Mycorrhizal Functioning. An Integrative Plant Fungal Process.

1994 ◽  
Vol 82 (2) ◽  
pp. 427
Author(s):  
E. I. Newman ◽  
M. F. Allen
Keyword(s):  
Fungal Process

scholarly journals Solitary Tracheobronchial Papilloma: Cytomorphology and ancillary studies with histologic correlation

CytoJournal ◽  
2011 ◽  
Vol 8 ◽  
pp. 6 ◽  
Author(s):  
Tee U. Lang ◽  
Walid E. Khalbuss ◽  
Sara E. Monaco ◽  
Liron Pantanowitz
Keyword(s):  
Squamous Cell ◽  
Squamous Metaplasia ◽  
Hpv Infection ◽  
Tracheobronchial Tree ◽  
Surface Erosion ◽  
Severe Dysplasia ◽  
Surgical Biopsy ◽  
Squamous Cells ◽  
Rare Benign Tumor ◽  
Fungal Process

Solitary tracheobronchial papilloma (STBP) is a rare benign tumor that primarily involves the tracheobronchial tree. Human papilloma virus (HPV) infection is associated with dysplasia and a high risk of carcinoma in these lesions. The cytomorphology of STBP is not well established in the literature. Our aim is to characterize the cytomorphologic features of STBP, with histologic correlation in a series of 6 patients — 4 males and 2 females — with a mean age of 67 years (range, 53-88 years). There were 5 biopsy-proven squamous papillomas and 1 glandular papilloma. On surgical biopsy, squamous papillomas exhibited cytological atypia (4 graded mild and 1 graded moderate with focal severe dysplasia), surface erosion, and inflammation. Cytology specimens available for review included a combination of 4 fine-needle aspirations (FNAs), 2 bronchoalveolar lavages and 2 (of 3) bronchial brushings. Cytologic findings associated with squamous papillomas included atypical squamous cells and rare squamous cell resembling koilocyte in 1 bronchial brushing. Sheets of squamous cells were identified in another specimen. Several cases had a prominent background of acute inflammation, and candida was present in 1 specimen. HPV in-situ hybridization was positive in 1 case and negative in 2 cases. A p16 immunocytochemical stain performed on 1 cell block was negative. In conclusion, although STBP is a rare neoplasm, these cases may be encountered in respiratory cytology samples. FNA of papillomas yields fewer lesional cells compared to exfoliative samples. These lesions may be mistaken in cytology specimens for squamous cell carcinoma, squamous-lined cavitary lesions, an infectious (fungal) process, reactive squamous metaplasia, or oral contamination.

scholarly journals Biochemical and genetic analysis of Ecm14, a conserved fungal pseudopeptidase

2020 ◽  
Author(s):  
R Christian McDonald ◽  
Matthew J Schott ◽  
Temitope A Idowu ◽  
Peter J Lyons
Keyword(s):  
Enzyme Activity ◽  
Large Scale ◽  
Structure And Function ◽  
Activation Mechanism ◽  
Marker Genes ◽  
Synthetic Lethal ◽  
Fungal Process ◽  
And Function

Abstract Background. Like most major enzyme families, the M14 family of metallocarboxypeptidases (MCPs) contains a number of pseudoenzymes predicted to lack enzyme activity and with poorly characterized molecular function. The genome of the yeast Saccharomyces cerevisiae encodes one member of the M14 MCP family, a pseudoenzyme named Ecm14 proposed to function in the extracellular matrix. In order to better understand the function of such pseudoenzymes, we studied the structure and function of Ecm14 in S. cerevisiae. Results. A phylogenetic analysis of Ecm14 in fungi found it to be conserved throughout the ascomycete phylum, with a group of related pseudoenzymes found in basidiomycetes. To investigate the structure and function of this conserved protein, His6-tagged Ecm14 was overexpressed in Sf9 cells and purified. The prodomain of Ecm14 was cleaved in vivo and in vitro by endopeptidases, suggesting an activation mechanism; however, no activity was detectable using standard carboxypeptidase substrates. In order to determine the function of Ecm14 using an unbiased screen, we undertook a synthetic lethal assay. Upon screening approximately 27,000 yeast colonies, twenty-two putative synthetic lethal clones were identified. Further analysis showed many to be synthetic lethal with auxotrophic marker genes and requiring multiple mutations, suggesting that there are few, if any, single S. cerevisiae genes that present synthetic lethal interactions with ecm14Δ. Conclusions. We show in this study that Ecm14, although lacking detectable enzyme activity, is a conserved carboxypeptidase-like protein that is secreted from cells and is processed to a mature form by the action of an endopeptidase. Our study and datasets from other recent large-scale screens suggest a role for Ecm14 in processes such as vesicle-mediated transport and aggregate invasion, a fungal process that has been selected against in modern laboratory strains of S. cerevisiae.

