyco-calix of pathogens can be a target for or represent a form of protection against the host’s immune system. In fact, a large part of the innate immune system is directed against non-self-carbohydrate structures. Cell wall glycosylation of host cells can serve as a receptor for virus entry or bacterial adhesion. Most soluble components of the immune system, on the other hand, are glycosylated proteins, whose exact glycan pattern can modulate their physiological efficacy.

The Special Issue “Glycosylation Modification in Immune Diseases” will gather front-line original research as well as topical reviews on the role of protein and cell wall glycosylation on the function of immune system components in health and in acute and chronic disease, including aging-related conditions. Particularly welcome will be insights into the role of defined glycan features in immune diseases and in changes of glycosylation triggered by immune processes.

Prof. Dr. Friedrich Altmann
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Journal of Clinical Medicine is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • glycoproteins
  • glycolipids
  • carbohydrate binding proteins
  • innate immunity
  • glycomics
  • mammalian lectins (selectins, galectins, siglecs, and others)

Published Papers (5 papers)

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Research

18 pages, 2695 KiB  
Article
Serum N-Glycomics Stratifies Bacteremic Patients Infected with Different Pathogens
by Sayantani Chatterjee, Rebeca Kawahara, Harry C. Tjondro, David R. Shaw, Marni A. Nenke, David J. Torpy and Morten Thaysen-Andersen
J. Clin. Med. 2021, 10(3), 516; https://doi.org/10.3390/jcm10030516 - 1 Feb 2021
Cited by 11 | Viewed by 3956
Abstract
Bacteremia—i.e., the presence of pathogens in the blood stream—is associated with long-term morbidity and is a potential precursor condition to life-threatening sepsis. Timely detection of bacteremia is therefore critical to reduce patient mortality, but existing methods lack precision, speed, and sensitivity to effectively [...] Read more.
Bacteremia—i.e., the presence of pathogens in the blood stream—is associated with long-term morbidity and is a potential precursor condition to life-threatening sepsis. Timely detection of bacteremia is therefore critical to reduce patient mortality, but existing methods lack precision, speed, and sensitivity to effectively stratify bacteremic patients. Herein, we tested the potential of quantitative serum N-glycomics performed using porous graphitized carbon liquid chromatography tandem mass spectrometry to stratify bacteremic patients infected with Escherichia coli (n = 11), Staphylococcus aureus (n = 11), Pseudomonas aeruginosa (n = 5), and Streptococcus viridans (n = 5) from healthy donors (n = 39). In total, 62 N-glycan isomers spanning 41 glycan compositions primarily comprising complex-type core fucosylated, bisecting N-acetylglucosamine (GlcNAc), and α2,3-/α2,6-sialylated structures were profiled across all samples using label-free quantitation. Excitingly, unsupervised hierarchical clustering and principal component analysis of the serum N-glycome data accurately separated the patient groups. P. aeruginosa-infected patients displayed prominent N-glycome aberrations involving elevated levels of fucosylation and bisecting GlcNAcylation and reduced sialylation relative to other bacteremic patients. Notably, receiver operating characteristic analyses demonstrated that a single N-glycan isomer could effectively stratify each of the four bacteremic patient groups from the healthy donors (area under the curve 0.93–1.00). Thus, the serum N-glycome represents a new hitherto unexplored class of potential diagnostic markers for bloodstream infections. Full article
(This article belongs to the Special Issue Glycosylation Modification in Immune Diseases)
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13 pages, 1744 KiB  
Article
Glycation Increases the Risk of Microbial Traversal through an Endothelial Model of the Human Blood-Brain Barrier after Use of Anesthetics
by Veronika Weber, Heidi Olzscha, Timo Längrich, Carla Hartmann, Matthias Jung, Britt Hofmann, Rüdiger Horstkorte and Kaya Bork
J. Clin. Med. 2020, 9(11), 3672; https://doi.org/10.3390/jcm9113672 - 16 Nov 2020
Cited by 5 | Viewed by 2153
Abstract
The function of the human blood–brain barrier (BBB), consisting mainly of the basement membrane and microvascular endothelial cells, is to protect the brain and regulate its metabolism. Dysfunction of the BBB can lead to increased permeability, which can be linked with several pathologies, [...] Read more.
