<i>In vivo</i> generation of linear plasmids with addition of telomeric sequences by <i>Histoplasma capsulatum</i>

Woods, Jon P.; Goldman, William E.

doi:10.1111/j.1365-2958.1992.tb01796.x

Cited by 61 publications

(78 citation statements)

References 25 publications

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“…We prepared H. capsulatum strain G217B genomic DNA as previously described (37). We PCR amplified the YPS3 open reading frame from G217B genomic DNA.…”

Section: Methodsmentioning

confidence: 99%

Surface Localization of the Yps3p Protein of Histoplasma capsulatum

Bohse

Woods

2005

Eukaryot Cell

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The YPS3 gene of Histoplasma capsulatum encodes a protein that is both resident in the cell wall and also released into the culture medium. This protein is produced only during the pathogenic yeast phase of infection and is also expressed differently in H. capsulatum strains that differ in virulence. We investigated the cellular localization of Yps3p. We demonstrated that the cell wall fraction of Yps3p was surface localized in restriction fragment length polymorphism class 2 strains. We also established that Yps3p released into the G217B culture supernatant binds to the surface of strains that do not naturally express the protein. This binding was saturable and occurred within 5 min of exposure and occurred similarly with live and heat-killed H. capsulatum. Flow cytometric analysis of H. capsulatum after enzymatic treatments was consistent with Yps3p binding to chitin, a carbohydrate polymer that is a component of fungal cell walls. Polysaccharide binding assays demonstrated that chitin but not cellulose binds to and extracts Yps3p from culture supernatants.

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“…We prepared H. capsulatum strain G217B genomic DNA as previously described (37). We PCR amplified the YPS3 open reading frame from G217B genomic DNA.…”

Section: Methodsmentioning

confidence: 99%

Surface Localization of the Yps3p Protein of Histoplasma capsulatum

Bohse

Woods

2005

Eukaryot Cell

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“…The Histoplasma capsulatum virulent strain G-217B (ATCC 26032 ; generously provided by W. E. Goldman, Washington University, St Louis, MO, USA) was used in all experiments. H. capsulatum yeast cultures were grown at 37 mC with gentle shaking in 3 % (v\v) glycerol or 2 % (w\v) glucose HMM medium (Worsham & Goldman, 1988 Woods & Goldman (1992), except that the lysed spheroplast extract was incubated with proteinase K overnight at 50 mC. For restriction enzyme digestions, PCR reactions or synthesis of radiolabelled probes, plasmid DNA was purified from E. coli by the CTAB method (Del Sal et al, 1989).…”

Section: Methodsmentioning

confidence: 99%

Redundancy, phylogeny and differential expression of Histoplasma capsulatum catalases The GenBank accession numbers for the cDNA sequences reported in this paper are AF139985 (CATB), AF189368 (CATA) and AF189369 (CATP).

et al. 2002

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Histoplasma capsulatum produces an extracellular catalase termed M antigen, which is similar to catalase B of Aspergillus and Emericella species. Evidence is presented here for two additional catalase isozymes in H. capsulatum. Catalase A is highly similar to a large-subunit catalase in Aspergillus and Emericella species, while catalase P is a small-subunit catalase protein with greatest similarity to known peroxisomal catalases of animals and Saccharomycotina yeasts. Complete cDNAs for the CATA and CATP genes (encoding catalases A and P, respectively) were isolated. The transcriptional expression of the H. capsulatum CATA, CATB (M antigen) and CATP genes was assessed by Northern blot hybridizations on total RNA. Results at the transcript levels for these genes are shown for three conditions : cell morphology (mycelial versus yeast phase cells), oxidative stress (in response to a challenge with H 2 O 2 ) and carbon source (glucose vs glycerol). Collectively, these results demonstrated regulation of CATA by both cell morphology and oxidative stress, but not by carbon source, and regulation of CATB and CATP by carbon source but not cell morphology or oxidative stress. A phylogenetic analysis of presently available catalase sequences and intron residences was done. The results support a model for evolution of eukaryotic monofunctional catalase genes from prokaryotic genes.

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“…capsulatum strain G217B (ATCC 26032; a kind gift of William Goldman, Washington University, St. Louis, MO) was grown in Histoplasma Macrophage Medium (HMM) broth (Worsham and Goldman, 1988) or on HMM agar plates supplemented with 5 mg/ml bovine serum albumin (BSA). H. capsulatum strain G217B ura5 Ϫ (a kind gift of William Goldman; Woods and Goldman, 1992) was grown in HMM broth supplemented with 0.2 mg/ml uracil (Sigma-Aldrich, St. Louis, MO). After transformation with URA5-containing plasmids, G217B ura5 Ϫ was grown in HMM broth or on HMM agarose plates with no uracil supplementation.…”

Section: Strains and Culture Growthmentioning

confidence: 99%

Identification ofHistoplasma capsulatumTranscripts Induced in Response to Reactive Nitrogen Species

Nittler

Hocking-Murray

Foo

et al. 2005

MBoC

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The pathogenic fungus Histoplasma capsulatum escapes innate immune defenses and colonizes host macrophages during infection. After the onset of adaptive immunity, the production of the antimicrobial effector nitric oxide ( ⅐ NO) restricts H. capsulatum replication. However, H. capsulatum can establish persistent infections, indicating that it survives in the host despite exposure to reactive nitrogen species (RNS). To understand how H. capsulatum responds to RNS, we determined the transcriptional profile of H. capsulatum to ⅐ NO-generating compounds using a shotgun genomic microarray. We identified 695 microarray clones that were induced >4-fold upon nitrosative stress. Because our microarray clones were generated from random fragments of genomic DNA, they did not necessarily correspond to H. capsulatum open reading frames. To identify induced genes, we used high-density oligonucleotide tiling arrays to determine the genomic boundaries and coding strand of 153 RNS-induced transcripts. Homologues of these genes in other organisms are involved in iron acquisition, energy production, stress response, protein folding/degradation, DNA repair, and ⅐ NO detoxification. Ectopic expression of one of these genes, a P450 nitric oxide reductase homologue, was sufficient to increase resistance of H. capsulatum to RNS in culture. We propose that H. capsulatum uses the pathways identified here to cope with RNS-induced damage during pathogenesis.

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In vivo generation of linear plasmids with addition of telomeric sequences by Histoplasma capsulatum

Cited by 61 publications

References 25 publications

Surface Localization of the Yps3p Protein of Histoplasma capsulatum

Surface Localization of the Yps3p Protein of Histoplasma capsulatum

Redundancy, phylogeny and differential expression of Histoplasma capsulatum catalases The GenBank accession numbers for the cDNA sequences reported in this paper are AF139985 (CATB), AF189368 (CATA) and AF189369 (CATP).

Identification ofHistoplasma capsulatumTranscripts Induced in Response to Reactive Nitrogen Species

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