scholarly journals Inhibition of Chitin Synthase 1 Leading to Increased Mortality in Arthropods

2021 ◽  
Author(s):  
Simon Schmid ◽  
You Song ◽  
Knut Erik Tollefsen
Keyword(s):  
Chitin Synthase

Potent Chitin Synthase Inhibitors from Plants

2020 ◽  
Vol 16 (1) ◽  
pp. 58-63
Author(s):  
Amrutha Vijayakumar ◽  
Ajith Madhavan ◽  
Chinchu Bose ◽  
Pandurangan Nanjan ◽  
Sindhu S. Kokkal ◽  
...  
Keyword(s):  
Cell Wall ◽  
Candida Albicans ◽  
Caenorhabditis Elegans ◽  
Aspergillus Niger ◽  
Small Molecules ◽  
Tip Growth ◽  
Chitin Synthase ◽  
Chitin Synthesis ◽  
Hyphal Tip Growth ◽  
Hyphal Tip

Background: Chitin is the main component of fungal, protozoan and helminth cell wall. They help to maintain the structural and functional characteristics of these organisms. The chitin wall is dynamic and is repaired, rearranged and synthesized as the cells develop. Active synthesis can be noticed during cytokinesis, laying of primary septum, maintenance of lateral cell wall integrity and hyphal tip growth. Chitin synthesis involves coordinated action of two enzymes namely, chitin synthase (that lays new cell wall) and chitinase (that removes the older ones). Since chitin synthase is conserved in different eukaryotic microorganisms that can be a ‘soft target’ for inhibition with small molecules. When chitin synthase is inhibited, it leads to the loss of viability of cells owing to the self- disruption of the cell wall by existing chitinase. Methods: In the described study, small molecules from plant sources were screened for their ability to interfere with hyphal tip growth, by employing Hyphal Tip Burst assay (HTB). Aspergillus niger was used as the model organism. The specific role of these small molecules in interfering with chitin synthesis was established with an in-vitro method. The enzyme required was isolated from Aspergillus niger and its activity was deduced through a novel method involving non-radioactively labelled substrate. The activity of the potential lead molecules were also checked against Candida albicans and Caenorhabditis elegans. The latter was adopted as a surrogate for the pathogenic helminths as it shares similarity with regard to cell wall structure and biochemistry. Moreover, it is widely studied and the methodologies are well established. Results: Out of the 11 compounds and extracts screened, 8 were found to be prospective. They were also found to be effective against Candida albicans and Caenorhabditis elegans. Conclusion: Purified Methyl Ethyl Ketone (MEK) Fraction1 (F1) of Coconut (Cocos nucifera) Shell Extract (COSE) was found to be more effective against Candida albicans with an IC50 value of 3.04 μg/mL and on L4 stage of Caenorhabditis elegans with an IC50 of 77.8 μg/mL.

scholarly journals There is more than chitin synthase in insect resistance to benzoylureas: molecular markers associated with teflubenzuron resistance in Spodoptera frugiperda

2021 ◽  
Author(s):  
Antonio Rogério Bezerra do Nascimento ◽  
Vitor Antonio Corrêa Pavinato ◽  
Juliana Gonzales Rodrigues ◽  
Karina Lucas Silva-Brandão ◽  
Fernando Luis Consoli ◽  
...  
Keyword(s):  
Molecular Markers ◽  
Insect Resistance ◽  
Spodoptera Frugiperda ◽  
Chitin Synthase

The fitness advantages of bistrifluron resistance related to chitin synthase A in Spodoptera litura (Fab.) (Noctuidae: Lepidoptera)

2021 ◽  
Author(s):  
Changwei Gong ◽  
Xuegui Wang ◽  
Qian Huang ◽  
Jinyue Zhang ◽  
Yuming Zhang ◽  
...  
Keyword(s):  
Spodoptera Litura ◽  
Chitin Synthase

scholarly journals Inhibition of solubilized chitin synthase by chlorinated aromatic compounds isolated from mushroom cultures.

