ijms-logo

Journal Browser

Journal Browser

Carbohydrate Recognition in the Immune System

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Immunology".

Deadline for manuscript submissions: closed (31 December 2020) | Viewed by 6101

Special Issue Editors


E-Mail Website
Guest Editor
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), University of Lille, CNRS, UMR 8576, 59658 Villeneuve d’Ascq, France
Interests: glycobiology; microbiome; adhesin; carbohydrate; glycoprotein; host-pathogen interactions
Gastroenterology Unit, Department of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Liverpool L69 3GE, UK
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Carbohydrate recognition plays a vital role in the activation and function of the immune system, but has remained understudied for the important reason that carbohydrates alone cannot bind thymus cells to activate B-cells to produce the highly specialized and matured immunoglobulin-G antibodies. Nevertheless, the immune system has developed an alternative and more intricate biology for the self-activation of B-cells, which largely manifests via the clustering of exogenous glycan antigenic structures on viruses, bacteria, and other intruders, or via the recognition of rare glycosylation signatures on our own cells for remediation purposes. With the advance of modern analytical techniques in glycoproteomics, a growing collection of rare glycan structures are being discovered, localized, and linked to diseases. Tumor-associated carbohydrate antigens found in metaplastic tissues, such as the embryonal Lex antigen in breast cancer, LacdiNAc in human gastric mucosa, and paucimannosidic glycans in pancreatic and colon cancer, are examples of known targets for lectins of pathogenic microorganisms, but also of carbohydrate-binding antibodies. However, our understanding about how our immune system and our microbiome react to aberrant glycosylation patterns on proteins and cells is still in its infancy.

In this Special Issue, we will focus on recent and rapidly growing progress in our knowledge of carbohydrate recognition in the immune system, by both exogenous and endogenous lectins and antibodies.

Dr. Julie Bouckaert
Dr. Lu-Gang Yu
Guest Editors

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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • immune system
  • glycosylation signature
  • protein-carbohydrate interaction
  • tumor-associated carbohydrate antigen
  • lectin
  • carbohydrate-binding antibody

Published Papers (2 papers)

Order results
Result details
Select all
Export citation of selected articles as:

Research

20 pages, 3146 KiB  
Article
Escherichia coli O157:H7 F9 Fimbriae Recognize Plant Xyloglucan and Elicit a Response in Arabidopsis thaliana
by Ashleigh Holmes, Yannick Rossez, Kathryn Mary Wright, Pete Edward Hedley, Jenny Morris, William George Tycho Willats and Nicola Jean Holden
Int. J. Mol. Sci. 2020, 21(24), 9720; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21249720 - 19 Dec 2020
Cited by 3 | Viewed by 2292
Abstract
Fresh produce is often a source of enterohaemorrhagic Escherichia coli (EHEC) outbreaks. Fimbriae are extracellular structures involved in cell-to-cell attachment and surface colonisation. F9 (Fml) fimbriae have been shown to be expressed at temperatures lower than 37 °C, implying a function beyond the [...] Read more.
Fresh produce is often a source of enterohaemorrhagic Escherichia coli (EHEC) outbreaks. Fimbriae are extracellular structures involved in cell-to-cell attachment and surface colonisation. F9 (Fml) fimbriae have been shown to be expressed at temperatures lower than 37 °C, implying a function beyond the mammalian host. We demonstrate that F9 fimbriae recognize plant cell wall hemicellulose, specifically galactosylated side chains of xyloglucan, using glycan arrays. E. coli expressing F9 fimbriae had a positive advantage for adherence to spinach hemicellulose extract and tissues, which have galactosylated oligosaccharides as recognized by LM24 and LM25 antibodies. As fimbriae are multimeric structures with a molecular pattern, we investigated whether F9 fimbriae could induce a transcriptional response in model plant Arabidopsis thaliana, compared with flagella and another fimbrial type, E. coli common pilus (ECP), using DNA microarrays. F9 induced the differential expression of 435 genes, including genes involved in the plant defence response. The expression of F9 at environmentally relevant temperatures and its recognition of plant xyloglucan adds to the suite of adhesins EHEC has available to exploit the plant niche. Full article
(This article belongs to the Special Issue Carbohydrate Recognition in the Immune System)
Show Figures

Figure 1

16 pages, 7816 KiB  
Article
Characterization of Asparagine Deamidation in Immunodominant Myelin Oligodendrocyte Glycoprotein Peptide Potential Immunotherapy for the Treatment of Multiple Sclerosis
by Maria-Eleni Androutsou, Agathi Nteli, Areti Gkika, Maria Avloniti, Anastasia Dagkonaki, Lesley Probert, Theodore Tselios and Simona Golič Grdadolnik
Int. J. Mol. Sci. 2020, 21(20), 7566; https://doi.org/10.3390/ijms21207566 - 13 Oct 2020
Cited by 6 | Viewed by 3298
Abstract
Mannan (polysaccharide) conjugated with a myelin oligodendrocyte glycoprotein (MOG) peptide, namely (KG)5MOG35–55, represents a potent and promising new approach for the immunotherapy of Multiple Sclerosis (MS). The MOG35–55 epitope conjugated with the oxidized form of mannan (poly-mannose) via [...] Read more.
Mannan (polysaccharide) conjugated with a myelin oligodendrocyte glycoprotein (MOG) peptide, namely (KG)5MOG35–55, represents a potent and promising new approach for the immunotherapy of Multiple Sclerosis (MS). The MOG35–55 epitope conjugated with the oxidized form of mannan (poly-mannose) via a (KG)5 linker was found to inhibit the symptoms of MOG35–55-induced experimental autoimmune encephalomyelitis (EAE) in mice using prophylactic and therapeutic vaccinated protocols. Deamidation is a common modification in peptide and protein sequences, especially for Gln and Asn residues. In this study, the structural solution motif of deaminated peptides and their functional effects in an animal model for MS were explored. Several peptides based on the MOG35–55 epitope have been synthesized in which the Asn53 was replaced with Ala, Asp, or isoAsp. Our results demonstrate that the synthesized MOG peptides were formed to the deaminated products in basic conditions, and the Asn53 was mainly modified to Asp. Moreover, both peptides (wild type and deaminated derivative) conjugated with mannan (from Saccharomyces cerevisiae) independently inhibited the development of neurological symptoms and inflammatory demyelinating spinal cord lesions in MOG35–55-induced EAE. To conclude, mannan conjugated with a deamidated product did not affect the efficacy of the parent peptide. Full article
(This article belongs to the Special Issue Carbohydrate Recognition in the Immune System)
Show Figures

Figure 1

Back to TopTop