P-glycoprotein-like protein, a possible genetic marker for ivermectin resistance selection in Onchocerca volvulus

2008 ◽  
Vol 158 (2) ◽  
pp. 101-111 ◽  
Author(s):  
Catherine Bourguinat ◽  
Bernadette F. Ardelli ◽  
Sébastien D.S. Pion ◽  
Joseph Kamgno ◽  
Jacques Gardon ◽  
...  
Keyword(s):  
Genetic Marker ◽  
Protein A ◽  
Onchocerca Volvulus ◽  
Resistance Selection ◽  
P Glycoprotein

Genomic organization and effects of ivermectin selection on Onchocerca volvulus P-glycoprotein

2005 ◽  
Vol 143 (1) ◽  
pp. 58-66 ◽  
Author(s):  
Bernadette F. Ardelli ◽  
Sean B. Guerriero ◽  
Roger K. Prichard
Keyword(s):  
Genomic Organization ◽  
Onchocerca Volvulus ◽  
P Glycoprotein

Tobacco fraction 1 protein: a unique genetic marker

Science ◽  
2003 ◽  
Vol 191 (4226) ◽  
pp. 429-434 ◽  
Author(s):  
S Kung
Keyword(s):  
Genetic Marker ◽  
Protein A ◽  
Fraction 1 Protein

Imaging of the P-glycoprotein in normal and multidrug-resistant small-cell lung carcinoma cells with the Atomic-Force Microscope(AFM)

1994 ◽  
Vol 52 ◽  
pp. 1074-1075
Author(s):  
J. M. Tsai ◽  
D. Sadava ◽  
S. A. C. Gould
Keyword(s):  
Tumor Cells ◽  
Small Cell Lung Carcinoma ◽  
Protein A ◽  
Multidrug Resistant ◽  
Extracellular Medium ◽  
Contact Mode ◽  
Cell Lung Carcinoma ◽  
Lung Carcinoma Cells ◽  
Atomic Force ◽  
P Glycoprotein

Cancer is characterized by the often rapid and uncontrolled rate of cell growth. This alteration in growth pattern causes normal cells to become tumor cells. After undergoing a period of chemotherapy, some tumor cells become resistant to a variety of drugs, a phenomenon known as the multidrug resistance (MDR). One explanation for this change is the overexpression of P-glycoprotein in the drug-resistant cells. This membrane protein is capable of pumping drugs into the extracellular medium. Since the drugs do not accumulate, the tumor cells are not killed. In order to examine this protein, a contact mode AFM was used to image the cell membranes of both the normal and the MDR tumor cells. The four figures provided show the topographical information of the membranes and suggest that there are differences between the cell lines.

Modelling profile of onchocerca volvulus glutamatecysteine ligase (ONCVO-GCL)

2021 ◽  
Vol 10 (3) ◽  
pp. 118-122
Author(s):  
Akinseye Olanrewaju Roland ◽  
Ale E Morayo ◽  
Ojomo Joan ◽  
Gbadamosi Folawiyo I ◽  
Ebenezer Kayode ◽  
...  
Keyword(s):  
Active Sites ◽  
Homology Modelling ◽  
Protein A ◽  
3D Structure ◽  
Chemotherapeutic Agents ◽  
Onchocerca Volvulus ◽  
Glutamate Cysteine Ligase ◽  
3 Dimensional ◽  
High Level ◽  
Favoured Region

Onchocerca volvulus Glutamate cysteine ligase (ONCVO-GCL) catalyzes the first step in the production of the cellular antioxidant glutathione (GSH), which involve the condensation of cysteine and glutamate to form the dipeptide gamma-glutamylcysteine (γ-GC). ONCVO-GCL is critical to cell survival. Its dysregulation could lead to decreased GSH biosynthesis, reduced cellular antioxidant capacity, and the induction of oxidative stress. ONCVO-GCL expression support the high level of cell proliferation and confer resistance to many chemotherapeutic agents, hence could serve as a molecular target for inhibitors. This study aims to model the 3-dimensional (3D) structure of ONCVO-GCL, validate and predict the active sites of the modelled protein. ONCVO-GCL (Uniprot ID: A0A044QR48) 3D structure was modelled and validated using SWISS-MODEL. The Computed Atlas of Surface Topography of proteins (CASTp) 3.0 was used to predict the active sites of the modelled protein. A percentage identity matrix of 41.81% was obtained, which confirms the similarity identity of 40.86% obtained from the homology modelling. Model with 88% in the most favoured region of Ramachandra plot was obtained and the more favourable active sites for docking analyses due to the similarities observed from the alignment of the modelled structure to the template structure were: GLY 2A, LEU3A, LEU 4A, ARG 40A, TRP 47A, GLY 48A, ASP 49A, GLU 50A, GLU 52A, and PRO 109A.

Sign in / Sign up

Export Citation Format

Share Document