Enzyme Encapsulation in an Engineered Lumazine Synthase Protein Cage

Author(s):  
Yusuke Azuma ◽  
Donald Hilvert
RSC Advances ◽  
2016 ◽  
Vol 6 (23) ◽  
pp. 19208-19213 ◽  
Author(s):  
Hansol Kim ◽  
Young Ji Kang ◽  
Junseon Min ◽  
Hyeokjune Choi ◽  
Sebyung Kang

A polyvalent antibody-binding lumazine synthase protein cage nanoparticle (ABD–AaLS) is constructed by genetically fusing lumazine synthase and antibody-binding domains. ABD–AaLS effectively displays targeting antibodies in an orientation-controlled manner.


RSC Advances ◽  
2014 ◽  
Vol 4 (89) ◽  
pp. 48596-48600 ◽  
Author(s):  
Junseon Min ◽  
Soohyun Kim ◽  
Jisu Lee ◽  
Sebyung Kang

Lumazine synthase protein cage nanoparticle is developed as a modular delivery nanoplatform that delivers drugs to their target cancer cells.


2020 ◽  
Vol 529 (3) ◽  
pp. 548-553
Author(s):  
Nikola Lončar ◽  
Henriette J. Rozeboom ◽  
Linda E. Franken ◽  
Marc C.A. Stuart ◽  
Marco W. Fraaije

2018 ◽  
Author(s):  
Daniel D. Brauer ◽  
Emily C. Hartman ◽  
Daniel L.V. Bader ◽  
Zoe N. Merz ◽  
Danielle Tullman-Ercek ◽  
...  

<div> <p>Site-specific protein modification is a widely-used strategy to attach drugs, imaging agents, or other useful small molecules to protein carriers. N-terminal modification is particularly useful as a high-yielding, site-selective modification strategy that can be compatible with a wide array of proteins. However, this modification strategy is incompatible with proteins with buried or sterically-hindered N termini, such as virus-like particles like the well-studied MS2 bacteriophage coat protein. To assess VLPs with improved compatibility with these techniques, we generated a targeted library based on the MS2-derived protein cage with N-terminal proline residues followed by three variable positions. We subjected the library to assembly, heat, and chemical selections, and we identified variants that were modified in high yield with no reduction in thermostability. Positive charge adjacent to the native N terminus is surprisingly beneficial for successful extension, and over 50% of the highest performing variants contained positive charge at this position. Taken together, these studies described nonintuitive design rules governing N-terminal extensions and identified successful extensions with high modification potential.</p> </div>


2010 ◽  
Vol 122 (39) ◽  
pp. 7168-7172 ◽  
Author(s):  
Thomas W. Ni ◽  
F. Akif Tezcan

2010 ◽  
Vol 100 (6) ◽  
pp. 573-581 ◽  
Author(s):  
Tingquan Wu ◽  
An Guo ◽  
Yanying Zhao ◽  
Xiaomeng Wang ◽  
Ying Wang ◽  
...  

Lumazine synthase (LS) catalyzes the penultimate reaction in the multistep riboflavin biosynthesis pathway, which is involved in plant defenses. Plant defenses are often subject to synergistic effects of jasmonic acid and ethylene whereas LS is a regulator of jasmonic acid signal transduction. However, little is known about whether the enzyme contributes to defense responses. To study the role of LS in plant pathogen defenses, we generated transgenic tobacco expressing the rice (Oryza sativa) LS gene, OsLS. OsLS was cloned and found to have strong identity with its homologues in higher plants and less homology to microbial orthologues. The OsLS protein localized to chloroplasts in three OsLS-expressing transgenic tobacco (LSETT) lines characterized as enhanced in growth and defense. Compared with control plants, LSETT had higher content of both riboflavin and the cofactors flavin mononucleotide and flavin adenine dinucleotide. In LSETT, jasmonic acid and ethylene were elevated, the expression of defense-related genes was induced, levels of resistance to pathogens were enhanced, and resistance was effective to viral, bacterial, and oomycete pathogens. Extents of OsLS expression correlated with increases in flavin, jasmonic acid, and ethylene content, and correlated with increases in resistance levels, suggesting a role for OsLS in defense responses.


Sign in / Sign up

Export Citation Format

Share Document