scholarly journals Mapping N-Linked Glycosylation Sites in the Secretome and Whole Cells of Aspergillus niger Using Hydrazide Chemistry and Mass Spectrometry

2011 ◽  
Vol 11 (1) ◽  
pp. 143-156 ◽  
Author(s):  
Lu Wang ◽  
Uma K. Aryal ◽  
Ziyu Dai ◽  
Alisa C. Mason ◽  
Matthew E. Monroe ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Aspergillus Niger ◽  
Whole Cells ◽  
Glycosylation Sites

A Mucin-Specific Protease Enables Molecular and Functional Analysis of Human Cancer-Associated Mucins

2018 ◽  
Author(s):  
Stacy A. Malaker ◽  
Kayvon Pedram ◽  
Michael J. Ferracane ◽  
Elliot C. Woods ◽  
Jessica Kramer ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Mechanisms ◽  
Cultured Cells ◽  
High Resolution Mass Spectrometry ◽  
Human Cancer ◽  
Glycosylation Sites ◽  
Bacterial Protease ◽  
Specific Protease ◽  
To Come ◽  
And Function

<div> <div> <div> <p>Mucins are a class of highly O-glycosylated proteins that are ubiquitously expressed on cellular surfaces and are important for human health, especially in the context of carcinomas. However, the molecular mechanisms by which aberrant mucin structures lead to tumor progression and immune evasion have been slow to come to light, in part because methods for selective mucin degradation are lacking. Here we employ high resolution mass spectrometry, polymer synthesis, and computational peptide docking to demonstrate that a bacterial protease, called StcE, cleaves mucin domains by recognizing a discrete peptide-, glycan-, and secondary structure- based motif. We exploited StcE’s unique properties to map glycosylation sites and structures of purified and recombinant human mucins by mass spectrometry. As well, we found that StcE will digest cancer-associated mucins from cultured cells and from ovarian cancer patient-derived ascites fluid. Finally, using StcE we discovered that Siglec-7, a glyco-immune checkpoint receptor, specifically binds sialomucins as biological ligands, whereas the related Siglec-9 receptor does not. Mucin-specific proteolysis, as exemplified by StcE, is therefore a powerful tool for the study of glycoprotein structure and function and for deorphanizing mucin-binding receptors. </p> </div> </div> </div>

Localization ofo-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry

1998 ◽  
Vol 33 (4) ◽  
pp. 358-362 ◽  
Author(s):  
Franz-Georg Hanisch ◽  
Brian N. Green ◽  
Robert Bateman ◽  
Jasna Peter-Katalinic
Keyword(s):  
Mass Spectrometry ◽  
Tandem Repeats ◽  
Glycosylation Sites ◽  
Esi Mass Spectrometry

scholarly journals Identification of Glycopeptides with Multiple Hydroxylysine O-Glycosylation Sites by Tandem Mass Spectrometry

2015 ◽  
Vol 14 (12) ◽  
pp. 5099-5108 ◽  
Author(s):  
Yanlin Zhang ◽  
Chuan-Yih Yu ◽  
Ehwang Song ◽  
Shuai Cheng Li ◽  
Yehia Mechref ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Tandem Mass ◽  
Glycosylation Sites

scholarly journals A sequencing strategy for the localization of O-glycosylation sites of MUC1 tandem repeats by PSD-MALDI mass spectrometry

Glycobiology ◽  
1997 ◽  
Vol 7 (7) ◽  
pp. 881-896 ◽  
Author(s):  
Steffen Goletz ◽  
Bernd Thiede ◽  
Franz-Georg Hanisch ◽  
Michael Schultz ◽  
Jasna Peter-Katalinic ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Repeats ◽  
Maldi Mass Spectrometry ◽  
Glycosylation Sites ◽  
Sequencing Strategy

Glucose biosensor based on whole cells of Aspergillus niger MIUG 34 coated with polypyrrole

2017 ◽  
Vol 256 ◽  
pp. S55-S56 ◽  
Author(s):  
Roxana Mihaela Apetrei ◽  
Geta Carac ◽  
Gabriela Bahrim ◽  
Pinar Çamurlu
Keyword(s):  
Aspergillus Niger ◽  
Glucose Biosensor ◽  
Whole Cells

scholarly journals Biodegradation of caffeine by whole cells of tea-derived fungi Aspergillus sydowii, Aspergillus niger and optimization for caffeine degradation

2018 ◽  
Vol 18 (1) ◽  
Author(s):  
Binxing Zhou ◽  
Cunqiang Ma ◽  
Hongzhen Wang ◽  
Tao Xia
Keyword(s):  
Aspergillus Niger ◽  
Aspergillus Sydowii ◽  
Whole Cells ◽  
Caffeine Degradation

Standardization and characterization of antigens for the diagnosis of aspergillosis

2012 ◽  
Vol 58 (4) ◽  
pp. 455-462 ◽  
Author(s):  
Cheila Denise Ottonelli Stopiglia ◽  
Alicia Arechavala ◽  
Mariana Carissimi ◽  
Julia Medeiros Sorrentino ◽  
Valério Rodrigues Aquino ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Aspergillus Niger ◽  
Sensitivity And Specificity ◽  
Predictive Value ◽  
High Sensitivity ◽  
Antigenic Activity ◽  
Sds Page ◽  
Mascot Search Engine ◽  
Commercial Kit

The aim of this study was to develop and characterize antigens for the diagnosis of aspergillosis. Nine strains of Aspergillus species Aspergillus fumigatus , Aspergillus flavus , and Aspergillus niger were grown in Sabouraud and Smith broth to produce exoantigens. The antigens were tested by immunodiffusion against sera from patients with aspergillosis and other systemic mycoses. The protein fraction of the antigens was detected by SDS–PAGE; Western blot and representative bands were assessed by mass spectrometry coupled to a nano Acquity UltraPerformance LC and analyzed by the Mascot search engine. Concurrently, all sera were tested with Platelia Aspergillus EIA. The most reactive antigens to sera from patients infected by A. fumigatus were produced by A. fumigatus MG2 Sabouraud and pooled A. fumigatus Sabouraud samples, both with a sensitivity of 93% and specificity of 100% and 97%, respectively. Aspergillus niger and A. flavus antigens were reactive against A. niger and A. flavus sera, each one with a sensitivity and specificity of 100%. Two proteins, probably responsible for antigenic activity, β-glucosidase in A. fumigatus and α-amylase in A. niger were attained. The commercial kit had a specificity of 22%, sensitivity of 100%, positive predictive value of 48%, and negative predictive value of 100%. The antigens produced showed high sensitivity and specificity and can be exploited for diagnostics of aspergilloma.

Sign in / Sign up

Export Citation Format

Share Document