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At least 19 recordsLinked to original sources
PubMed1968

Development and use of a polyvalent conjugate to differentiate Histoplasma capsulatum and Histoplasma duboisii from other pathogens.

Previous investigations have demonstrated the existence of five Histoplasma capsulatum serotypes. Available specific fluorescent-antibody reagents stain only four of the five serotypes. Antibodies produced against the most complete H. capsulatum serotype were labeled with fluorescein isothiocyanate to develop a reagent specific for H. capsulatum that was reactive with all the known serotypes. The unadsorbed reagent not only stained all the H. capsulatum serotypes, but it also stained cultures of Blastomyces dermatitidis, H. duboisii, several Candida species, and a variety of other fungi. Adsorption of the conjugate with antigens of C. albicans produced a reagent that intensely stained only H. capsulatum, H. duboisii, and B. dermatitidis. Differentiation of B. dermatitidis from the Histoplasma species was accomplished by application of a B. dermatitidis specific fluorescent antibody to antigens positive with the H. capsulatum reagent. At present, differentiation of H. capsulatum from H. duboisii may be accomplished only by animal inoculation. Our data substantiate the antigenic relationships hypothesized earlier, and they indicate that H. capsulatum shares at least two antigens with the other fungi that were studied.

Antibodies↗
PubMedDate not supplied

Production of extracellular collagenolytic proteinases by Histoplasma capsulatum var. duboisii and Histoplasma capsulatum var. capsulatum in the yeast phase.

Yeast cultures of Histoplasma capsulatum var. duboisii and H. capsulatum var. capsulatum in collagen containing defined, semi-defined and complex media produced extracellular collagenolytic proteinases, assayed using 4-phenylazo-benzyloxycarbonyl-L-propyl-L-leucyl- glycyl-L-propyl-D-arginine, a specific collagenase substrate. Significant levels of hydroxyproline were measured in the cultures and clear zones of hydrolysis were produced in collagen buffer agar by the crude enzyme preparations. Hydrolysis of casein and bovine serum albumin at pH 8 suggests the presence, in the crude enzymes, of multiple proteinases rather than a collagenase with broad substrate specificity since collagenolytic activity was not detected at pH 5 and above. Collagenolytic activities in the crude enzymes of both fungi were optimal at pH 4, 40 degrees C and were inhibited by EDTA, phosphoramidion and aprotinin indicating a metallo-serine nature. The molecular weights, estimated by column chromatography, were both 17 kD. The enzymes probably constitute a shared antigen. A probable role in the pathogenesis of histoplasmosis is discussed.

Amino Acid Sequence↗
PubMedDate not supplied

In vitro production of extracellular elastolytic proteinase by Histoplasma capsulatum var. duboisii and Histoplasma capsulatum var. capsulatum in the yeast phase.

Extracellular elastolytic proteinase was produced by yeast cultures of Histoplasma capsulatum var. duboisii and H. capsulatum var. capsulatum in three different induction media, assayed using elastin-orcein as the substrate. Medium-dependent variations in the time-course for enzyme production were observed and no peak was recorded. The proteinases hydrolysed both casein and bovine serum albumin indicating a broad substrate specificity. Both elastolytic proteinases had similar optimum pH (pH 8) and temperature (35 degrees C); over 90% residual elastolytic activity was measured in the crude enzymes of v. duboisii and v. capsulatum after incubation in the pH ranges 4.5-8.0 and 4.0-7.0 respectively, at 4 degrees C for 24 h. The proteinases were not significantly inhibited by any of the tested proteinase inhibitors. The molecular weights, estimated by column chromatography, were 23 kD. A probable role in the pathogenesis of histoplasmosis is discussed.

Histoplasma↗
PubMed1992

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

Histoplasma capsulatum is a dimorphic pathogenic fungus that is a major cause of respiratory and systemic mycosis. We previously developed a transformation system for Histoplasma and demonstrated chromosomal integration of transforming plasmid sequences. In this study, we describe another Histoplasma mechanism for maintaining transforming DNA i.e. the generation of modified, multicopy linear plasmids carrying DNA from the transforming Escherichia coli plasmid. Under selective conditions, these linear plasmids were stable and capable of retransforming Histoplasma without further modification. In vivo modification of the transforming DNA included duplication of plasmid sequence and telomeric addition at the termini of linear DNA. Apparently Histoplasma telomerase, like that of other organisms such as humans and Tetrahymena, is able to act on non-telomeric substrates. The terminus of a Histoplasma linear plasmid was cloned and shown to contain multiple repeats of GGGTTA, the telomeric repeat unit also found in vertebrates, trypanosomes, and slime moulds.

