Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Kalyan K. Banerjee"'
Publikováno v:
Molecular Immunology. 45:266-270
Vibrio cholerae hemolysin (HlyA) can exist as a monomer with hemolytic activity and an oligomer that agglutinates erythrocytes. Biochemical differences accompanying the change in state of aggregation led us to weigh possible differences between the t
Publikováno v:
Journal of Biological Chemistry. 278:38470-38475
Vibrio cholerae hemolysin (HlyA) is a pore-forming toxin that exists in two stable forms: a hemolytically active water-soluble monomer with a native molecular weight of 65,000 and a hemolytically inactive SDS-stable heptamer with the configuration of
Publikováno v:
Immunology Letters. 89:143-147
The monomeric and oligomeric forms of Vibrio cholerae hemolysin (HlyA), a membrane damaging toxin that forms transmembrane pentameric diffusion channels in target eukaryotic membrane, show a pronounced difference in protease susceptibility, presumabl
Publikováno v:
European Journal of Biochemistry. 269:4351-4358
Vibrio cholerae hemolysin (HlyA), a water-soluble protein with a native monomeric relative molecular mass of 65 000, forms transmembrane pentameric channels in target biomembranes. The HlyA binds to lipid vesicles nonspecifically and without saturati
Autor:
Nayanendu Saha, Kalyan K. Banerjee
Publikováno v:
Journal of Biological Chemistry. 272:162-167
Vibrio cholerae hemolysin is an extracellular pore-forming monomeric protein with a native molecular weight of about 60,000. In this study, we showed that the hemolysin interacted with immobilized phospholipids and cholesterol and formed oligomers in
Publikováno v:
The FASEB Journal. 26
Vibrio cholerae N-acetylglucosamine binding protein (GbpA) is a secretory protein which is essential for bacterial survival in environment as well as in human gut. Here we show that GbpA binds to t...
Autor:
Pallavi Banerjee, Kalyan K. Banerjee, Deep Chandan Chakraborty, Gayatri Mukherjee, T. K. Biswas
Publikováno v:
The Journal of biological chemistry. 286(40)
Vibrio cholerae hemolysin (HlyA) displays bipartite property while supervising macrophages (MΦ). The pore-forming toxin causes profound apoptosis within 3 h of exposure and in parallel supports activation of the defying MΦ. HlyA-induced apoptosis o
Publikováno v:
The Indian Journal of Medical Research
Background & objectives: Vibrio cholerae cytolysin/hemolysin (VCC) is a 65 kDa pore-forming toxin (PFT) secreted by O1 El Tor and non-O1 strains. The purified toxin, which contains two C-terminus carbohydrate-binding domains in addition to the cytoly
Autor:
Jason B. Harris, Azim Hossain, Kalyan K. Banerjee, Fahima Chowdhury, Ashraful Islam Khan, Kenneth C. Parker, Firdausi Qadri, Aaron M. Harris, Abdullah A. Tarique, Stephen B. Calderwood, Emily A. Kendall, Regina C. LaRocque, Mohammad Arifuzzaman, Edward T. Ryan, Ana A. Weil, Taufiqur Rahman Bhuiyan, Farhan Murshed, Alaullah Sheikh
Publikováno v:
Infection and immunity. 77(11)
Vibrio cholerae O1 can cause diarrheal disease that may be life-threatening without treatment. Natural infection results in long-lasting protective immunity, but the role of T cells in this immune response has not been well characterized. In contrast
The hemolysin oligomer promotes the proliferation of B-1a cells and the expression of CD25, which is indicative of cell activation, on B-1a cells. The upregulation of CD86 induced by the oligomer showed its selective bias for the B7-2 member of B7 fa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7728912915a4eb93992670d1942e75b1
https://europepmc.org/articles/PMC4651271/
https://europepmc.org/articles/PMC4651271/