Transmembrane domain mediated self-assembly of major coat protein subunits from Ff bacteriophage11Edited by G. von Heijne

2002 ◽  
Vol 315 (1) ◽  
pp. 63-72 ◽  
Author(s):  
Roman A Melnyk ◽  
Anthony W Partridge ◽  
Charles M Deber
Keyword(s):  
Coat Protein ◽  
Self Assembly ◽  
Transmembrane Domain ◽  
Major Coat Protein ◽  
Protein Subunits

scholarly journals Functionalized Tobacco Mosaic Virus Coat Protein Monomers and Oligomers as Nanocarriers for Anti-Cancer Peptides

Cancers ◽  
2019 ◽  
Vol 11 (10) ◽  
pp. 1609 ◽  
Author(s):  
Coralie Gamper ◽  
Caroline Spenlé ◽  
Sonia Boscá ◽  
Michael van der Heyden ◽  
Mathieu Erhardt ◽  
...  
Keyword(s):  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Cancer Cells ◽  
Mosaic Virus ◽  
Self Assembly ◽  
Transmembrane Domain ◽  
Plant Viruses ◽  
Neuropilin 1 ◽  
Angiogenic Effect ◽  
Highly Hydrophobic

Components with self-assembly properties derived from plant viruses provide the opportunity to design biological nanoscaffolds for the ordered display of agents of diverse nature and with complementing functions. With the aim of designing a functionalized nanoscaffold to target cancer, the coat protein (CP) of Tobacco mosaic virus (TMV) was tested as nanocarrier for an insoluble, highly hydrophobic peptide that targets the transmembrane domain of the Neuropilin-1 (NRP1) receptor in cancer cells. The resulting construct CPL-K (CP-linker-“Kill”) binds to NRP1 in cancer cells and disrupts NRP1 complex formation with PlexA1 as well as downstream Akt survival signaling. The application of CPL-K also inhibits angiogenesis and cell migration. CP was also fused to a peptide that targets the extracellular domain of NRP1 and this fusion protein (CPL-F, CP-Linker-“Find”) is shown to bind to cultured cancer cells and to inhibit NRP1-dependent angiogenesis as well. CPL-K and CPL-F maintain their anti-angiogenic properties upon co-assembly to oligomers/nanoparticles together with CPL. The observations show that the CP of TMV can be employed to generate a functionalized nanoparticle with biological activity. Remarkably, fusion to CPL allowed us to solubilize the highly insoluble transmembrane NRP1 peptide and to retain its anti-angiogenic effect.

scholarly journals Extracellular self-assembly of virus-like particles from secreted recombinant polyoma virus major coat protein

2007 ◽  
Vol 20 (12) ◽  
pp. 591-598 ◽  
Author(s):  
J. Ng ◽  
O. Koechlin ◽  
M. Ramalho ◽  
D. Raman ◽  
N. Krauzewicz
Keyword(s):  
Coat Protein ◽  
Self Assembly ◽  
Polyoma Virus ◽  
Major Coat Protein ◽  
Virus Like Particles

scholarly journals Uniqueness of RNA Coliphage Qβ Display System in Directed Evolutionary Biotechnology

Viruses ◽  
2021 ◽  
Vol 13 (4) ◽  
pp. 568
Author(s):  
Godwin W. Nchinda ◽  
Nadia Al-Atoom ◽  
Mamie T. Coats ◽  
Jacqueline M. Cameron ◽  
Alain Bopda Waffo
Keyword(s):  
Life Cycle ◽  
Coat Protein ◽  
Phage Display ◽  
Display System ◽  
Phage Display Technology ◽  
Library Size ◽  
Exterior Surface ◽  
Major Coat Protein ◽  
Display Technology ◽  
Minor Coat Protein

Phage display technology involves the surface genetic engineering of phages to expose desirable proteins or peptides whose gene sequences are packaged within phage genomes, thereby rendering direct linkage between genotype with phenotype feasible. This has resulted in phage display systems becoming invaluable components of directed evolutionary biotechnology. The M13 is a DNA phage display system which dominates this technology and usually involves selected proteins or peptides being displayed through surface engineering of its minor coat proteins. The displayed protein or peptide’s functionality is often highly reduced due to harsh treatment of M13 variants. Recently, we developed a novel phage display system using the coliphage Qβ as a nano-biotechnology platform. The coliphage Qβ is an RNA phage belonging to the family of Leviviridae, a long investigated virus. Qβ phages exist as a quasispecies and possess features making them comparatively more suitable and unique for directed evolutionary biotechnology. As a quasispecies, Qβ benefits from the promiscuity of its RNA dependent RNA polymerase replicase, which lacks proofreading activity, and thereby permits rapid variant generation, mutation, and adaptation. The minor coat protein of Qβ is the readthrough protein, A1. It shares the same initiation codon with the major coat protein and is produced each time the ribosome translates the UGA stop codon of the major coat protein with the of misincorporation of tryptophan. This misincorporation occurs at a low level (1/15). Per convention and definition, A1 is the target for display technology, as this minor coat protein does not play a role in initiating the life cycle of Qβ phage like the pIII of M13. The maturation protein A2 of Qβ initiates the life cycle by binding to the pilus of the F+ host bacteria. The extension of the A1 protein with a foreign peptide probe recognizes and binds to the target freely, while the A2 initiates the infection. This avoids any disturbance of the complex and the necessity for acidic elution and neutralization prior to infection. The combined use of both the A1 and A2 proteins of Qβ in this display system allows for novel bio-panning, in vitro maturation, and evolution. Additionally, methods for large library size construction have been improved with our directed evolutionary phage display system. This novel phage display technology allows 12 copies of a specific desired peptide to be displayed on the exterior surface of Qβ in uniform distribution at the corners of the phage icosahedron. Through the recently optimized subtractive bio-panning strategy, fusion probes containing up to 80 amino acids altogether with linkers, can be displayed for target selection. Thus, combined uniqueness of its genome, structure, and proteins make the Qβ phage a desirable suitable innovation applicable in affinity maturation and directed evolutionary biotechnology. The evolutionary adaptability of the Qβ phage display strategy is still in its infancy. However, it has the potential to evolve functional domains of the desirable proteins, glycoproteins, and lipoproteins, rendering them superior to their natural counterparts.

Local Dynamics of the M13 Major Coat Protein in Different Membrane-Mimicking Systems†

Biochemistry ◽  
1996 ◽  
Vol 35 (48) ◽  
pp. 15467-15473 ◽  
Author(s):  
David Stopar ◽  
Ruud B. Spruijt ◽  
Cor J. A. M. Wolfs ◽  
Marcus A. Hemminga
Keyword(s):  
Coat Protein ◽  
Major Coat Protein ◽  
Local Dynamics

scholarly journals Major coat protein and single-stranded DNA-binding protein of filamentous virus Pf3.

1984 ◽  
Vol 81 (3) ◽  
pp. 699-703 ◽  
Author(s):  
D. G. Putterman ◽  
A. Casadevall ◽  
P. D. Boyle ◽  
H. L. Yang ◽  
B. Frangione ◽  
...  
Keyword(s):  
Coat Protein ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Stranded Dna ◽  
Major Coat Protein
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