scholarly journals Persistence pays: a case of primary cutaneous B-cell lymphoma masked by granulomas

2020 ◽  
Vol 7 (1) ◽  
pp. 126
Author(s):  
Ruple Jairath ◽  
Neil K. Jairath ◽  
Timothy Vandenboom ◽  
Michael T. Goldfarb
Keyword(s):  
B Cell ◽  
Cell Lymphoma ◽  
Delayed Diagnosis ◽  
B Cell Lymphoma ◽  
Skin Lesions ◽  
Clonal Proliferation ◽  
Large B Cell Lymphoma ◽  
Initial Biopsy ◽  
Fungal Process ◽  
Large B Cell

<p class="abstract">Primary cutaneous diffuse large B cell lymphoma is a form of cutaneous lymphoma characterized by a clonal proliferation of B cells that is often presents with a delayed diagnosis, and therefore often carries poor prognosis. We report a 77-year-old female presenting with a shin lesion resembling a deep dermal or fungal process. Initial biopsy revealed superficial and deep mixed granulomatous inflammatory infiltrate, which suggested an initial diagnosis of Majocchi’s granuloma, despite negative fungal cultures. Despite treatment, the progressive worsening of the skin lesions prompted multiple repeat biopsies, which eventually revealed CD20, Bcl-2, and Bcl-6 staining, loss of CD3 and CD30, and high Ki67, compatible with a cutaneous high-grade B-cell lymphoma. Clinical presentations of primary cutaneous diffuse large B cell lymphoma can mimic several different clinical entities, rarely including granulomatous disease, such as a fungal pathology. This report highlights the importance of persistence and a multimodal approach to the diagnosis of unidentified skin lesions, especially in the setting of failure to respond to standard therapies.</p>

scholarly journals Biochemical and genetic analysis of Ecm14, a conserved fungal pseudopeptidase

2020 ◽  
Vol 21 (1) ◽  
Author(s):  
R. Christian McDonald ◽  
Matthew J. Schott ◽  
Temitope A. Idowu ◽  
Peter J. Lyons
Keyword(s):  
Enzyme Activity ◽  
Large Scale ◽  
Structure And Function ◽  
Activation Mechanism ◽  
Marker Genes ◽  
Synthetic Lethal ◽  
Fungal Process ◽  
And Function

Abstract Background Like most major enzyme families, the M14 family of metallocarboxypeptidases (MCPs) contains a number of pseudoenzymes predicted to lack enzyme activity and with poorly characterized molecular function. The genome of the yeast Saccharomyces cerevisiae encodes one member of the M14 MCP family, a pseudoenzyme named Ecm14 proposed to function in the extracellular matrix. In order to better understand the function of such pseudoenzymes, we studied the structure and function of Ecm14 in S. cerevisiae. Results A phylogenetic analysis of Ecm14 in fungi found it to be conserved throughout the ascomycete phylum, with a group of related pseudoenzymes found in basidiomycetes. To investigate the structure and function of this conserved protein, His6-tagged Ecm14 was overexpressed in Sf9 cells and purified. The prodomain of Ecm14 was cleaved in vivo and in vitro by endopeptidases, suggesting an activation mechanism; however, no activity was detectable using standard carboxypeptidase substrates. In order to determine the function of Ecm14 using an unbiased screen, we undertook a synthetic lethal assay. Upon screening approximately 27,000 yeast colonies, twenty-two putative synthetic lethal clones were identified. Further analysis showed many to be synthetic lethal with auxotrophic marker genes and requiring multiple mutations, suggesting that there are few, if any, single S. cerevisiae genes that present synthetic lethal interactions with ecm14Δ. Conclusions We show in this study that Ecm14, although lacking detectable enzyme activity, is a conserved carboxypeptidase-like protein that is secreted from cells and is processed to a mature form by the action of an endopeptidase. Our study and datasets from other recent large-scale screens suggest a role for Ecm14 in processes such as vesicle-mediated transport and aggregate invasion, a fungal process that has been selected against in modern laboratory strains of S. cerevisiae.

