For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
18
views
145
references
 Top references
cited by
72
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      309
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: not found

      Antiviral lectins: Selective inhibitors of viral entry

      review-article
      Author(s): , , ∗
      Publication date (Electronic):
      Journal: Antiviral Research
      Publisher: Elsevier

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Many natural lectins have been reported to have antiviral activity. As some of these have been put forward as potential development candidates for preventing or treating viral infections, we have set out in this review to survey the literature on antiviral lectins. The review groups lectins by structural class and class of source organism we also detail their carbohydrate specificity and their reported antiviral activities. The review concludes with a brief discussion of several of the pertinent hurdles that heterologous proteins must clear to be useful clinical candidates and cites examples where such studies have been reported for antiviral lectins. Though the clearest path currently being followed is the use of antiviral lectins as anti-HIV microbicides via topical mucosal administration, some investigators have also found systemic efficacy against acute infections following subcutaneous administration.

          Highlights

          • •

            Many natural lectins have been reported to have antiviral activity.

          • •

            This article reviews source organisms for antiviral lectins.

          • •

            We discuss structural classes and carbohydrate specificity for various antiviral lectins.

          • •

            We detail the antiviral activity reported for various natural lectins.

          • •

            We discuss challenges to clinical utility for heterologous proteins.

          Related collections

          Most cited references145

          • Record: found
          • Abstract: found
          • Article: not found

          Virus entry: molecular mechanisms and biomedical applications

          Dimiter Dimitrov (2004)
          Key Points Virus entry into animal cells is initiated by attachment to receptors and is followed by important conformational changes of viral proteins, penetration through (non-enveloped viruses) or fusion with (enveloped viruses) cellular membranes. The process ends with transfer of viral genomes inside host cells. Viral proteins mediating entry are very diverse, but many share common three-dimensional structural motifs. Conformational changes in the viral proteins that drive entry are typically initiated by high-affinity interactions with receptors, or changes in pH after receptor binding and internalization. They include formation of coiled-coils in class I fusion proteins, dimer to trimer transitions in class II fusion proteins, movement of capsid proteins in non-enveloped viruses and exposure of membrane destabilizing sequences. Fusion with, or penetration through, cell membranes might involve multimolecular protein complexes and requires structural rearrangements of membrane lipids. Inhibitors of virus entry can prevent virus attachment, or bind to entry intermediates; small organic molecules, peptides, soluble receptors and antibodies are in clinical trials. Six virus-specific polyclonal human immunoglobulins, one monoclonal antibody and one peptide have been approved by the US Food and Drug Administration for clinical use. Viral proteins involved in entry can induce immune responses and be used as vaccine immunogens. Viral entry machineries could be beneficial for human physiology and retargeted for the treatment of cancer and other diseases.
          Article 0 comments Cited 229 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Isolation and characterization of griffithsin, a novel HIV-inactivating protein, from the red alga Griffithsia sp.

            R Gardella, Alex R. Boyd, Raymond C Sowder … (2005)
            Griffithsin (GRFT), a novel anti-HIV protein, was isolated from an aqueous extract of the red alga Griffithsia sp. The 121-amino acid sequence of GRFT has been determined, and biologically active GRFT was subsequently produced by expression of a corresponding DNA sequence in Escherichia coli. Both native and recombinant GRFT displayed potent antiviral activity against laboratory strains and primary isolates of T- and M- tropic HIV-1 with EC50 values ranging from 0.043 to 0.63 nM. GRFT also aborted cell-to-cell fusion and transmission of HIV-1 infection at similar concentrations. High concentrations (e.g. 783 nM) of GRFT were not lethal to any tested host cell types. GRFT blocked CD4-dependent glycoprotein (gp) 120 binding to receptor-expressing cells and bound to viral coat glycoproteins (gp120, gp41, and gp160) in a glycosylation-dependent manner. GRFT preferentially inhibited gp120 binding of the monoclonal antibody (mAb) 2G12, which recognizes a carbohydrate-dependent motif, and the (mAb) 48d, which binds to CD4-induced epitope. In addition, GRFT moderately interfered with the binding of gp120 to sCD4. Further data showed that the binding of GRFT to soluble gp120 was inhibited by the monosaccharides glucose, mannose, and N-acetylglucosamine but not by galactose, xylose, fucose, N-acetylgalactosamine, or sialic acid-containing glycoproteins. Taken together these data suggest that GRFT is a new type of lectin that binds to various viral glycoproteins in a monosaccharide-dependent manner. GRFT could be a potential candidate microbicide to prevent the sexual transmission of HIV and AIDS.
            Article 0 comments Cited 166 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Plant lectins are potent inhibitors of coronaviruses by interfering with two targets in the viral replication cycle

              Els Keyaerts, Leen Vijgen, Christophe Pannecouque … (2007)
              We describe the antiviral activity of plant lectins with specificity for different glycan structures against the severe acute respiratory syndrome coronavirus (SARS-CoV) and the feline infectious peritonitis virus (FIPV) in vitro. The SARS-CoV emerged in 2002 as an important cause of severe lower respiratory tract infection in humans, and FIPV infection causes a chronic and often fatal peritonitis in cats. A unique collection of 33 plant lectins with different specificities were evaluated. The plant lectins possessed marked antiviral properties against both coronaviruses with EC50 values in the lower microgram/ml range (middle nanomolar range), being non-toxic (CC50) at 50–100 μg/ml. The strongest anti-coronavirus activity was found predominantly among the mannose-binding lectins. In addition, a number of galactose-, N-acetylgalactosamine-, glucose-, and N-acetylglucosamine-specific plant agglutinines exhibited anti-coronaviral activity. A significant correlation (with an r-value of 0.70) between the EC50 values of the 10 mannose-specific plant lectins effective against the two coronaviruses was found. In contrast, little correlation was seen between the activity of other types of lectins. Two targets of possible antiviral intervention were identified in the replication cycle of SARS-CoV. The first target is located early in the replication cycle, most probably viral attachment, and the second target is located at the end of the infectious virus cycle.
              Article 0 comments Cited 126 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                Barry R. O'Keefe
                Journal
                Journal ID (nlm-ta): Antiviral Res
                Journal ID (iso-abbrev): Antiviral Res
                Title: Antiviral Research
                Publisher: Elsevier
                ISSN (Print): 0166-3542
                ISSN (Electronic): 1872-9096
                Publication date PMC-release: 18 March 2017
                Publication date (Print): June 2017
                Publication date (Electronic): 18 March 2017
                Volume: 142
                Pages: 37-54
                Affiliations
                [1]Molecular Targets Laboratory, Center for Cancer Research, National Cancer Institute, NIH, Frederick, MD, 21702-1201, USA
                Author notes
                [∗ ]Corresponding author. 1050 Boyles Street, Bldg. 562 Rm. 201, Frederick, MD, 21702, USA. okeefeba@ 123456mail.nih.gov
                Article
                Publisher ID: S0166-3542(16)30799-9
                DOI: 10.1016/j.antiviral.2017.03.007
                PMC ID: 5414728
                PubMed ID: 28322922
                SO-VID: 7b8f749e-a938-4f95-a1b4-2a86cfce7e56
                License:

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

                History
                Date received : 21 December 2016
                Date accepted : 13 March 2017
                Categories
                Subject: Article

                ScienceOpen disciplines: Infectious disease & Microbiology
                Data availability:
                ScienceOpen disciplines: Infectious disease & Microbiology

                Comments

                Comment on this article

                scite_

                Similar content309

                See all similar

                Cited by71

                See all cited by

                Most referenced authors1,568

                See all reference authors