Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 8 de 8
Filter
Add more filters










Database
Language
Publication year range
1.
Transpl Infect Dis ; 13(1): 73-9, 2011 Feb.
Article in English | MEDLINE | ID: mdl-20738833

ABSTRACT

Dematiaceous fungi are an opportunistic pathogen seen in solid organ transplant recipients. We report 2 cases of Exophiala infection and review the medical literature to summarize the spectrum of disease this pathogen can cause in this patient population.


Subject(s)
Antifungal Agents/therapeutic use , Dermatomycoses , Exophiala/isolation & purification , Kidney Transplantation/adverse effects , Aged , Arm/pathology , Dermatomycoses/diagnosis , Dermatomycoses/drug therapy , Dermatomycoses/microbiology , Dermatomycoses/surgery , Exophiala/drug effects , Fatal Outcome , Humans , Male , Skin/microbiology , Skin/pathology , Treatment Outcome
2.
Transpl Infect Dis ; 11(4): 337-40, 2009 Aug.
Article in English | MEDLINE | ID: mdl-19392730

ABSTRACT

Legionella feeleii is a rare cause of community-acquired pneumonia that occurs in immunocompromised hosts who are often receiving corticosteroid therapy. We report a 69-year-old man who underwent bone marrow transplantation and developed pneumonia due to L. feeleii, and review the clinical characteristics of 7 cases of L. feeleii infection reported in the literature.


Subject(s)
Bone Marrow Transplantation/adverse effects , Legionella/isolation & purification , Legionellosis , Pneumonia, Bacterial , Aged , Female , Humans , Legionella/classification , Legionellosis/diagnostic imaging , Legionellosis/microbiology , Legionellosis/pathology , Lung/microbiology , Lung/pathology , Male , Pneumonia, Bacterial/diagnostic imaging , Pneumonia, Bacterial/microbiology , Pneumonia, Bacterial/pathology , Tomography, X-Ray Computed
3.
Transpl Infect Dis ; 10(2): 137-41, 2008 Apr.
Article in English | MEDLINE | ID: mdl-17605735

ABSTRACT

Strongyloides stercoralis is a helminth with the ability to autoinfect the human host and persist asymptomatically for several years. Immunosuppression can accelerate autoinfection and result in Strongyloides hyperinfection syndrome (SHS), which is associated with significant morbidity and mortality. Immunosuppressed solid organ transplant recipients, particularly in the setting of rejection, are at increased risk for reactivation of latent infections, such as Strongyloides. We describe a case of SHS in an intestinal transplant recipient; we hypothesize that she acquired the infection from the donor. We also review the current literature and address both prophylaxis and treatment of strongyloidiasis in the solid organ transplant patient.


Subject(s)
Anthelmintics/therapeutic use , Immunocompromised Host , Intestines/transplantation , Strongyloides stercoralis/pathogenicity , Strongyloidiasis/diagnosis , Animals , Female , Humans , Middle Aged , Postoperative Complications , Strongyloidiasis/drug therapy , Strongyloidiasis/etiology , Syndrome , Treatment Outcome
4.
J Bacteriol ; 179(11): 3736-45, 1997 Jun.
Article in English | MEDLINE | ID: mdl-9171424

