Macrophage distinguishes Vibrio cholerae hemolysin from its protease insensitive oligomer by time dependent and selective expression of CD80–CD86
| Autor: | Avijit Ray, Tapas Biswas, Kalyan K. Banerjee, Kausik Chattopadhyay |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
medicine.medical_treatment
Immunology Cell chemical and pharmacologic phenomena Biology medicine.disease_cause Oligomer Hemolysin Proteins Mice chemistry.chemical_compound Bacterial Proteins Antigens CD medicine Animals Immunology and Allergy Vibrio cholerae CD86 Mice Inbred BALB C Membrane Glycoproteins Protease Macrophages hemic and immune systems Hemolysin Transmembrane protein Cell biology medicine.anatomical_structure chemistry Biochemistry Pronase B7-1 Antigen B7-2 Antigen CD80 |
| Zdroj: | Immunology Letters. 89:143-147 |
| ISSN: | 0165-2478 |
| DOI: | 10.1016/s0165-2478(03)00135-4 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect