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Special Issue "Cellular Interaction in Immunity"

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).

Special Issue Editors

Prof. Dr. Cheorl-Ho Kim
E-Mail Website
Guest Editor
Molecular and Cellular Glycobiology Unit, Department of Biological Sciences, College of Science, Sungkyukwan University, Suwon City, Korea
Interests: glycobiology; sialobiology; sialyltransferase; N-glycan; O-glycan; glycolipid; sphingolipid; glycoprotein; surface sugar; ganglioside; sialic acid; sialyl Le antigen; lectin; galectin; siglec; ER-Golgi glyosylation; sugar–receptor interaction; innate immune; xenotransplantation; cell–cell interaction
Special Issues, Collections and Topics in MDPI journals
Prof. Lee Young-Choon
E-Mail Website
Guest Editor
Department of Medicinal Biotechnology, College of Health Sciences, Dong-A university, Busan 604-714, Korea
Interests: transcriptional regulation of sialyltransferase and ganglioside synthesis-related genes; sialobiology; autophagy; apoptosis

Special Issue Information

Dear Colleagues,

Cellular communication is established through basic platforms used for regulation of cellular function and signaling at the contact sites of two neighboring cells. The most integrated exchanges of cellular information through cellular communication or interaction are known in the immune responses, which cooperatively progress with modulation of immune cells between the innate immune cells and lymphoid cells. The host defense system against invading agents has evolved to control the evasion of recognition and removal. The well-known case is the immunological synapses. Communication between the invader and innate immune cells is established by their cellular interaction with actual components such as membrane-localized carbohydrate receptors attached to membrane lipids and proteins. For example, the known carriers of membrane carbohydrate include glycosphingolipids or gangliosides, glycosylphosphatidylinositol-anchored proteins, proteoglycans attached with glycosaminoglycans, and membrane receptor proteins.  

We invite researchers to contribute original research and review articles regarding cellular interaction and communication in immunity in mammals.

Prof. Cheorl-Ho Kim

Prof. Lee Young-Choon
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 papers will be 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.

Published Papers (3 papers)

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Research

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Article
Glycosylation of Zika Virus is Important in Host–Virus Interaction and Pathogenic Potential
Int. J. Mol. Sci. 2019, 20(20), 5206; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20205206 - 21 Oct 2019
Cited by 12 | Viewed by 1689
Abstract
Zika virus (ZIKV) is a global public health issue due to its association with severe developmental disorders in infants and neurological disorders in adults. ZIKV uses glycosylation of its envelope (E) protein to interact with host cell receptors to facilitate entry; these interactions [...] Read more.
Zika virus (ZIKV) is a global public health issue due to its association with severe developmental disorders in infants and neurological disorders in adults. ZIKV uses glycosylation of its envelope (E) protein to interact with host cell receptors to facilitate entry; these interactions could also be important for designing therapeutics and vaccines. Due to a lack of proper information about Asn-linked (N-glycans) on ZIKV E, we analyzed ZIKV E of various strains derived from different cells. We found ZIKV E proteins being extensively modified with oligomannose, hybrid and complex N-glycans of a highly heterogeneous nature. Host cell surface glycans correlated strongly with the glycomic features of ZIKV E. Mechanistically, we observed that ZIKV N-glycans might play a role in viral pathogenesis, as mannose-specific C-type lectins DC-SIGN and L-SIGN mediate host cell entry of ZIKV. Our findings represent the first detailed mapping of N-glycans on ZIKV E of various strains and their functional significance. Full article
(This article belongs to the Special Issue Cellular Interaction in Immunity)
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Review

