In SituAggregational State of M13 Bacteriophage Major Coat Protein in Sodium Cholate and Lipid Bilayers†

Biochemistry ◽  
1997 ◽  
Vol 36 (40) ◽  
pp. 12268-12275 ◽  
Author(s):  
David Stopar ◽  
Ruud B. Spruijt ◽  
Cor J. A. M. Wolfs ◽  
Marcus A. Hemminga
Keyword(s):  
Coat Protein ◽  
Lipid Bilayers ◽  
Sodium Cholate ◽  
Major Coat Protein ◽  
M13 Bacteriophage

scholarly journals Constrained modeling of spin-labeled major coat protein mutants from M13 bacteriophage in a phospholipid bilayer

2001 ◽  
Vol 10 (5) ◽  
pp. 979-987 ◽  
Author(s):  
Denys Bashtovyy ◽  
Derek Marsh ◽  
Marcus A. Hemminga ◽  
Tibor PÁLI
Keyword(s):  
Coat Protein ◽  
Phospholipid Bilayer ◽  
Major Coat Protein ◽  
M13 Bacteriophage ◽  
Protein Mutants

scholarly journals Mutation of M13 Bacteriophage Major Coat Protein for Increased Conjugation to Exogenous Compounds

2018 ◽  
Vol 29 (6) ◽  
pp. 1872-1875 ◽  
Author(s):  
Matthew Tridgett ◽  
James R. Lloyd ◽  
Jack Kennefick ◽  
Charles Moore-Kelly ◽  
Timothy R. Dafforn
Keyword(s):  
Coat Protein ◽  
Major Coat Protein ◽  
M13 Bacteriophage ◽  
Exogenous Compounds

scholarly journals Interaction of colicin E7 with the major coat protein (g8p) may confer limited protection on colicinogenic Escherichia coli against M13 bacteriophage infection

Microbiology ◽  
2010 ◽  
Vol 156 (11) ◽  
pp. 3379-3385 ◽  
Author(s):  
Yuh-Ren Chen ◽  
Tsung-Yeh Yang ◽  
Guang-Sheng Lei ◽  
Chen-Chung Liao ◽  
Kin-Fu Chak
Keyword(s):  
Escherichia Coli ◽  
Coat Protein ◽  
Protective Effect ◽  
Cytoplasmic Membrane ◽  
Receptor Binding Domain ◽  
Major Coat Protein ◽  
M13 Bacteriophage ◽  
Bacteriophage Infection ◽  
Colicin E7 ◽  
Producer Strains

Colicin release provides producer strains with a competitive advantage under certain circumstances. We found that propagation of M13 bacteriophage in cells producing colicin E7 is impaired, without alteration in the efficiency of bacteriophage adsorption, as compared with non-producing cells. In contrast to the protective effect of the colicin against M13 bacteriophage infection, the endogenously expressed colicin does not confer limited protection against transfection with M13 bacteriophage DNA. Furthermore, it was found that the translocation-receptor-binding domain and toxicity domain of the colicin are able to interact with the M13 major coat protein, g8p, during bacteriophage infection. Based on these observations, we propose that interaction between colicin E7 and g8p during infection interferes with g8p depolymerizing into the cytoplasmic membrane during bacteriophage DNA penetration, thus resulting in the limited protection against M13 bacteriophage infection.

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

Dynamics of fd coat protein in lipid bilayers

Biochemistry ◽  
1987 ◽  
Vol 26 (3) ◽  
pp. 854-862 ◽  
Author(s):  
G. C. Leo ◽  
L. A. Colnago ◽  
K. G. Valentine ◽  
S. J. Opella
Keyword(s):  
Coat Protein ◽  
Lipid Bilayers

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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