The function of the human blood–brain barrier (BBB), consisting mainly of the basement membrane and microvascular endothelial cells, is to protect the brain and regulate its metabolism. Dysfunction of the BBB can lead to increased permeability, which can be linked with several pathologies, including meningitis, sepsis, and postoperative delirium. Advanced glycation end products (AGE) are non-enzymatic, posttranslational modifications of proteins, which can affect their function. Increased AGE levels are strongly associated with ageing and degenerative diseases including diabetes. Several studies demonstrated that the formation of AGE interfere with the function of the BBB and may change its permeability for soluble compounds. However, it is still unclear whether AGE can facilitate microbial traversal through the BBB and how small compounds including anesthetics modulate this process. Therefore, we developed a cellular model, which allows for the convenient testing of different factors and compounds with a direct correlation to bacterial traversal through the BBB. Our results demonstrate that both glycation and anesthetics interfere with the function of the BBB and promote microbial traversal. Importantly, we also show that the essential nutrient and antioxidant ascorbic acid, commonly known as vitamin C, can reduce the microbial traversal through the BBB and partly reverse the effects of AGE. Full article
(This article belongs to the Special Issue Glycosylation Modification in Immune Diseases)
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30 pages, 3690 KiB  
Article
New Insights into Immunological Involvement in Congenital Disorders of Glycosylation (CDG) from a People-Centric Approach
by Rita Francisco, Carlota Pascoal, Dorinda Marques-da-Silva, Sandra Brasil, Fernando M. Pimentel-Santos, Ruqaiah Altassan, Jaak Jaeken, Ana Rita Grosso, Vanessa dos Reis Ferreira and Paula A. Videira
J. Clin. Med. 2020, 9(7), 2092; https://doi.org/10.3390/jcm9072092 - 3 Jul 2020
Cited by 21 | Viewed by 6038
Abstract
Congenital disorders of glycosylation (CDG) are rare diseases with variable phenotypes and severity. Immunological involvement remains a largely uncharted topic in CDG, mainly due to lack of robust data. To better characterize immune-related manifestations’ prevalence, relevance, and quality-of-life (QoL) impact, we developed electronic [...] Read more.
Congenital disorders of glycosylation (CDG) are rare diseases with variable phenotypes and severity. Immunological involvement remains a largely uncharted topic in CDG, mainly due to lack of robust data. To better characterize immune-related manifestations’ prevalence, relevance, and quality-of-life (QoL) impact, we developed electronic questionnaires targeting (1) CDG patients and (2) the general “healthy” population. Two-hundred and nine CDG patients/caregivers and 349 healthy participants were included in this study. PMM2-CDG was the most represented CDG (n = 122/209). About half of these participants (n = 65/122) described relevant infections with a noteworthy prevalence of those affecting the gastrointestinal tract (GI) (63.1%, n = 41/65). Infection burden and QoL impact were shown as infections correlated with more severe clinical phenotypes and with a set of relevant non-immune PMM2-CDG signs. Autoimmune diseases had only a marginal presence in PMM2-CDG (2.5%, n = 3/122), all being GI-related. Allergy prevalence was also low in PMM2-CDG (33%, n = 41/122) except for food allergies (26.8%, n = 11/41, of PMM2-CDG and 10.8%, n = 17/158, of controls). High vaccination compliance with greater perceived ineffectiveness (28.3%, n = 17/60) and more severe adverse reactions were described in PMM2-CDG. This people-centric approach not only confirmed literature findings, but created new insights into immunological involvement in CDG, namely by highlighting the possible link between the immune and GI systems in PMM2-CDG. Finally, our results emphasized the importance of patient/caregiver knowledge and raised several red flags about immunological management. Full article
(This article belongs to the Special Issue Glycosylation Modification in Immune Diseases)
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12 pages, 831 KiB  
Article
Sialylation of Human Natural Killer (NK) Cells Is Regulated by IL-2
