» Articles » PMID: 27007716

Cyanovirin-N Produced in Rice Endosperm Offers Effective Pre-exposure Prophylaxis Against HIV-1BaL Infection in Vitro

Overview
Journal Plant Cell Rep
Publisher Springer
Date 2016 Mar 24
PMID 27007716
Citations 15
Authors
Affiliations
Soon will be listed here.
Abstract

Cyanovirin-N produced in rice endosperm provides efficient pre-exposure prophylaxis against HIV-1 BaL infection in vitro. Cyanovirin-N (CV-N) is a lectin with potent antiviral activity that has been proposed as a component of microbicides for the prevention of infection with Human immunodeficiency virus (HIV). The production of protein-based microbicide components requires a platform that is sufficiently economical and scalable to meet the demands of the large at-risk population, particularly in resource poor developing countries. We, therefore, expressed CV-N in rice endosperm, because the dried seed is ideal for storage and transport and crude extracts could be prepared locally and used as a microbicide component without further purification. We found that crude extracts from rice seeds expressing up to 10 µg CV-N per gram dry seed weight showed dose-dependent gp120 binding activity, confirming that the protein was soluble, correctly folded and active. The recombinant lectin ((OS)CV-N) reduced the infectivity of HIV-1BaL (an R5 virus strain representing the majority of transmitted infections) by ~90 % but showed only weak neutralization activity against HIV-1RF (representative of X4 virus, rarely associated with transmission), suggesting it would be highly effective for pre-exposure prophylaxis against the vast majority of transmitted strains. Crude extracts expressing (OS)CV-N showed no toxicity towards human cells at working dilutions indicating that microbicide components produced in rice endosperm are safe for direct application as topical microbicides in humans.

Citing Articles

Lactic acid bacterial surface display of scytovirin inhibitors for anti-ebolavirus infection.

Wiggins J, Nguyen N, Wei W, Wang L, Hollingsead Olson H, Xiang S Front Microbiol. 2023; 14:1269869.

PMID: 38075878 PMC: 10704896. DOI: 10.3389/fmicb.2023.1269869.


Cyanovirin-N binds to select SARS-CoV-2 spike oligosaccharides outside of the receptor binding domain and blocks infection by SARS-CoV-2.

Munoz-Basagoiti J, Monteiro F, Krumpe L, Armario-Najera V, Shenoy S, Perez-Zsolt D Proc Natl Acad Sci U S A. 2023; 120(10):e2214561120.

PMID: 36853940 PMC: 10013841. DOI: 10.1073/pnas.2214561120.


Therapeutic Potential of Marine Bioactive Peptides against Human Immunodeficiency Virus: Recent Evidence, Challenges, and Future Trends.

Al-Khayri J, Asghar W, Khan S, Akhtar A, Ayub H, Khalid N Mar Drugs. 2022; 20(8).

PMID: 35892945 PMC: 9394390. DOI: 10.3390/md20080477.


Physicochemical characterization of the recombinant lectin scytovirin and microbicidal activity of the SD1 domain produced in rice against HIV-1.

Armario-Najera V, Blanco-Perera A, Shenoy S, Sun Y, Marfil S, Munoz-Basagoiti J Plant Cell Rep. 2022; 41(4):1013-1023.

PMID: 35178612 PMC: 9034974. DOI: 10.1007/s00299-022-02834-5.


Contributions of the international plant science community to the fight against human infectious diseases - part 1: epidemic and pandemic diseases.

Lobato Gomez M, Huang X, Alvarez D, He W, Baysal C, Zhu C Plant Biotechnol J. 2021; 19(10):1901-1920.

PMID: 34182608 PMC: 8486245. DOI: 10.1111/pbi.13657.


References
1.
Colleluori D, Tien D, Kang F, Pagliei T, Kuss R, McCormick T . Expression, purification, and characterization of recombinant cyanovirin-N for vaginal anti-HIV microbicide development. Protein Expr Purif. 2005; 39(2):229-36. DOI: 10.1016/j.pep.2004.10.009. View

2.
Naqvi S, Zhu C, Farre G, Ramessar K, Bassie L, Breitenbach J . Transgenic multivitamin corn through biofortification of endosperm with three vitamins representing three distinct metabolic pathways. Proc Natl Acad Sci U S A. 2009; 106(19):7762-7. PMC: 2683132. DOI: 10.1073/pnas.0901412106. View

3.
Drake P, Barbi T, Sexton A, McGowan E, Stadlmann J, Navarre C . Development of rhizosecretion as a production system for recombinant proteins from hydroponic cultivated tobacco. FASEB J. 2009; 23(10):3581-9. DOI: 10.1096/fj.09-131771. View

4.
Shenoy S, Barrientos L, Ratner D, OKeefe B, Seeberger P, Gronenborn A . Multisite and multivalent binding between cyanovirin-N and branched oligomannosides: calorimetric and NMR characterization. Chem Biol. 2002; 9(10):1109-18. DOI: 10.1016/s1074-5521(02)00237-5. View

5.
Mori T, Barrientos L, Han Z, Gronenborn A, Turpin J, Boyd M . Functional homologs of cyanovirin-N amenable to mass production in prokaryotic and eukaryotic hosts. Protein Expr Purif. 2002; 26(1):42-9. DOI: 10.1016/s1046-5928(02)00513-2. View