A Bipartite Bacteriophage T4 SOC and HOC Randomized Peptide Display Library: Detection and Analysis of Phage T4 Terminase (gp17) and Late σ Factor (gp55) Interaction

Malys, Naglis; Chang, Dau-Yin; Baumann, Richard G.; Xie, Dongmei; Black, Lindsay W.

doi:10.1016/s0022-2836(02)00298-x

Cited by 54 publications

(39 citation statements)

References 36 publications

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“…Recruitment of Dp-1 Gp71 (DNA polymerase I) via Gp22/Gp23 interaction could also initiate DNA repair or primase primer displacement in parallel to packaging. Interestingly, the Gp23 of Dp-1 also interacts with the DNA polymerase III ␤-clamp subunit (Gp10), while in T4 the large terminase subunit was shown to interact with the ␤-clamp subunit (58). This suggests a role of the ␤-clamp/DNA polymerase III in DNA packaging in vivo, which cannot be simulated in the pairwise interaction tests carried here.…”

Section: Vol 193 2011 Genome and Interactome Of S Pneumoniae Phagementioning

confidence: 83%

“…In many other phages, portal proteins undergo a homomeric interaction by building dodecameric rings (20). In coliphage T4, the portal protein was found interacting with the major capsid protein and the large terminase subunit (22,58). In Bacillus phage SPP1, the portal protein connects the capsid with the tail (50).…”

Section: Vol 193 2011 Genome and Interactome Of S Pneumoniae Phagementioning

confidence: 99%

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Genome Annotation and Intraviral Interactome for the Streptococcus pneumoniae Virulent Phage Dp-1

et al. 2011

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Streptococcus pneumoniae causes several diseases, including pneumonia, septicemia, and meningitis. Phage Dp-1 is one of the very few isolated virulent S. pneumoniae bacteriophages, but only a partial characterization is currently available. Here, we confirmed that Dp-1 belongs to the family Siphoviridae. Then, we determined its complete genomic sequence of 56,506 bp. It encodes 72 open reading frames, of which 44 have been assigned a function. We have identified putative promoters, Rho-independent terminators, and several genomic clusters. We provide evidence that Dp-1 may be using a novel DNA replication system as well as redirecting host protein synthesis through queuosine-containing tRNAs. Liquid chromatography-mass spectrometry analysis of purified phage Dp-1 particles identified at least eight structural proteins. Finally, using comprehensive yeast two-hybrid screens, we identified 156 phage protein interactions, and this intraviral interactome was used to propose a structural model of Dp-1.Streptococcus pneumoniae (pneumococcus) is a low-GC-content, Gram-positive bacterium belonging to the mitis group of streptococci (40). It is a facultative human pathogen, colonizing the mucosal surface of the upper respiratory tract and causing invasive infections such as pneumonia, meningitis, and sepsis (97). S. pneumoniae diseases are associated with severe morbidity and a high rate of mortality, especially among young children and the elderly. Antibiotics are commonly used to control and cure the invasive pneumococcal diseases, but this high exposure to antibiotics has led to multiresistant S. pneumoniae strains worldwide (79). Vaccination is efficient in preventing invasive diseases (103), but pneumococcal clones expressing capsular polysaccharides with serotypes not included in the current vaccines' formulations exist, and the incidence of invasive diseases induced by these vaccine-escaping clones is increasing (34). Replacement of the vaccine-included clones by the vaccine-escaping ones is possible (91).The appearance of antibiotic-resistant and vaccine-escaping clones is partly due to the high genome plasticity of S. pneumoniae. This genome plasticity is supported by the ability of the pneumococcus to acquire DNA through natural competence and by genome rearrangements facilitated by the mobile elements present in its genome (15,43,93). S. pneumoniae is also able to colonize many sites inside the human host using phase variation of cell surface components such as polysaccharide capsule, lipoteichoic acid, and cell-surface expressed proteins (42,78,101). The complexity of physiology and genetics of S. pneumoniae complicates the search for novel therapeutic approaches needed to counter increasing antibiotic resistance and emergence of the vaccine-escaping clones.One of the novel therapeutic approaches toward antibioticresistant strains is the use of bacteriophage proteins to lyse pneumococcus cells. The feasibility of this approach was first demonstrated when bacteriophage endolysin enzymes were used successfully t...

