Bacteriophage B103: complete DNA sequence of its genome and relationship to other Bacillus phages

Pečenková, Tamara; Beneš, Vladimı́r; Pačes, Jan; Vlček, Čestmı́r; Pačes, Václav

doi:10.1016/s0378-1119(97)00363-6

Cited by 30 publications

(23 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…7). Phylogenetic analysis of pRNAs from Bacillus subtilis phages SF5, B103, phi29, PZA, M2, NF, and GA1, 42,52,53 shows very low sequence identity and few conserved bases, yet the family of pRNAs appears to have similar predicted secondary structures 42,52 ( Figure 8). All seven pRNAs of these phages contain both the right-and lefthand loops, which form a loop/loop interaction via W.C. base pairing.…”

Section: Discussionmentioning

confidence: 99%

Bacterial virus phi29 pRNA as a hammerhead ribozyme escort to destroy hepatitis B virus

et al. 2003

View full text Add to dashboard Cite

The DNA-packaging pRNA of bacterial virus phi29, which forms dimers and then hexamers, contains two independent tightly self-folded domains. Circularly permuted pRNAs were constructed without impacting pRNA folding. Connecting the pRNA 5 0 /3 0 ends with variable sequences did not disturb its folding and function. These unique features, which help prevent two common problems -exonuclease degradation and misfolding in the cell, make pRNA an ideal vector to carry therapeutic RNAs. A pRNA-based vector was designed to carry hammerhead ribozymes that cleave the hepatitis B virus (HBV) polyA signal. The chimeric HBV-targeting ribozyme was connected to the pRNA 5 0 /3 0 ends as circularly permuted pRNA. Two cis-cleaving ribozymes were used to flank and process the chimeric ribozyme. The hammerhead ribozyme including its two arms for HBV targeting was able to fold correctly while escorted by the pRNA. The chimeric ribozyme cleaved the polyA signal of HBV mRNA in vitro almost completely. Cell culture studies showed that the chimeric ribozyme was able to enhance the inhibition of HBV replication when compared with the ribozyme not escorted by pRNA, as demonstrated by Northern blot and e-antigen assays. pRNA could also carry another hammerhead ribozyme to cleave other RNA substrate. These findings suggest that pRNA can be used as a vector for imparting stability to ribozymes, antisense, and other therapeutic RNA molecules in vivo.

show abstract

Section: Discussionmentioning

confidence: 99%

Bacterial virus phi29 pRNA as a hammerhead ribozyme escort to destroy hepatitis B virus

et al. 2003

View full text Add to dashboard Cite

show abstract

“…Analysis of the host range showed that 29 was able to infect B. subtilis strains 168, 110NA, and Marburg, B. amyloliquefaciens H, and several strains of B. licheniformis and B. pumilus (reviewed in reference 177). The host range of B103 has not been studied, but it is known to infect B. subtilis 9/3 (163). Finally, GA-1 was shown to infect lytically Bacillus species strain G1R (39).…”

Section: General Features Of Phages 29 B103 and Ga-1mentioning

confidence: 99%

“…The DNA sequences of the complete genomes of 29 and PZA (83,84,161,216,221,224) belonging to group I and that of B103 (163) belonging to group II have been determined. However, only parts of the GA-1 sequence, belonging to group III, have been determined so far (78,86,111,114,222).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

φ29 Family of Phages

Meijer

Horcajadas

Salas

2001

Microbiol Mol Biol Rev

185

223

View full text Add to dashboard Cite

SUMMARY Continuous research spanning more than three decades has made the Bacillus bacteriophage φ29 a paradigm for several molecular mechanisms of general biological processes, such as DNA replication, regulation of transcription, phage morphogenesis, and phage DNA packaging. The genome of bacteriophage φ29 consists of a linear double-stranded DNA (dsDNA), which has a terminal protein (TP) covalently linked to its 5′ ends. Initiation of DNA replication, carried out by a protein-primed mechanism, has been studied in detail and is considered to be a model system for the protein-primed DNA replication that is also used by most other linear genomes with a TP linked to their DNA ends, such as other phages, linear plasmids, and adenoviruses. In addition to a continuing progress in unraveling the initiation of DNA replication mechanism and the role of various proteins involved in this process, major advances have been made during the last few years, especially in our understanding of transcription regulation, the head-tail connector protein, and DNA packaging. Recent progress in all these topics is reviewed. In addition to φ29, the genomes of several other Bacillus phages consist of a linear dsDNA with a TP molecule attached to their 5′ ends. These φ29-like phages can be divided into three groups. The first group includes, in addition to φ29, phages PZA, φ15, and BS32. The second group comprises B103, Nf, and M2Y, and the third group contains GA-1 as its sole member. Whereas the DNA sequences of the complete genomes of φ29 (group I) and B103 (group II) are known, only parts of the genome of GA-1 (group III) were sequenced. We have determined the complete DNA sequence of the GA-1 genome, which allowed analysis of differences and homologies between the three groups of φ29-like phages, which is included in this review.

