Griffithsin binds to the glycosylated proteins (E and prM) of Japanese encephalitis virus and inhibit its infection

Ishag, Hassan Zackaria Ali; Li, Chen; Wang, Fengjuan

doi:10.1016/j.virusres.2016.01.016

Cited by 21 publications

(19 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The envelope glycoprotein of JEV contains two potential glycosylation sites that are important for virus infection. It has been shown that GRFT can inhibit infection of baby hamster kidney (BHK)-21 cells with IC 50 in the nanomolar range [33], and that such inhibition is due to the interaction between GRFT and the glycosylated viral proteins (Envelope, E and premembrane, prM) [50]. Additionally, mice challenged with lethal doses of JEV showed reduced virus titers in the mouse brain and 100% survival rate compared with a 0% survival rate in the control group [33].…”

Section: Antiviral Activitymentioning

confidence: 99%

Griffithsin: An Antiviral Lectin with Outstanding Therapeutic Potential

Lusvarghi

Bewley

2016

Viruses

111

107

View full text Add to dashboard Cite

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.

show abstract

Section: Antiviral Activitymentioning

confidence: 99%

Griffithsin: An Antiviral Lectin with Outstanding Therapeutic Potential

Lusvarghi

Bewley

2016

Viruses

111

107

View full text Add to dashboard Cite

show abstract

“…The dimeric structure of GRFT having six binding sites is the underlying cause of its high affinity to interact with the viral glycosylated proteins and prevent its entry into cells (Ziolkowska et al 2006). Its mechanism of action involves binding of GRFT to the JEV glycosylated viral proteins, specifically E and prM; however, increasing concentrations of mannose inhibit GRFT binding to JEV as revealed by in vitro experiments using Pull-down assay and Co-immunoprecipitation (CO-IP) assay (Ishag et al 2016). Thus, the binding of GRFT to the glycosylated viral proteins contributes to its anti-JEV activity and has potentials in the development of therapeutics against JEV or other flavivirus infection (Ishag et al 2016).…”

Section: Anti-encephalitis Virusmentioning

confidence: 99%

Lectins from red algae and their biomedical potential

Singh

Walia

2017

J Appl Phycol

View full text Add to dashboard Cite

Lectins are unique proteins or glycoproteins of nonimmune origin that bind specifically to carbohydrates. They recognise and interact reversibly to either free carbohydrates or glycoconjugates, without modifying their structure. Lectins are highly diverse and widely distributed in nature and have been extensively reported from various red algae species. Numerous red algae species have been reported to possess lectins having carbohydrate specificity towards complex glycoproteins or high-mannose N-glycans. These lectin-glycan interactions further trigger many biochemical responses which lead to their extensive use as valuable tools in biomedical research. Thus, owing to their exceptional glycan recognition property, red algae lectins are potential candidate for inhibition of various viral diseases. Hence, the present report integrates existing information on the red algae lectins, their carbohydrate specificity, and characteristics of purified lectins. Further, the review also reports the current state of research into their anti-viral activity against various enveloped viruses such as HIV, hepatitis, influenza, encephalitis, coronavirus and herpes simplex virus and other biomedical activities such as anti-cancer, anti-microbial, anti-inflammatory, antinociceptive and acaricidal activities.

show abstract

“…It has been established that GRFT can bind to a variety of enveloped viruses through their surface glycoproteins [9,16,21,23,26]. PRRSV is, therefore, a candidate for GRFT binding as it is an example of an enveloped virus that expresses surface glycoproteins.…”

Section: Discussionmentioning

confidence: 99%

“…[16], provides the basis for our virus purification strategy. GRFT, a 13-kDa lectin, was recently shown to tightly bind to the glycoprotein on the surface of a number of enveloped viruses including human immunodeficiency virus [5,30,33], severe acute respiratory syndrome corona virus [28], hepatitis C virus [21], herpes simplex virus 2 [27], Japanese encephalitis virus [9], Middle East respiratory syndrome coronavirus [23] and human papillomavirus [13]. However, there are limited data available regarding the binding activities of GRFT to viruses in the veterinary field.…”

Section: Introductionmentioning

confidence: 99%

Surface-displayed porcine reproductive and respiratory syndrome virus from cell culture onto gram-positive enhancer matrix particles

Qiao

Chen

et al. 2018

Journal of Industrial Microbiology and Biotechnology

View full text Add to dashboard Cite

Vaccine immunization is now one of the most effective ways to control porcine reproductive and respiratory syndrome virus (PRRSV) infection. Impurity is one of the main factors affecting vaccine safety and efficacy. Here we present a novel innovative PRRSV purification approach based on surface display technology. First, a bifunctional protein PA-GRFT (protein anchor-griffithsin), the crucial factor in the purification process, was successfully produced in Escherichia coli yielding 80 mg/L of broth culture. Then PRRSV purification was performed by incubation of PA-GRFT with PRRSV and gram-positive enhancer matrix (GEM) particles, followed by centrifugation to collect virions loaded onto GEM particles. Our results showed that most of the bulk impurities had been removed, and PA-GRFT could capture PRRSV onto GEM particles. Our lactic acid bacteria-based purification method, which is promising as ease of operation, low cost and easy to scale-up, may represent a candidate method for the large-scale purification of this virus for vaccine production.

show abstract

Griffithsin binds to the glycosylated proteins (E and prM) of Japanese encephalitis virus and inhibit its infection

Cited by 21 publications

References 18 publications

Griffithsin: An Antiviral Lectin with Outstanding Therapeutic Potential

Griffithsin: An Antiviral Lectin with Outstanding Therapeutic Potential

Lectins from red algae and their biomedical potential

Surface-displayed porcine reproductive and respiratory syndrome virus from cell culture onto gram-positive enhancer matrix particles

Contact Info

Product

Resources

About