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1.
Acta Gastroenterol Belg ; 86(3): 499-501, 2023.
Article in English | MEDLINE | ID: mdl-37814569

ABSTRACT

Adenocarcinomas of the ampulla of Vater represent only 0.2% of all gastrointestinal cancers. Due to the low incidence no large clinical trials evaluating efficacy of treatments are available. Adjuvant therapy is often administered in patients with stage IB or higher. Oxaliplatin is considered as an effective and well tolerated therapeutic option. Adverse events associated with this therapy include cardio-, neuro-, nephrotoxicity and myelosuppression. Previously granulomatous pulmonary and liver manifestations have been described in oxaliplatin-based chemotherapy. In this report peritoneal manifestation of granulomatous disease associated with oxaliplatin is described for the first time. Sarcoidlike reactions may be misinterpreted as tumour progression or metastatic disease, and may consequently result in over-treatment.


Subject(s)
Adenocarcinoma , Ampulla of Vater , Common Bile Duct Neoplasms , Peritoneal Diseases , Humans , Oxaliplatin/adverse effects , Ampulla of Vater/pathology , Adenocarcinoma/pathology , Common Bile Duct Neoplasms/drug therapy , Common Bile Duct Neoplasms/etiology , Common Bile Duct Neoplasms/pathology , Antineoplastic Combined Chemotherapy Protocols/adverse effects
4.
JBR-BTR ; 97(2): 81-3, 2014.
Article in English | MEDLINE | ID: mdl-25073236

ABSTRACT

Pseudoangiomatous stromal hyperplasia is a benign mesenchymal tumor of the breast. It is a rare condition and until a few years mainly described in pathological and surgical literature. Here, we provide a case report of PASH and an overview of its radiological features.


Subject(s)
Angiomatosis/diagnosis , Breast Diseases/diagnosis , Breast Neoplasms/diagnosis , Breast/pathology , Hyperplasia/diagnosis , Magnetic Resonance Imaging/methods , Mammography/methods , Adult , Biopsy, Needle , Contrast Media , Diagnosis, Differential , Female , Humans , Image Enhancement/methods , Ultrasonography, Mammary/methods
6.
Genetika ; 44(5): 713-6, 2008 May.
Article in Russian | MEDLINE | ID: mdl-18672806

ABSTRACT

Genome sizes of Pseudomonas aeruginosa phages phiKZ and EL earlier determined by sequence analysis were shown to correspond to sizes of their DNAs assessed by pulse-electrophoresis (PFGE). Putative "redundant" genes in phiKZ phage genome are supposed to control functions promoting vigorous growth of the phage belonging to this species, compared to phages of EL species.


Subject(s)
DNA, Viral/chemistry , Genes, Viral , Pseudomonas Phages/genetics , Pseudomonas aeruginosa/virology , Electrophoresis, Gel, Pulsed-Field
9.
Arch Virol ; 152(10): 1955-9, 2007.
Article in English | MEDLINE | ID: mdl-17680323

ABSTRACT

The proposed phiKZ genus of myoviruses has 21 members. Phages are virulent, lyse Pseudomonas bacteria, and are characterized by very large heads and correspondingly high DNA contents. The genome of the type virus, phiKZ, has 306 ORFs and over 280 kbp and is the second-largest phage genome known. The phiKZ genus has very few relationships to other phages and includes three species and one possible species.


Subject(s)
Myoviridae/classification , Myoviridae/genetics , Myoviridae/pathogenicity , Pseudomonas Phages/classification , Pseudomonas Phages/genetics , Pseudomonas Phages/pathogenicity , Base Composition , Base Sequence , Chromosome Mapping , Chromosomes , DNA, Circular , DNA, Intergenic , DNA, Viral/analysis , DNA, Viral/isolation & purification , Genome, Viral , Hot Temperature , Myoviridae/chemistry , Myoviridae/isolation & purification , Myoviridae/ultrastructure , Open Reading Frames , Pseudomonas Phages/chemistry , Pseudomonas Phages/isolation & purification , Pseudomonas Phages/ultrastructure , RNA, Transfer/genetics , Viral Proteins/analysis , Virion/chemistry , Virion/ultrastructure , Virulence
10.
Arch Virol ; 152(8): 1467-75, 2007.
Article in English | MEDLINE | ID: mdl-17534690

