Tracking and elucidating alphavirus host protein interactions Free sex chatting online messaging chat with beautiful girls
The entry and infection pathways of virus are thus largely defined by the interactions between virus particles and their cell surface and cytoplasmic receptors.
A thorough analysis of virus–host interactomes may reveal novel mechanisms in virus entry, virus infection, and pathogenic strategies to modulate host metabolic pathways.
As a consequence, alphavirus–host interactions are now understood in much more molecular detail, and important novel mechanisms have been elucidated.
It has become clear that alphaviruses not only cause a general host shut-off in infected vertebrate cells, but also specifically suppress different host antiviral pathways using their viral nonstructural proteins, ns P2 and ns P3.
Accepted for publication 29 September 2015 Published 1 December 2015 Volume 2015:7 Pages 57—66 DOI https://doi.org/10.2147/VAAT.
S60265 Checked for plagiarism Yes Review by Single-blind Peer reviewers approved by Dr Malathi Krishnamurthy Peer reviewer comments 2 Editor who approved publication: Professor Jonathan Dinman Soumen Bhattacharjee Cell and Molecular Biology Laboratory, Department of Zoology, University of North Bengal, Siliguri, Darjeeling, West Bengal, India Abstract: Viral infections and pandemics result in millions of deaths worldwide each year.
Viruses replicate and proliferate in host cells while continuously adjusting to and modulating the host environment.
They encode a wide spectrum of multifunctional proteins, which interplay with and modify proteins in host cells.
The transport of genetic material and other essential components through the host cell barriers requires, in most cases, precise attachment of the virions to the cell surface receptor(s) of the permissive host cells.
Site-directed mutagenesis showed that the Rin-ns P3 interaction involved the NTF2-like domain of Rin and two conserved TFGD repeats in the C-terminal variable domain of ns P3.
Although We identified the ns P3 hypervariable C-terminal domain as a critical factor for granular localization and sequestration of mosquito Rin.
In this research we studied the domains required for localization of CHIKV ns P3 in insect cells and demonstrated its molecular interaction with Rasputin (Rin), the mosquito homologue of G3BP.
The biological involvement of Rin in CHIKV infection was investigated in live Rin displayed a diffuse, cytoplasmic localization, but was effectively sequestered into ns P3-granules upon ns P3 co-expression.