Mannostatin A, a new glycoprotein-processing inhibitor

Biochemistry ◽  
1990 ◽  
Vol 29 (43) ◽  
pp. 10062-10069 ◽  
Author(s):  
Joseph E. Tropea ◽  
G. P. Kaushal ◽  
Irena Pastuszak ◽  
Mike Mitchell ◽  
Takaaki Aoyagi ◽  
...  
Keyword(s):  
Glycoprotein Processing ◽  
Mannostatin A

Unique nCoV-2019 (COVID 19) spike glycoprotein processing by host protease: Analysis and Implication on infection

2020 ◽  
Vol 17 ◽  
Author(s):  
Ajoy Basak ◽  
Sarmistha Basak
Keyword(s):  
World Health ◽  
Spike Glycoprotein ◽  
Binding Domains ◽  
Corona Virus ◽  
Global Pandemic ◽  
High Infection ◽  
Crucial Information ◽  
Glycoprotein Processing ◽  
Health Organization ◽  
Host Reservoir

: The current global pandemic outbreak of a novel type of corona virus termed by World Health Organization as COVID-19 became an grave concern and worry to human health and world economy. Intense research efforts are now underway worldwide to combat and prevent the spread of this deadly disease. This zoonotic virus, a native to bat population is most likely transmitted to human via a host reservoir. Due to its close similarity to previously known SARS CoV (Severe Acute Respiratory Syndrome Corona Virus) of 2002 and related MERS CoV (Middle East Respiratory Syndrome Corona Virus) of 2012, it is also known as SARS CoV2. But unlike them it is far too infectious, virulent and lethal. Among its various proteins, the surface spike glycoprotein “S” has drawn significant attention because of its implication in viral recognition and host-virus fusion process. A detail comparative analysis of “S” proteins of SARS CoV (now called SARS CoV1), SARS CoV2 (COVID-19) and MERS CoV based on structure, sequence alignment, host cleavage sites, receptor binding domains, potential glycosylation and Cys-disulphide bridge locations has been performed. It revealed some key features and variations that may elucidate the high infection and virulence character of COVID-19. Moreover this crucial information may become useful in our quest for COVID-19 therapeutics and vaccines.

Glycoprotein processing in mutants of HSV-1 that induce cell fusion

Virology ◽  
1982 ◽  
Vol 117 (2) ◽  
pp. 293-306 ◽  
Author(s):  
Stanley Person ◽  
Konstantin G. Kousoulas ◽  
Robert W. Knowles ◽  
G. Sullivan Read ◽  
Thomas C. Holland ◽  
...  
Keyword(s):  
Cell Fusion ◽  
Glycoprotein Processing ◽  
Hsv 1

scholarly journals O-Linked glycans control glycoprotein processing by antigen-presenting cells: a biochemical approach to the molecular aspects of MUC1 processing by dendritic cells

2003 ◽  
Vol 33 (12) ◽  
pp. 3242-3254 ◽  
Author(s):  
Franz-Georg Hanisch ◽  
Tilo Schwientek ◽  
Michael S. Von Bergwelt-Baildon ◽  
Joachim L. Schultze ◽  
Olivera Finn
Keyword(s):  
Dendritic Cells ◽  
Antigen Presenting Cells ◽  
Glycoprotein Processing ◽  
Biochemical Approach ◽  
Molecular Aspects ◽  
Antigen Presenting

Ectopic growth of the fungal symbiont (Chaetothyriales) on Ipomoea carnea

Botany ◽  
2021 ◽  
Author(s):  
Aziza Ibrahim Noor ◽  
Amy Nava ◽  
Marwa Neyaz ◽  
Peter Cooke ◽  
Rebecca Creamer ◽  
...  
Keyword(s):  
Cross Sections ◽  
Storage Disease ◽  
Growth Habit ◽  
Leaf Surface ◽  
Livestock Grazing ◽  
Lysosomal Storage ◽  
Lower Leaf Surface ◽  
Ipomoea Carnea ◽  
Show Evidence ◽  
Glycoprotein Processing

Swainsonine, an indolizidine alkaloid, is an alpha-mannosidase and mannosidase II inhibitor that alters glycoprotein processing and causes lysosomal storage disease. Swainsonine is the toxic principle in several plant species worldwide and causes severe toxicosis in livestock grazing these plants. All swainsonine-containing plant taxa investigated to date are associated with fungal symbionts that produce swainsonine. Among the swainsonine-containing convolvulaceous species, Ipomoea carnea is associated with a seed transmitted symbiont belonging to the fungal order Chaetothyriales. The nature of this association was unclear therefore this association was investigated further using microscopy. Macroscopic and microscopic data reported here demonstrate that the Chaetothyriales symbiont associated with I. carnea grows ectopically on the adaxial (upper) surface of leaves as lacy mycelia in plants that contain swainsonine and was not present on plants lacking swainsonine that were derived from fungicide treated seeds. Hyphae were not observed on the surface of any other tissues including the abaxial (lower) leaf surface, petiole, and stem. Mycelia were not visible in internal tissues below the epidermis and there did not appear to be any hyphal extensions within the fibrovascular bundles or stomata. Longitudinal and/or cross sections of the stems or petioles did not show evidence of hyphae growing between cells. These results suggest an epibiotic growth habit of the Chaetothyriales symbiont in association with I. carnea.

Sign in / Sign up

Export Citation Format

Share Document