Griffithsin: An Antiviral Lectin with Outstanding Therapeutic Potential

被引:113
作者
Lusvarghi, Sabrina [1 ]
Bewley, Carole A. [1 ]
机构
[1] NIDDK, Bioorgan Chem Lab, NIH, Bethesda, MD 20892 USA
来源
VIRUSES-BASEL | 2016年 / 8卷 / 10期
关键词
carbohydrate binding agent; viral envelope glycoproteins; multivalency; resistance; immunogenicity; HIV; HSV; HCV; ENTRY INHIBITOR GRIFFITHSIN; JAPANESE ENCEPHALITIS-VIRUS; ANTI-HIV ACTIVITY; CYANOVIRIN-N; PROTEIN GRIFFITHSIN; IN-VITRO; BINDING; GP120; COMBINATION; TYPE-1;
D O I
10.3390/v8100296
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Griffithsin (GRFT), an algae-derived lectin, is one of the most potent viral entry inhibitors discovered to date. It is currently being developed as a microbicide with broad-spectrum activity against several enveloped viruses. GRFT can inhibit human immunodeficiency virus (HIV) infection at picomolar concentrations, surpassing the ability of most anti-HIV agents. The potential to inhibit other viruses as well as parasites has also been demonstrated. Griffithsin's antiviral activity stems from its ability to bind terminal mannoses present in high-mannose oligosaccharides and crosslink these glycans on the surface of the viral envelope glycoproteins. Here, we review structural and biochemical studies that established mode of action and facilitated construction of GRFT analogs, mechanisms that may lead to resistance, and in vitro and pre-clinical results that support the therapeutic potential of this lectin.
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页数:18
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