ABSTRACT

Little is known about the bacteriophage proteins expressed immediately after infection of the host cell. Most of these early proteins are probably involved in bacteriophage-host interactions redirecting the bacterial metabolism to phage production. Interaction analysis of the first 16 phiKMV gene products (gp) identified homotypic interactions of gp7, gp9 and gp15. Two related yeast two-hybrid procedures, a matrix and a minilibrary approach, were applied to detect protein-protein interactions. A two-step selection procedure enabled drastic reduction of the background. Interactions were confirmed by drop tests. Multimerization of gp15 is consistent with its putative function as a DNA helicase involved in DNA replication. Homotypic interaction of gp7 and gp9 suggests they function as dimers or multimers. The absence of heterotypic interactions among early phiKMV proteins hints at their functional independence from other early phage proteins and their involvement in phage-host interactions that are important for creating optimal conditions for phage propagation. Besides, these results demonstrate the compatibility of phiKMV early gene products with the yeast two-hybrid system. Therefore, they are promising candidates to screen for interactions with host proteins.


Subject(s)
Podoviridae/metabolism , Pseudomonas Phages/metabolism , Viral Proteins/metabolism , DNA Helicases/genetics , DNA Helicases/metabolism , DNA Primase/genetics , DNA Primase/metabolism , DNA-Binding Proteins/genetics , DNA-Binding Proteins/metabolism , Dimerization , Podoviridae/genetics , Pseudomonas Phages/genetics , Pseudomonas aeruginosa/virology , Two-Hybrid System Techniques , Viral Proteins/genetics , Viral Structural Proteins/genetics , Viral Structural Proteins/metabolism
12.
Genetika ; 42(8): 1065-74, 2006 Aug.
Article in Russian | MEDLINE | ID: mdl-17025156

ABSTRACT

Study of two recently isolated giant bacteriophages Lu11 and OBP that are active on Pseudomonas putida var. Manila and Pseudomonas fluorescens, respectively, demonstrated their similarity in morphology, genome size, and size of phage particles, with giant bacteriophages of Pseudomonas aeruginosa assigned to the supergroup of phiKZ-like phages of the family Myoviridae designated in this manner according to the best studied phage phiKZ that belongs to the species of this group widely distributed in nature. Comparison of major polypeptide sizes of mature particles suggests the similarity of certain proteins in the phages examined. In OBP particles visualized with an electron microscope, an "inner body" was detected, which points to the specific DNA package intrinsic to phages of phiKZ group. In the meantime, phages Lul11 and OBP do not exhibit resemblance among themselves or with any of earlier described phiKZ-like phages in respect to other traits; particularly, they have no detectable DNA homology. Note that phage Lu11 of P. putida var. Manila exhibits very slight homology with phage Lin68 of the family of P. aeruginosa phiKZ-like phages detected only in blot hybridization. This suggests the possible involvement of these phages in interspecies recombination ("gene shuffling") between phages of various bacterial species. Results of partial sequencing of phage genomes confirmed the phylogenetic relatedness of phage OBP to phages of the phiKZ-supergroup, whereas phage Lu11 most probably belongs to a novel species that is not a member of supergroup phiKZ composition. The results of the study are discussed in terms of the evolution of these phages.