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Section: Vol 193 2011 Genome and Interactome Of S Pneumoniae Phagementioning

confidence: 83%

Section: Vol 193 2011 Genome and Interactome Of S Pneumoniae Phagementioning

confidence: 99%

Genome Annotation and Intraviral Interactome for the Streptococcus pneumoniae Virulent Phage Dp-1

et al. 2011

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“…The mature DNA-carrying capsid is taken up with high efficiency by eukaryotic cells and can be heavily labeled with fluorescent dye molecules (6). Additionally, the mature procapsid can bind high-affinity head outer capsid (Hoc) and small outer capsid (Soc) proteins that can be manipulated to display peptides or full-length proteins that confer the potential to enhance uptake into specific cell types (8)(9)(10)(11).…”

mentioning

confidence: 99%

“…Thus, the large bacteriophage T4 capsid can serve in vaccine development, as displayed by surface decoration of full-length and active proteins (8)(9)(10), or for affinity studies using bipartite randomized peptide display libraries ( Fig. 1) (11).…”

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confidence: 99%

Viral nanoparticle-encapsidated enzyme and restructured DNA for cell delivery and gene expression

Liu

Dixit

Robertson

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Packaging specific exogenous active proteins and DNAs together within a single viral-nanocontainer is challenging. The bacteriophage T4 capsid (100 × 70 nm) is well suited for this purpose, because it can hold a single long DNA or multiple short pieces of DNA up to 170 kb packed together with more than 1,000 protein molecules. Any linear DNA can be packaged in vitro into purified procapsids. The capsid-targeting sequence (CTS) directs virtually any protein into the procapsid. Procapsids are assembled with specific CTS-directed exogenous proteins that are encapsidated before the DNA. The capsid also can display on its surface high-affinity eukaryotic cell-binding peptides or proteins that are in fusion with small outer capsid and head outer capsid surface-decoration proteins that can be added in vivo or in vitro. In this study, we demonstrate that the site-specific recombinase cyclic recombination (Cre) targeted into the procapsid is enzymatically active within the procapsid and recircularizes linear plasmid DNA containing two terminal loxP recognition sites when packaged in vitro. mCherry expression driven by a cytomegalovirus promoter in the capsid containing Cre-circularized DNA is enhanced over linear DNA, as shown in recipient eukaryotic cells. The efficient and specific packaging into capsids and the unpackaging of both DNA and protein with release of the enzymatically altered protein-DNA complexes from the nanoparticles into cells have potential in numerous downstream drug and gene therapeutic applications.terminase | DNA packaging | capsid decoration proteins | Soc | Hoc V iral-based nanoparticles (NPs) that deliver cargo to specific targets continue to be of widespread interest for drug-and gene-delivery applications in human diseases and other areas of technology, such as diagnostic and cellular imaging (1-4). NPs derived from bacteriophage capsids are among the most attractive for these purposes (5-7). As NPs for medical applications, bacteriophage capsids have the advantages of (i) biocompatibility and demonstrated stability in the circulatory system and widespread delivery to tissues; (ii) absence of eukaryotic cell toxicity and of a preexisting immune response; (iii) ease and flexibility of molecular manipulation of the capsids and the encapsidated cargo; and (iv) easy accessibility of large amounts of material from fully characterized and nonpathogenic bacteria. Bacteriophage capsids and bacteriophages themselves vary tremendously in size and shape as well as complexity. The T4-like phages, which are among the largest and most complex of such bacteriophages, are particularly attractive because they are exceedingly well studied at the molecular and structural level. Thus, the large bacteriophage T4 capsid can serve in vaccine development, as displayed by surface decoration of full-length and active proteins (8-10), or for affinity studies using bipartite randomized peptide display libraries (Fig. 1) (11).The phage T4 capsid has an additional unusual feature among bacteriophages: It is able to pack m...

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“…[54][55][56] For example, Robertson et al 48 engineered a T4-based nanoprobe with applications in cellular imaging and flow cytometry by conjugating fluorescent dyes to the capsid. By inducing the expressing of NH 2 groups on the capsid for subsequent NH 2 -N-hydroxysuccinimide (NHS) conjugation with Alexa Fluor ® 546 (Life Technologies), the authors demonstrate cellular uptake of their proof-of-concept bacteriophage for a variety of imaging applications ( Figure 5A).…”

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confidence: 99%

Nanoscale bacteriophage biosensors beyond phage display

Lee¹,

Song²,

Hwang³

et al. 2013

IJN

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A Bipartite Bacteriophage T4 SOC and HOC Randomized Peptide Display Library: Detection and Analysis of Phage T4 Terminase (gp17) and Late σ Factor (gp55) Interaction

Cited by 54 publications

References 36 publications

Genome Annotation and Intraviral Interactome for the Streptococcus pneumoniae Virulent Phage Dp-1

Genome Annotation and Intraviral Interactome for the Streptococcus pneumoniae Virulent Phage Dp-1

Viral nanoparticle-encapsidated enzyme and restructured DNA for cell delivery and gene expression

Nanoscale bacteriophage biosensors beyond phage display

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