Base Sequence↗
PubMed1968

Inhibition of Histoplasma capsulatum by Candida albicans and other yeasts on Sabouraud's agar media.

The inhibition of growth of Histoplasma capsulatum by Candida albicans and other yeasts on Sabouraud's agar was investigated. Histoplasma (yeast-phase inoculum) was grown alone and in mixtures with yeasts at 25 C for 4-week periods. As few as 10 colonies of C. albicans completely inhibited the growth of approximately 50,000 potential colonies of Histoplasma. The pH was determined in cultures of 36 colonies of Candida on media containing 1, 2, and 4% glucose by spotting the agar with pH indicators. A drop in the pH became noticeable in all three media about the 3rd day of incubation, and a pH of 3.5 was reached in about 7 days. Subsequently, the pH remained almost stationary in the 4% glucose-agar, rose slowly in the 2% glucose-agar, and rose sharply in the 1% glucose-agar. The growth of Histoplasma was inhibited completely at pH 4 and below. When the pH was controlled in mixed cultures, some growth of Histoplasma was obtained. Substitution of maltose for glucose delayed the development of acidity and allowed the appearance of numerous mycelial colonies in the presence of Candida. This growth was arrested as soon as the medium became acid. Four other species which also acidified the Sabouraud's medium effected similar inhibition. It was thus shown that severe and prolonged acidity produced by some yeasts in the sugar-rich Sabouraud's media is alone sufficient to completely inhibit Histoplasma during the standard 4-week incubation of specimens such as sputum.

Candida↗
PubMed1990

Histoplasma capsulatum endophthalmitis after cataract extraction.

A 60-year-old white man from an area endemic for Histoplasma capsulatum presented with a vitreous wick, hypopyon iritis, and dense vitreitis 2 months after removal of an anterior chamber intraocular lens (IOL) for chronic iritis. A diagnostic vitrectomy was performed and H. capsulatum was cultured and identified 2 weeks later. Despite intravitreal and intravenous amphotericin as well as repeat vitrectomies, the inflammation worsened and the eye was removed. Results of histopathologic examination showed Histoplasma organisms along the vitreous wick, over the surface of the iris and ciliary body, and over the retina. No organisms were found in the choroid. Dalen-Fuchs-type nodules similar to those of sarcoid also were noted, but there was no evidence of granulomatous inflammation in the uvea. Because of his unilateral disease with Histoplasma in the vitreous wick, negative serology, and an absence of systemic infection, the authors believe that this patient had a previously unreported form of ocular Histoplasma, exogenous postoperative Histoplasma endophthalmitis.

Cataract Extraction↗
PubMed2000

Monitoring phase-specific gene expression in Histoplasma capsulatum with telomeric GFP fusion plasmids.

Dimorphism is an essential feature of Histoplasma capsulatum pathogenesis, and much attention has been focused on characteristics that are unique to the saprophytic mycelial phase or the parasitic yeast phase. Recently, we identified a secreted calcium-binding protein, CBP, that is produced in large amounts by yeast cells but is undetectable in mycelial cultures. In this study, the green fluorescent protein (GFP) was established as a reporter in H. capsulatum to study regulation of CBP1 expression in cultures and in single cells grown under different conditions and inside macrophages. One GFP version that was optimized for human codon usage yielded highly fluorescent Histoplasma yeast cells. By monitoring GFP fluorescence during the transition from mycelia to yeast, we demonstrated that the CBP1 promoter is only fully active after complete morphological conversion to the yeast form, indicating for the first time that CBP1 is developmentally regulated rather than simply temperature regulated. Continuous activity of the CBP1 promoter during infection of macrophages supports the hypothesis that CBP secretion plays an important role for Histoplasma survival within the phagolysosome. Broth cultures of Histoplasma yeasts carrying a CBP-GFP protein fusion construct were able to secrete a full-length fluorescent fusion protein that remained localized within the phagolysosomes of infected macrophages. Additionally, a comparison of two Histoplasma strains carrying the CBP1 promoter fusion construct either epichromosomally or integrated into the chromosome revealed cell-to-cell variation in plasmid copy number due to uneven plasmid partitioning into daughter cells.

Animals↗