1990 ◽  
Vol 54 (6) ◽  
pp. 1381-1384 ◽  
Author(s):  
Walter PFEFFERLE ◽  
Heidrun ANKE ◽  
Monika BROSS ◽  
Wolfgang STEGLICH
Keyword(s):  
Aromatic Compounds ◽  
Chitin Synthase ◽  
Chlorinated Aromatic Compounds

scholarly journals Chitin synthase in the stipe of Agaricus bisporus (J. Lange) Imbach

1981 ◽  
Vol 10 (1) ◽  
pp. 43-47 ◽  
Author(s):  
G.D. Craig ◽  
D.A. Wood ◽  
K. Gull
Keyword(s):  
Agaricus Bisporus ◽  
Chitin Synthase

Nikkomycins: Microbial inhibitors of chitin synthase

2007 ◽  
Vol 32 (1) ◽  
pp. 271-280 ◽  
Author(s):  
H.-P. Fiedler ◽  
R. Kurth ◽  
J. Langhärig ◽  
J. Delzer ◽  
H. Zähner
Keyword(s):  
Chitin Synthase ◽  
Microbial Inhibitors

chs-4, a class IV chitin synthase gene fromNeurospora crassa

1996 ◽  
Vol 250 (2) ◽  
pp. 214-222 ◽  
Author(s):  
Adi Beth Din ◽  
Charles A. Specht ◽  
Phillips W. Robbins ◽  
Oded Yarden
Keyword(s):  
Chitin Synthase ◽  
Class Iv

Species‐specific primers of chitin synthase 1 gene for the differentiation of the Trichophyton mentagrophytes complex

Mycoses ◽  
1999 ◽  
Vol 42 (1‐2) ◽  
pp. 71-74 ◽  
Author(s):  
R. Kano ◽  
Y. Nakamura ◽  
T. Watari ◽  
S. Watanabe ◽  
H. Takahashi ◽  
...  
Keyword(s):  
Trichophyton Mentagrophytes ◽  
Chitin Synthase ◽  
Specific Primers ◽  
Trichophyton Mentagrophytes Complex ◽  
Species Specific

scholarly journals Prenylation of Saccharomyces cerevisiae Chs4p Affects Chitin Synthase III Activity and Chitin Chain Length

2006 ◽  
Vol 6 (2) ◽  
pp. 328-336 ◽  
Author(s):  
Kariona A. Grabińska ◽  
Paula Magnelli ◽  
Phillips W. Robbins
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Chain Length ◽  
Attachment Site ◽  
Chitin Synthase ◽  
Yeast Cells ◽  
Average Chain Length ◽  
Calcofluor White ◽  
Protein Factor

ABSTRACT Chs4p (Cal2/Csd4/Skt5) was identified as a protein factor physically interacting with Chs3p, the catalytic subunit of chitin synthase III (CSIII), and is indispensable for its enzymatic activity in vivo. Chs4p contains a putative farnesyl attachment site at the C-terminal end (CVIM motif) conserved in Chs4p of Saccharomyces cerevisiae and other fungi. Several previous reports questioned the role of Chs4p prenylation in chitin biosynthesis. In this study we reinvestigated the function of Chs4p prenylation. We provide evidence that Chs4p is farnesylated by showing that purified Chs4p is recognized by anti-farnesyl antibody and is a substrate for farnesyl transferase (FTase) in vitro and that inactivation of FTase increases the amount of unmodified Chs4p in yeast cells. We demonstrate that abolition of Chs4p prenylation causes a ∼60% decrease in CSIII activity, which is correlated with a ∼30% decrease in chitin content and with increased resistance to the chitin binding compound calcofluor white. Furthermore, we show that lack of Chs4p prenylation decreases the average chain length of the chitin polymer. Prenylation of Chs4p, however, is not a factor that mediates plasma membrane association of the protein. Our results provide evidence that the prenyl moiety attached to Chs4p is a factor modulating the activity of CSIII both in vivo and in vitro.

Sign in / Sign up

Export Citation Format

Share Document