title: Differential changes in heat shock protein-, lipoarabinomannan-, and purified protein derivative-specific immunoglobulin G1 and G2 isotype responses during bovine Mycobacterium avium subsp. paratuberculosis infection.
abstract: Bovine paratuberculosis is caused by infection of young calves with Mycobacterium avium subsp. paratuberculosis. In some of the chronically infected cows the long asymptomatic stage (2 to 4 years) is followed by a rapid progression to a clinical stage due to protein-losing enteropathy, which will ultimately be fatal. The current dogma is that in early stages of disease the cell-mediated responses predominate, whereas in the clinical stage of the disease the humoral responses prevail, possibly signaling a switch in immune reactivity related to disease progression. We developed immunoglobulin M (IgM)-, IgA-, and IgG1- and IgG2-isotype-specific enzyme-linked immunosorbent assays for M. avium subsp. paratuberculosis-derived antigens (heat shock proteins of 70 kDa [Hsp70] and 65 kDa [Hsp65], lipoarabinomannan [LAM], and M. avium subsp. paratuberculosis purified protein derivative PPD [PPDP]). The serological responses of cows in different stages of paratuberculosis were used to evaluate the putative shift in immune responsiveness. In the clinical stage the PPDP-specific IgG1 responses were increased compared to those in the asymptomatic stage. However, total IgG1 and IgG2 and the Hsp70-, Hsp65-, and LAM-specific isotype responses were decreased in the clinical stage were decreased compared to those in the asymptomatic stage of disease. Thus, the classical pattern was found only for PPDP antigens and the IgG1 isotype. For other antigens and isotypes and the total IgG levels, the response pattern is different and indicates that there is no uniform association with increased antibody responses during the progression from the asymptomatic stage to the clinical stage of bovine paratuberculosis.
authors.affiliation: Department of Immunology, Institute of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands. a.p.koets@vet.uu.nl
authors.forename: A P
authors.initials: AP
authors.lastname: Koets
authors.forename: V P
authors.initials: VP
authors.lastname: Rutten
authors.forename: M
authors.initials: M
authors.lastname: de Boer
authors.forename: D
authors.initials: D
authors.lastname: Bakker
authors.forename: P
authors.initials: P
authors.lastname: Valentin-Weigand
authors.forename: W
authors.initials: W
authors.lastname: van Eden
mesh_terms: D000818:Animals; D000907:Antibodies, Bacterial / Q000097:blood*; D000918:Antibody Specificity; D000942:Antigens, Bacterial / Q000276:immunology*; D001426:Bacterial Proteins; D002417:Cattle; D002418:Cattle Diseases / Q000276:immunology*; D018834:Chaperonin 60; D018833:Chaperonins / Q000276:immunology; D004797:Enzyme-Linked Immunosorbent Assay / Q000379:methods; D005260:Female; D018840:HSP70 Heat-Shock Proteins / Q000276:immunology; D006360:Heat-Shock Proteins / Q000276:immunology; D007074:Immunoglobulin G / Q000097:blood*; D007132:Immunoglobulin Isotypes / Q000097:blood; D008070:Lipopolysaccharides / Q000276:immunology; D016927:Mycobacterium avium subsp. paratuberculosis / Q000276:immunology*; D010283:Paratuberculosis / Q000276:immunology*; D014373:Tuberculin
chemical_list: D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D018834:Chaperonin 60; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D007074:Immunoglobulin G; D007132:Immunoglobulin Isotypes; D008070:Lipopolysaccharides; D014373:Tuberculin; C074119:heat-shock protein 65, Mycobacterium; C050016:lipoarabinomannan; D018833:Chaperonins