by Philip Rosenstock, Kaya Bork, Chiara Massa, Philipp Selke, Barbara Seliger and Rüdiger Horstkorte
J. Clin. Med. 2020, 9(6), 1816; https://doi.org/10.3390/jcm9061816 - 11 Jun 2020
Cited by 9 | Viewed by 2840
Abstract
Sialic acids are terminal sugars on the cell surface that are found on all cell types including immune cells like natural killer (NK) cells. The attachment of sialic acids to different glycan structures is catalyzed by sialyltransferases in the Golgi. However, the expression [...] Read more.
Sialic acids are terminal sugars on the cell surface that are found on all cell types including immune cells like natural killer (NK) cells. The attachment of sialic acids to different glycan structures is catalyzed by sialyltransferases in the Golgi. However, the expression pattern of sialyltransferases in NK cells and their expression after activation has not yet been analyzed. Therefore, the present study determines which sialyltransferases are expressed in human NK cells and if activation with IL-2 changes the sialylation of NK cells. The expression of sialyltransferases was analyzed in the three human NK cell lines NK-92, NKL, KHYG-1 and primary NK cells. NK-92 cells were cultured in the absence or presence of IL-2, and changes in the sialyltransferase expression were measured by qPCR. Furthermore, specific sialylation was investigated by flow cytometry. In addition, polySia and NCAM were measured by Western blot analyses. IL-2 leads to a reduced expression of ST8SIA1, ST6GAL1 and ST3GAL1. α-2,3-Sialylation remained unchanged, while α-2,6-sialylation was increased after IL-2 stimulation. Moreover, an increase in the amount of NCAM and polySia was observed in IL-2-activated NK cells, whereas GD3 ganglioside was decreased. In this study, all sialyltransferases that were expressed in NK cells could be identified. IL-2 regulates the expression of some sialyltransferases and leads to changes in the sialylation of NK cells. Full article
(This article belongs to the Special Issue Glycosylation Modification in Immune Diseases)
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14 pages, 1989 KiB  
Article
N-Glycosylation Alteration of Serum and Salivary Immunoglobulin A Is a Possible Biomarker in Oral Mucositis
by Enikő Gebri, Zsuzsanna Kovács, Brigitta Mészáros, Ferenc Tóth, Ádám Simon, Hajnalka Jankovics, Ferenc Vonderviszt, Attila Kiss, András Guttman and Tibor Hortobágyi
J. Clin. Med. 2020, 9(6), 1747; https://doi.org/10.3390/jcm9061747 - 5 Jun 2020
Cited by 7 | Viewed by 3913
Abstract
Background: Oral and enteral mucositis due to high-dose cytostatic treatment administered during autologous and allogeneic stem-cell transplantation increases mortality. Salivary secretory immunoglobulin A (sIgA) is a basic pillar of local immunity in the first line of defense. Altered salivary sialoglycoprotein carbohydrates are important [...] Read more.
Background: Oral and enteral mucositis due to high-dose cytostatic treatment administered during autologous and allogeneic stem-cell transplantation increases mortality. Salivary secretory immunoglobulin A (sIgA) is a basic pillar of local immunity in the first line of defense. Altered salivary sialoglycoprotein carbohydrates are important in the pathologies in the oral cavity including inflammation, infection and neoplasia. Therefore, we assessed whether changes in the salivary and serum IgA glycosylation correlated with development and severity of oral mucositis. Methods: Using capillary electrophoresis, comparative analysis of serum and salivary IgA total N-glycans was conducted in 8 patients with autologous peripheral stem-cell transplantation (APSCT) at four different stages of transplantation (day −3/−7, 0, +7, +14) and in 10 healthy controls. Results: Fourteen out of the 31 structures identified in serum and 6 out of 38 in saliva showed significant changes upon transplantation compared with the control group. Only serum core fucosylated, sialylated bisecting biantennary glycan (FA2BG2S2) showed significant differences between any two stages of transplantation (day −3/−7 and day +14; p = 0.0279). Conclusion: Our results suggest that changes in the serum IgA total N-glycan profile could serve as a disease-specific biomarker in patients undergoing APSCT, while analysis of salivary IgA N-glycan reflects the effect of APSCT on local immunity. Full article
(This article belongs to the Special Issue Glycosylation Modification in Immune Diseases)
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