Human polymeric IgA is superior to IgG and single-chain Fv of the same monoclonal specificity to inhibit urease activity associated with Helicobacter pylori

@article{citeulike:2615688, abstract = {Helicobacter-induced gastritis is considered nowadays an epidemic, the prevalence of which is one of the highest world-wide (70\%), with as much as 40\% of the population in industrialized countries. Helicobacter pylori (H. pylori) antigens (Ag) capable to elicit a protective immune response in animal models have been identified, but these antigens have not been shown to be strongly immunogenic when administered to humans. Due to their stability in the gastric environment and avidity, passive administration of secretory immunoglobulin A (SIgA) antibodies (Ab) targeting protective Ag might be particularly relevant as a substitute or complement to current therapies. To this aim, we have designed expression vectors to convert a scFv polypeptide specific for H. pylori urease subunit A into human IgG, polymeric IgA (IgAp/d) and SIgA. Purified proteins show proper binding characteristics toward both the native and denatured forms of H. pylori urease. The direct comparison between different isotype and molecular forms, but of unique specificity, demonstrates that SIgA and IgAp/d are more efficient in blocking free and H. pylori-associated urease than IgG and scFv. We conclude that the expression system reported herein will represent a valuable tool to produce human SIgA Ab of multiple specificities against H. pylori antigens involved in colonization and persistence.}, author = {Berdoz, Jose and Corthesy, Blaise }, citeulike-article-id = {2615688}, doi = {10.1016/j.molimm.2004.05.006}, journal = {Molecular Immunology}, keywords = {methods, pylori}, month = {August}, number = {10}, pages = {1013--1022}, posted-at = {2008-03-31 11:11:43}, priority = {2}, title = {Human polymeric IgA is superior to IgG and single-chain Fv of the same monoclonal specificity to inhibit urease activity associated with Helicobacter pylori}, url = {http://dx.doi.org/10.1016/j.molimm.2004.05.006}, volume = {41}, year = {2004} }

TY - JOUR ID - citeulike:2615688 L3 - citeulike-article-id:2615688 TI - Human polymeric IgA is superior to IgG and single-chain Fv of the same monoclonal specificity to inhibit urease activity associated with Helicobacter pylori JF - Molecular Immunology VL - 41 IS - 10 SP - 1013 EP - 1022 N2 - Helicobacter-induced gastritis is considered nowadays an epidemic, the prevalence of which is one of the highest world-wide (70%), with as much as 40% of the population in industrialized countries. Helicobacter pylori (H. pylori) antigens (Ag) capable to elicit a protective immune response in animal models have been identified, but these antigens have not been shown to be strongly immunogenic when administered to humans. Due to their stability in the gastric environment and avidity, passive administration of secretory immunoglobulin A (SIgA) antibodies (Ab) targeting protective Ag might be particularly relevant as a substitute or complement to current therapies. To this aim, we have designed expression vectors to convert a scFv polypeptide specific for H. pylori urease subunit A into human IgG, polymeric IgA (IgAp/d) and SIgA. Purified proteins show proper binding characteristics toward both the native and denatured forms of H. pylori urease. The direct comparison between different isotype and molecular forms, but of unique specificity, demonstrates that SIgA and IgAp/d are more efficient in blocking free and H. pylori-associated urease than IgG and scFv. We conclude that the expression system reported herein will represent a valuable tool to produce human SIgA Ab of multiple specificities against H. pylori antigens involved in colonization and persistence. KW - methods KW - pylori AU - Berdoz, Jose AU - Corthesy, Blaise PY - 2004/08// UR - http://dx.doi.org/10.1016/j.molimm.2004.05.006 ER -