Subject(s)
Pseudomonas Phages/genetics , Pseudomonas Phages/physiology , Pseudomonas aeruginosa/virology , Soil Microbiology , Genome, Viral/genetics , Phylogeny , Pseudomonas Phages/ultrastructure , Sequence Analysis, DNA
13.
Cell Mol Life Sci ; 63(16): 1899-905, 2006 Aug.
Article in English | MEDLINE | ID: mdl-16847574

ABSTRACT

The kinetic, thermodynamic and structural stability of gp36C, the virion-associated peptidoglycan hydrolase domain of bacteriophage phiKMV, is analyzed. Recombinant gp36C is highly thermoresistant (k = 0.595 h(-1) at 95 degrees C), but not thermostable (T(m) = 50.2 degrees C, DeltaH(cal) = 6.86 x 10(4) cal mol(-1)). However, aggregation influences kinetic stability in an unusual manner since aggregation is more pronounced at 55 degrees C than at higher temperatures. Furthermore, gp36C reversibly unfolds in a two-state endothermic transition, and circular dichroism analysis shows that gp36C almost completely refolds after a 3-h heat treatment at 85 degrees C. These properties are in agreement with gp36C being part of the extensible tail which is ejected in an unfolded state during phage infection.


Subject(s)
Bacteriophages/pathogenicity , Pseudomonas/virology , Viral Proteins/chemistry , Amino Acid Sequence , Calorimetry, Differential Scanning , Circular Dichroism , Kinetics , Molecular Sequence Data , Sequence Alignment , Sequence Homology, Amino Acid , Spectrophotometry , Thermodynamics , Viral Proteins/pharmacology
15.
Genetika ; 41(4): 455-65, 2005 Apr.
Article in Russian | MEDLINE | ID: mdl-15909907

ABSTRACT

Bacteriophages of the family Myoviridae represent one of the most widespread domains of the biosphere substantially affecting the ecological balance of microorganisms. Interestingly, sequence analysis of genomic DNAs of large bacteriophages revealed many genes coding for proteins with unknown functions. A new approach is proposed to improve the functional identification of genes. This approach is based on comparing the genome sequence for phylogenetically and morphologically related phages showing no considerable homology at the level of genomic DNA. It is assumed that gene functions essential for the development of phages of a given family are conserved and that the corresponding genes code for similar orthologous proteins even when lacking sequence homology. The genome was sequenced and compared for two Pseudomonas aeruginosa giant bacteriophages, phiKZ and EL, which belong to a group of (phiKZ-related phages. A substantial difference in genome organization was observed, suggesting specific features of phage evolution. In addition, the problem of the minimal genome of the superfamily is discussed on the basis of the difference in size and structure between the phiKZ and EL genomes.


Subject(s)
Evolution, Molecular , Genome, Viral , Pseudomonas Phages/genetics , Viral Proteins/genetics , Base Sequence , Molecular Sequence Data , Pseudomonas aeruginosa , Sequence Analysis, DNA
17.
J Biotechnol ; 115(3): 249-60, 2005 Feb 09.
Article in English | MEDLINE | ID: mdl-15639087

ABSTRACT

Two family 11 endoxylanases (EC 3.2.1.8) were functionally displayed on the surface of bacteriophage M13. The genes encoding endo-1,4-xylanase I from Aspergillus niger (ExlA) and endo-1,4-xylanase A from Bacillus subtilis (XynA) were fused to the gene encoding the minor coat protein g3p in phagemid vector pHOS31. Phage rescue resulted in functional monovalent display of the enzymes as was demonstrated by three independent tests. Firstly, purified recombinant phage particles showed a clear hydrolytic activity in an activity assay based on insoluble, chromagenic arabinoxylan substrate. Secondly, specific binding of endoxylanase displaying phages to immobilized endoxylanase inhibitors was demonstrated by interaction ELISA. Finally, two rounds of selection and amplification in a biopanning procedure against immobilized endoxylanase inhibitor were performed. Phages displaying endoxylanases were strongly enriched from background phages displaying unrelated proteins. These results open perspectives to use phage display for analysing protein-protein interactions at the interface between endoxylanases and their inhibitors. In addition, this technology should enable engineering of endoxylanases into novel variants with altered binding properties towards endoxylanase inhibitors.