Antimicrobial effect of silver nanoparticles produced by fungal process on cotton fabrics

2010 ◽  
Vol 80 (3) ◽  
pp. 779-782 ◽  
Author(s):  
M.H. El-Rafie ◽  
A.A. Mohamed ◽  
Th.I. Shaheen ◽  
A. Hebeish
Keyword(s):  
Silver Nanoparticles ◽  
Antimicrobial Effect ◽  
Cotton Fabrics ◽  
Fungal Process

Antibacterial Effect of Silver Nanoparticles Produced by Fungal Process on Textile Fabrics and Their Effluent Treatment

2007 ◽  
Vol 3 (2) ◽  
pp. 203-208 ◽  
Author(s):  
Nelson Durán ◽  
Priscyla D. Marcato ◽  
Gabriel I. H. De Souza ◽  
Oswaldo L. Alves ◽  
Elisa Esposito
Keyword(s):  
Silver Nanoparticles ◽  
Antibacterial Effect ◽  
Effluent Treatment ◽  
Textile Fabrics ◽  
Fungal Process

scholarly journals Biochemical and genetic analysis of Ecm14, a conserved fungal pseudopeptidase

2020 ◽  
Author(s):  
R Christian McDonald ◽  
Matthew J Schott ◽  
Temitope A Idowu ◽  
Peter J Lyons
Keyword(s):  
Enzyme Activity ◽  
Large Scale ◽  
Structure And Function ◽  
Activation Mechanism ◽  
Marker Genes ◽  
Synthetic Lethal ◽  
Fungal Process ◽  
And Function

Abstract Background. Like most major enzyme families, the M14 family of metallocarboxypeptidases (MCPs) contains a number of pseudoenzymes predicted to lack enzyme activity and with poorly characterized molecular function. The genome of the yeast S. cerevisiae encodes one member of the M14 MCP family, a pseudoenzyme named Ecm14 proposed to function in the extracellular matrix. In order to better understand the function of such pseudoenzymes, we studied the structure and function of Ecm14 in S. cerevisiae. Results. A phylogenetic analysis of Ecm14 in fungi found it to be conserved throughout the ascomycete phylum, with a group of related pseudoenzymes found in basidiomycetes. To investigate the structure and function of this conserved protein, his6-tagged Ecm14 was overexpressed in Sf9 cells and purified. The prodomain of Ecm14 was cleaved in vivo and in vitro by endopeptidases, suggesting an activation mechanism; however, no activity was detectable using standard carboxypeptidase substrates. In order to determine the function of Ecm14 using an unbiased screen, we undertook a synthetic lethal assay. Upon screening approximately 27,000 yeast colonies, twenty-two putative synthetic lethal clones were identified. Further analysis showed many to be synthetic lethal with auxotrophic marker genes and requiring multiple mutations, suggesting that there are few, if any, single S. cerevisiae genes that present synthetic lethal interactions with ecm14. Conclusions. We show in this study that Ecm14, although lacking detectable enzyme activity, is a conserved carboxypeptidase-like protein that is secreted from cells and is processed to a mature form by the action of an endopeptidase. Our study and datasets from other recent large-scale screens suggest a role for Ecm14 in processes such as vesicle-mediated transport and aggregate invasion, a fungal process that has been selected against in modern laboratory strains of S. cerevisiae.

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