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Review
SARS-CoV-2 Evolutionary Adaptation toward Host Entry and Recognition of Receptor O-Acetyl Sialylation in Virus–Host Interaction
Int. J. Mol. Sci. 2020, 21(12), 4549; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21124549 - 26 Jun 2020
Cited by 31 | Viewed by 3248
Abstract
The recently emerged SARS-CoV-2 is the cause of the global health crisis of the coronavirus disease 2019 (COVID-19) pandemic. No evidence is yet available for CoV infection into hosts upon zoonotic disease outbreak, although the CoV epidemy resembles influenza viruses, which use sialic [...] Read more.
The recently emerged SARS-CoV-2 is the cause of the global health crisis of the coronavirus disease 2019 (COVID-19) pandemic. No evidence is yet available for CoV infection into hosts upon zoonotic disease outbreak, although the CoV epidemy resembles influenza viruses, which use sialic acid (SA). Currently, information on SARS-CoV-2 and its receptors is limited. O-acetylated SAs interact with the lectin-like spike glycoprotein of SARS CoV-2 for the initial attachment of viruses to enter into the host cells. SARS-CoV-2 hemagglutinin-esterase (HE) acts as the classical glycan-binding lectin and receptor-degrading enzyme. Most β-CoVs recognize 9-O-acetyl-SAs but switched to recognizing the 4-O-acetyl-SA form during evolution of CoVs. Type I HE is specific for the 9-O-Ac-SAs and type II HE is specific for 4-O-Ac-SAs. The SA-binding shift proceeds through quasi-synchronous adaptations of the SA-recognition sites of the lectin and esterase domains. The molecular switching of HE acquisition of 4-O-acetyl binding from 9-O-acetyl SA binding is caused by protein–carbohydrate interaction (PCI) or lectin–carbohydrate interaction (LCI). The HE gene was transmitted to a β-CoV lineage A progenitor by horizontal gene transfer from a 9-O-Ac-SA–specific HEF, as in influenza virus C/D. HE acquisition, and expansion takes place by cross-species transmission over HE evolution. This reflects viral evolutionary adaptation to host SA-containing glycans. Therefore, CoV HE receptor switching precedes virus evolution driven by the SA-glycan diversity of the hosts. The PCI or LCI stereochemistry potentiates the SA–ligand switch by a simple conformational shift of the lectin and esterase domains. Therefore, examination of new emerging viruses can lead to better understanding of virus evolution toward transitional host tropism. A clear example of HE gene transfer is found in the BCoV HE, which prefers 7,9-di-O-Ac-SAs, which is also known to be a target of the bovine torovirus HE. A more exciting case of such a switching event occurs in the murine CoVs, with the example of the β-CoV lineage A type binding with two different subtypes of the typical 9-O-Ac-SA (type I) and the exclusive 4-O-Ac-SA (type II) attachment factors. The protein structure data for type II HE also imply the virus switching to binding 4-O acetyl SA from 9-O acetyl SA. Principles of the protein–glycan interaction and PCI stereochemistry potentiate the SA–ligand switch via simple conformational shifts of the lectin and esterase domains. Thus, our understanding of natural adaptation can be specified to how carbohydrate/glycan-recognizing proteins/molecules contribute to virus evolution toward host tropism. Under the current circumstances where reliable antiviral therapeutics or vaccination tools are lacking, several trials are underway to examine viral agents. As expected, structural and non-structural proteins of SARS-CoV-2 are currently being targeted for viral therapeutic designation and development. However, the modern global society needs SARS-CoV-2 preventive and therapeutic drugs for infected patients. In this review, the structure and sialobiology of SARS-CoV-2 are discussed in order to encourage and activate public research on glycan-specific interaction-based drug creation in the near future. Full article
(This article belongs to the Special Issue Cellular Interaction in Immunity)
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Review
Sialic Acid-Siglec Axis as Molecular Checkpoints Targeting of Immune System: Smart Players in Pathology and Conventional Therapy
Int. J. Mol. Sci. 2020, 21(12), 4361; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21124361 - 19 Jun 2020
Cited by 4 | Viewed by 914
Abstract
The sialic acid-based molecular mimicry in pathogens and malignant cells is a regulatory mechanism that leads to cross-reactivity with host antigens resulting in suppression and tolerance in the immune system. The interplay between sialoglycans and immunoregulatory Siglec receptors promotes foreign antigens hiding and [...] Read more.
The sialic acid-based molecular mimicry in pathogens and malignant cells is a regulatory mechanism that leads to cross-reactivity with host antigens resulting in suppression and tolerance in the immune system. The interplay between sialoglycans and immunoregulatory Siglec receptors promotes foreign antigens hiding and immunosurveillance impairment. Therefore, molecular targeting of immune checkpoints, including sialic acid-Siglec axis, is a promising new field of inflammatory disorders and cancer therapy. However, the conventional drugs used in regular management can interfere with glycome machinery and exert a divergent effect on immune controlling systems. Here, we focus on the known effects of standard therapies on the sialoglycan-Siglec checkpoint and their importance in diagnosis, prediction, and clinical outcomes. Full article
(This article belongs to the Special Issue Cellular Interaction in Immunity)
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