Subject(s)
Aspergillus niger/enzymology , Bacillus subtilis/enzymology , Bacteriophage M13/enzymology , Endo-1,4-beta Xylanases/metabolism , Membrane Proteins/metabolism , Peptide Library , Protein Interaction Mapping/methods , Aspergillus niger/genetics , Bacillus subtilis/genetics , Bacteriophage M13/genetics , Cloning, Molecular , Endo-1,4-beta Xylanases/genetics , Gene Expression Regulation, Enzymologic/physiology , Gene Expression Regulation, Viral/physiology , Protein Engineering/methods , Recombinant Proteins/metabolism
18.
Protein Pept Lett ; 12(7): 645-8, 2005 Oct.
Article in English | MEDLINE | ID: mdl-16522177

ABSTRACT

Gene 17 product (gp17) of the Pseudomonas aeruginosa-infecting bacteriophage phiKMV shows in silico similarity to T7 DNA ligase. In a semi-quantitative activity assay, it is shown that gp17 is a functional, ATP-dependent DNA ligase, in spite of some structural differences related to DNA-binding properties). Enzymatic activity of His6-based purified expression product was optimised (4 degrees C at 24h for sticky end double-stranded DNA fragments) and estimated at 0.5 Weiss U/microg.


Subject(s)
Bacteriophages/enzymology , DNA Ligases/metabolism , Amino Acid Sequence , Bacteriophages/genetics , Computational Biology , Conserved Sequence , DNA Ligase ATP , DNA Ligases/chemistry , DNA Ligases/genetics , DNA Ligases/isolation & purification , Models, Molecular , Molecular Sequence Data , Phylogeny , Protein Structure, Tertiary , Sequence Alignment
19.
Cell Mol Life Sci ; 61(21): 2753-9, 2004 Nov.
Article in English | MEDLINE | ID: mdl-15549178

ABSTRACT

Pseudomonas aeruginosa bacteriophage phiKMV is a T7-like lytic phage. Liquid chromatography-mass spectrometry of the structural proteins revealed gene product 36 (gp36) as part of the phiKMV phage particle. The presence of a lysozyme domain in the C terminal of this protein (gp36C) was verified by turbidimetric assays on chloroform-treated P. aeruginosa PAO1 and Escherichia coli WK6 cells. The molecular mass (20,884 Da) and pI (6.4) of recombinant gp36C were determined, as were the optimal enzymatic conditions (pH 6.0 in 16.7 mM phosphate buffer) and activity (4800 U/mg). Recombinant gp36C is a highly thermostable lysozyme, retaining 26% of its activity after 2 h at 100 degrees C and 21% after autoclaving. This thermostability could prove an interesting characteristic for food conservation technology.


Subject(s)
Bacteriophages/enzymology , Muramidase/chemistry , Muramidase/metabolism , Amino Acid Sequence , Enzyme Stability , Hydrogen-Ion Concentration , Molecular Sequence Data , Molecular Weight , Muramidase/isolation & purification , Protein Structure, Tertiary , Sequence Alignment , Temperature
20.
JBR-BTR ; 85(5): 260-3, 2002.
Article in English | MEDLINE | ID: mdl-12463503

ABSTRACT

A 23-year-old man was admitted to the hospital because of dyspnea. Chest X-ray showed reticulo-nodular opacities. The crazy paving appearance on high-resolution CT was highly suggestive of pulmonary alveolar proteinosis. Histologic examination confirmed the diagnosis. Pulmonary alveolar proteinosis is a rare disease but an important diagnosis to make as treatment with pulmonary lavage is curative in a large proportion of patients.


Subject(s)
Pulmonary Alveolar Proteinosis/diagnostic imaging , Tomography, X-Ray Computed , Adult , Biopsy , Bronchoalveolar Lavage , Bronchoscopy , Diagnosis, Differential , Dyspnea/etiology , Humans , Lung/diagnostic imaging , Lung/pathology , Male , Pulmonary Alveolar Proteinosis/pathology , Pulmonary Alveolar Proteinosis/therapy
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