Related Experiment Video
Updated: Jan 27, 2026

A Loop-mediated Isothermal Amplification LAMP Assay for Rapid Identification of Bemisia tabaci
Published on: October 29, 2018
A thioredoxin-like protein of Bemisia tabaci interacts with coat protein of begomoviruses
Gunjan Kumar Saurav1, Vipin Singh Rana1,2, Sonam Popli1,3
1Gut Biology Laboratory, Department of Zoology, University of Delhi, Room No. 117, Delhi, 110007, India.
Abstract:
Bemisia tabaci (whitefly) is the sole vector of begomoviruses, which transmits them in a persistent and circulative manner from infected to healthy plants. During this process, begomoviruses interact with various proteins in the insect vector B. tabaci that would play a specific role in the virus transmission. Identification and characterization of such proteins are important to understand the complete process of virus transmission. Coat protein (CP) of begomoviruses is the only protein which is reported to interact with proteins of the insect vector B. tabaci. In this study, we performed yeast two-hybrid assay using CP of cotton leaf curl Rajasthan virus (CLCuV) and Tomato leaf curl New Delhi virus (ToLCNDV) as bait in separate experiments and cDNA prepared from total RNA of B. tabaci was used as prey. Yeast two-hybrid assay resulted in identification of a thioredoxin-like protein (TLP) from CLCuV yeast two-hybrid library. Later TLP was also found to interact with CP of ToLCNDV. In vitro pull-down assay showed TLP interaction with CP of both CLCuV and ToLCNDV. TLP was found to interact with ToLCNDV virus particles isolated from tomato leaves.
Related Concept Videos
Protein-protein Interfaces
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...
What are Proteins?
Protein Networks
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
Protein Organization