ABSTRACT

Entamoeba histolytica is an amitochondriate protozoan parasite with numerous bacterium-like fermentation enzymes including the pyruvate:ferredoxin oxidoreductase (POR), ferredoxin (FD), and alcohol dehydrogenase E (ADHE). The goal of this study was to determine whether the genes encoding these cytosolic E. histolytica fermentation enzymes might derive from a bacterium by horizontal transfer, as has previously been suggested for E. histolytica genes encoding heat shock protein 60, nicotinamide nucleotide transhydrogenase, and superoxide dismutase. In this study, the E. histolytica por gene and the adhE gene of a second amitochondriate protozoan parasite, Giardia lamblia, were sequenced, and their phylogenetic positions were estimated in relation to POR, ADHE, and FD cloned from eukaryotic and eubacterial organisms. The E. histolytica por gene encodes a 1,620-amino-acid peptide that contained conserved iron-sulfur- and thiamine pyrophosphate-binding sites. The predicted E. histolytica POR showed fewer positional identities to the POR of G. lamblia (34%) than to the POR of the enterobacterium Klebsiella pneumoniae (49%), the cyanobacterium Anabaena sp. (44%), and the protozoan Trichomonas vaginalis (46%), which targets its POR to anaerobic organelles called hydrogenosomes. Maximum-likelihood, neighbor-joining, and parsimony analyses also suggested as less likely E. histolytica POR sharing more recent common ancestry with G. lamblia POR than with POR of bacteria and the T. vaginalis hydrogenosome. The G. lamblia adhE encodes an 888-amino-acid fusion peptide with an aldehyde dehydrogenase at its amino half and an iron-dependent (class 3) ADH at its carboxy half. The predicted G. lamblia ADHE showed extensive positional identities to ADHE of Escherichia coli (49%), Clostridium acetobutylicum (44%), and E. histolytica (43%) and lesser identities to the class 3 ADH of eubacteria and yeast (19 to 36%). Phylogenetic analyses inferred a closer relationship of the E. histolytica ADHE to bacterial ADHE than to the G. lamblia ADHE. The 6-kDa FD of E. histolytica and G. lamblia were most similar to those of the archaebacterium Methanosarcina barkeri and the delta-purple bacterium Desulfovibrio desulfuricans, respectively, while the 12-kDa FD of the T. vaginalis hydrogenosome was most similar to the 12-kDa FD of gamma-purple bacterium Pseudomonas putida. E. histolytica genes (and probably G. lamblia genes) encoding fermentation enzymes therefore likely derive from bacteria by horizontal transfer, although it is not clear from which bacteria these amebic genes derive. These are the first nonorganellar fermentation enzymes of eukaryotes implicated to have derived from bacteria.


Subject(s)
Alcohol Dehydrogenase/genetics , Entamoeba histolytica/genetics , Evolution, Molecular , Ferredoxins/genetics , Ketone Oxidoreductases/genetics , Amino Acid Sequence , Animals , Entamoeba histolytica/enzymology , Genes, Bacterial , Molecular Sequence Data , Phylogeny , Pyruvate Synthase , Sequence Alignment
5.
Mol Biochem Parasitol ; 85(2): 139-47, 1997 Apr.
Article in English | MEDLINE | ID: mdl-9106188

ABSTRACT

Entamoeba histolytica (Eh) and Entamoeba dispar (Ed) are protozoan parasites that infect hundreds of millions of persons. In the colonic lumen, amebae form chitin-walled cysts, the infectious stage of the parasite. Entamoeba invadens (Ei), which infects reptiles and is a model for amebic encystation, produces chitin synthase and chitinase during encystation. Ei cysts formation is blocked by the chitinase-inhibitor allosamidin. Here molecular cloning techniques were used to identify homologous genes of Eh, Ed, and Ei that encode chitinases (EC 3.2.1.14). The Eh gene (Eh cht1) predicts a 507-amino acid (aa) enzyme, which has 93 and 74% positional identities with Ed and Ei chitinases, respectively. The Entamoeba chitinases have signal sequences, followed by acidic and hydrophilic sequences composed of multiple tandemly arranged 7-aa repeats (Eh and Ed) or repeats varying in length (Ei). The aa compositions of the chitinase repeats are similar to those of the repeats of the Eh and Ed Ser-rich proteins. The COOH-terminus of each chitinase has a catalytic domain, which resembles those of Brugia malayi (33% positional identity) and Manduca sexta (29%). Recombinant entamoeba chitinases are precipitated by chitin and show chitinase activity with chitooligosacharide substrates. Consistent with previous biochemical data, chitinase mRNAs are absent in Ei trophozoites and accumulate to maximal levels in Ei encysting for 48 h.


Subject(s)
Chitinases/biosynthesis , Chitinases/genetics , Entamoeba histolytica/enzymology , Entamoeba histolytica/genetics , Entamoeba/genetics , Amino Acid Sequence , Animals , Base Sequence , Chitinases/chemistry , Cloning, Molecular , Entamoeba/enzymology , Entamoeba histolytica/growth & development , Gene Expression , Genes, Protozoan/genetics , Molecular Sequence Data , Polymerase Chain Reaction , Protein Binding , Recombinant Proteins/biosynthesis , Recombinant Proteins/genetics , Recombinant Proteins/isolation & purification , Repetitive Sequences, Nucleic Acid , Sequence Analysis , Sequence Homology, Amino Acid , Sequence Homology, Nucleic Acid
SELECTION OF CITATIONS
SEARCH DETAIL
...