ijms-logo

Journal Browser

Journal Browser

Antiviral Activity of Lectins

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

Deadline for manuscript submissions: 20 October 2024 | Viewed by 1001

Special Issue Editor


E-Mail Website
Guest Editor
Department of Medical Pharmacy, Faculty of Pharmacy, Yasuda Women’s University, 6-13-1 Yasuhigashi, Asaminami, Hiroshima 731-0153, Japan
Interests: lectin; antiviral activity; anticancer activity; autophagy; anti-influenza virus activity

Special Issue Information

Dear Colleagues,

Lectins are ubiquitous proteins found in various taxonomy, animals, plants, algae, and bacteria. Numerous lectins have been reported to show antiviral activity against viruses such as influenza virus, human immunodeficiency virus (HIV), SARS-CoV, ebola virus, human herpes viruses, and hepatitis C virus (HCV). As the glycan profiles on viral surface are diverse among these viruses, antiviral potency of lectins are largely depended on their unique carbohydrate-binding specificity as well as the characteristic structure of lectins. Like the pandemic case caused by the recent emerged SARS-CoV-2, we are consistently facing the risk to encounter unknown viruses to which no one has sufficient immunity. Therefore, antiviral agents are in great demand to confront the emergence of new viruses. To develop therapeutic or prophylactic agents targeted for pathogenic viral glycans, fundamental information on lectin-virus interaction via glycan moiety is truly valuable. In this open-access special issue, we welcome any research articles regarding novel aspects of antiviral lectins. We hope that this issue will contribute to advancing our understanding on lectins that are ultimately applicable for microbicides to prevent the transmission of viruses.

Dr. Yuichiro Sato
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. 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

  • lectin
  • carbohydrate-binding specificity
  • virus
  • antiviral activity
  • glycan

Published Papers (1 paper)

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

Research

14 pages, 2386 KiB  
Article
A Complex-Type N-Glycan-Specific Lectin Isolated from Green Alga Halimeda borneensis Exhibits Potent Anti-Influenza Virus Activity
by Jinmin Mu, Makoto Hirayama, Kinjiro Morimoto and Kanji Hori
Int. J. Mol. Sci. 2024, 25(8), 4345; https://doi.org/10.3390/ijms25084345 - 15 Apr 2024
Viewed by 587
Abstract
Marine algal lectins specific for high-mannose N-glycans have attracted attention because they strongly inhibit the entry of enveloped viruses, including influenza viruses and SARS-CoV-2, into host cells by binding to high-mannose-type N-glycans on viral surfaces. Here, we report a novel anti-influenza [...] Read more.
Marine algal lectins specific for high-mannose N-glycans have attracted attention because they strongly inhibit the entry of enveloped viruses, including influenza viruses and SARS-CoV-2, into host cells by binding to high-mannose-type N-glycans on viral surfaces. Here, we report a novel anti-influenza virus lectin (named HBL40), specific for complex-type N-glycans, which was isolated from a marine green alga, Halimeda borneensis. The hemagglutination activity of HBL40 was inhibited with both complex-type N-glycan and O-glycan-linked glycoproteins but not with high-mannose-type N-glycan-linked glycoproteins or any of the monosaccharides examined. In the oligosaccharide-binding experiment using 26 pyridylaminated oligosaccharides, HBL40 only bound to complex-type N-glycans with bi- and triantennary-branched sugar chains. The sialylation, core fucosylation, and the increased number of branched antennae of the N-glycans lowered the binding activity with HBL40. Interestingly, the lectin potently inhibited the infection of influenza virus (A/H3N2/Udorn/72) into NCI-H292 cells at IC50 of 8.02 nM by binding to glycosylated viral hemagglutinin (KD of 1.21 × 10−6 M). HBL40 consisted of two isolectins with slightly different molecular masses to each other that could be separated by reverse-phase HPLC. Both isolectins shared the same 16 N-terminal amino acid sequences. Thus, HBL40 could be useful as an antivirus lectin specific for complex-type N-glycans. Full article
(This article belongs to the Special Issue Antiviral Activity of Lectins)
Show Figures

Figure 1

Back to TopTop