show abstract

“…4A) (32). Of the 595 amino acid residues of the BacL 1 protein, the N-terminal 151 amino acid residues showed a high level of homology with the lysozyme encoded on Bacillus subtilis bacteriophage B103 (accession number Q37896) (37). The 150-amino-acid sequence from residue 160 to residue 309, which is located in the center of the bacL 1 -encoded protein, showed a high level of homology with the N-terminal amino acid residues of the lysin encoded on the S. agalactiae prophage lambda Sa1 (accession number NP 687631) (43), and the C-terminal 260 amino acid residues showed a high level of homology with the C-terminal amino acid residues of the muramidase of Lactobacillus plantarum WCFS1 (accession number CAD64901) (30).…”

Section: Cloning Of Component L Component a And The Immunity Genesmentioning

confidence: 99%

Cloning and Genetic Analyses of the Bacteriocin 41 Determinant Encoded on the Enterococcus faecalis Pheromone-Responsive Conjugative Plasmid pYI14: a Novel Bacteriocin Complemented by Two Extracellular Components (Lysin and Activator)

Tomita¹,

Kamei²,

Ike

2008

J Bacteriol

View full text Add to dashboard Cite

The conjugative plasmid pYI14 (61 kbp) was isolated from Enterococcus faecalis YI714, a clinical isolate. pYI14 conferred a pheromone response on its host and encoded bacteriocin 41 (bac41). Bacteriocin 41 (Bac41) only showed activity against E. faecalis. Physical mapping of pYI14 showed that it consisted of EcoRI fragments A to P. The clone pHT1100, containing EcoRI fragments A (12.6 kbp) and H (3.5 kbp), conferred the bacteriocin activity on E. faecalis strains. Genetic analysis showed that the determinant was located in a 6.6-kbp region within the EcoRI AH fragments. Six open reading frames (ORFs) were identified in this region and designated ORF7 (bacL 1 ) ORF8 (bacL 2 ), ORF9, ORF10, ORF11 (bacA), and ORF12 (bacI). They were aligned in this order and oriented in the same direction. ORFs bacL 1 , bacL 2 , bacA, and bacI were essential for expression of the bacteriocin in E. faecalis. Extracellular complementation of bacteriocin expression was possible for bacL 1 and -L 2 and bacA mutants. bacL 1 and -L 2 and bacA encoded bacteriocin component L and activator component A, respectively. The products of these genes are secreted into the culture medium and extracellularly complement bacteriocin expression. bacI encoded immunity, providing the host with resistance to its own bacteriocin activity. The bacL 1 -encoded protein had significant homology with lytic enzymes that attack the gram-positive bacterial cell wall. Sequence data for the deduced bacL 1 -encoded protein suggested that it has a domain structure consisting of an N-terminal signal peptide, a second domain with the enzymatic activity, and a third domain with a three-repeat structure directing the proenzyme to its cell surface receptor.Bacteriocins are bacterial proteins or peptides which inhibit the growth of other bacteria that are closely related to the producer strain. They usually exhibit a relatively narrow spectrum of activity and are produced by a wide variety of grampositive and gram-negative bacteria (27). Bacteriocin production is thought to provide the host strain with an ecological or other selective advantage over other strains.Many Enterococcus faecalis clinical isolates produce a bacteriocin (3, 5), and the bacteriocin is frequently encoded on the E. faecalis pheromone-responding conjugative plasmid (6,14,21,46). Several E. faecalis bacteriocins have been genetically and biochemically characterized (15, 35), including the ␤-hemolysin/bacteriocin (cytolysin) (6,7,18,20,22) and the peptide antibiotics AS-48 (33), bacteriocin 21 (47), and bacteriocin 31 (46), which are encoded by the E. faecalis conjugative plasmids pAD1 (58 kbp), pMB2 (58 kbp), pPD1 (59 kbp), and pYI17 (57.5 kbp), respectively. A significant number of E. faecalis clinical isolates produce hemolysin/bacteriocin (10, 26), and more than 50% of the hemolytic clinical isolates carry transferable hemolysin/bacteriocin determinants (21, 26). The hemolysin/bacteriocin of pAD1 is associated with virulence in animal models (4,25,29), and this plasmid is considered to be a typical ...

show abstract

Bacteriophage B103: complete DNA sequence of its genome and relationship to other Bacillus phages

Cited by 30 publications

References 25 publications

Bacterial virus phi29 pRNA as a hammerhead ribozyme escort to destroy hepatitis B virus

Bacterial virus phi29 pRNA as a hammerhead ribozyme escort to destroy hepatitis B virus

φ29 Family of Phages

Cloning and Genetic Analyses of the Bacteriocin 41 Determinant Encoded on the Enterococcus faecalis Pheromone-Responsive Conjugative Plasmid pYI14: a Novel Bacteriocin Complemented by Two Extracellular Components (Lysin and Activator)

Contact Info

Product

Resources

About