Macrophage distinguishes Vibrio cholerae hemolysin from its protease insensitive oligomer by time dependent and selective expression of CD80-CD86.

Authors:
Avijit Ray, PhD
Avijit Ray, PhD
AbbVie
Senior Scientist II
Immunology, Immuno-oncology, Autoimmunity and Inflammation, Immune tolerance
North Chicago, IL | United States
Kausik Chattopadhyay
Kausik Chattopadhyay
Indian Institute of Science Education and Research (IISER) Mohali
India
Kalyan K Banerjee
Kalyan K Banerjee
National Institute of Cholera and Enteric Diseases
India
Tapas Biswas
Tapas Biswas
National Institute of Cholera and Enteric Diseases

Immunol Lett 2003 Oct;89(2-3):143-7

Division of Immunology and Vaccine Development, National Institute of Cholera and Enteric Diseases, P-33, CIT Road, Scheme XM, 700 010, Kolkata, India.

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, presumably due to masking of sensitive peptide bonds during oligomerization. In this work, we examined if resistance of a protein to proteolytic processing affects the expression of costimulatory molecules, CD80 and CD86, on macrophage exposed to the same antigen. The murine peritoneal cavity macrophages expressed both CD80 and CD86 after 24 h of incubation with HlyA monomer but failed to express the costimulatory molecules when treated with the HlyA oligomer. The expression of CD80 molecule on macrophage after 48 h by the HlyA oligomer that failed to express the costimulatory molecules after 24 h indicates that proteolytic processing plays a decisive role in expression of CD80 and CD86 on cell surface.

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October 2003
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2 Citations
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