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A comparative study of α-Hemolysin and Jacalin that influence mammalian cell signaling

Shodhganga@INFLIBNET

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Field Value
 
Title A comparative study of α-Hemolysin and Jacalin that influence mammalian cell signaling
 
Contributor Bhat, Manoj Kumar
 
Subject Cell Science, Cell Signalings, Biotechnology, Mammals
 
Description To overcome host cell defense and for pathogenesis, pathogenic bacteria secrete soluble factors to interact and interfere with essential host systems. Most of these soluble factors are known as pore forming toxins and likely to be the primary virulence factors. They modulate host cell signaling or damage host cell membranes by pore formation upon binding to susceptible target cells. Staphylococcus aureus bacteria secrete a soluble pore forming toxin “α-hemolysin”, which follows a multi-step oligomerization process to assemble into a heptameric functional pore on the target or host cell membrane after binding. Membrane binding of α-HL and its oligomerization into heptameric pore either modulates host cell signaling or permeabilizes the target cells. Although α-HL binds to virtually all mammalian cells but also shows cell tropism dependent differential membrane recognition. Differential membrane recognition compels us to believe that α-HL may bind to specific receptor(s) on susceptible host membrane for its action. But the eukaryotic cell micro-domain (lipid raft/caveolae) specific receptor(s) or molecules that aid susceptibility dependent membrane recognition and assembly of α-HL was not ascertained. Here we studied the molecular basis of differential membrane recognition domain of α-HL and how it exploits eukaryotic membrane receptor for assembly and modulation of mammalian cell signaling.
Abstract includes, References p.113-128
 
Date 2011-08-17T12:13:51Z
2011-08-17T12:13:51Z
2011-08-17
0
January, 2008
2008
 
Type Ph.D.
 
Identifier http://hdl.handle.net/10603/2226
 
Language English
 
Rights university
 
Format 128p.
DVD
 
Publisher Pune
University of Pune
National Centre for Cell Science
 
Source INFLIBNET