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Review
. 2019 Oct 6;17(10):567.
doi: 10.3390/md17100567.

Griffithsin, a Highly Potent Broad-Spectrum Antiviral Lectin from Red Algae: From Discovery to Clinical Application

Choongho Lee  1
Affiliations
Review

Griffithsin, a Highly Potent Broad-Spectrum Antiviral Lectin from Red Algae: From Discovery to Clinical Application

Choongho Lee. Mar Drugs. .

Abstract

Keywords: griffithsin (GRFT); lectin; carbohydrate-binding; human immunodeficiency virus (HIV); microbicide; virus entry inhibitor.

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Conflict of interest statement

The author declares that there are no competing interests regarding the publication of this paper.

Figures

Figure 1
Figure 1
The amino acid sequence of griffithsin (GRFT). Corresponding secondary β-sheet structures are marked with yellow arrows based on the crystal structure of a GRFT dimer with mannose at a resolution of 1.78 Å [19]. Tyrosine and aspartate residues in three carbohydrate-binding domains, which are essential for mannose-binding, are noted with blue and orange arrows, respectively. Wild-type GRFT has a non-standard amino acid at position 31, but it is replaced by alanine (colored in red) in recombinant GRFT. The sequence display was generated by the RCSB protein data bank website (www.rcsb.org).
Figure 2
Figure 2
The crystal structure of a GRFT dimer with six mannoses at a resolution of 1.78 Å [19]. Each GRFT monomer is presented in either red or blue. Six bound mannose molecules are shown with ball and stick models. This image was created with PDB ID and associated publication, NGL Viewer (AS Rose et al. (2018) NGL viewer: web-based molecular graphics for large complexes. Bioinformatics doi:10.1093/bioinformatics/bty419), and RCSB PDB.
See this image and copyright information in PMC

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