ABSTRACT
A monoclonal antibody (mAb) has been developed and selected by immunofluorescence for the radial canals of the contractile vacuole complex (CVC) of Paramecium multimicronucleatum. By applying indirect immunogold labeling to thin frozen sections this mAb has been shown at the electron microscopic level to be specific for the decorated spongiome. We have used the mAb to study the normal interfission appearance as well as developmental stages of the decorated spongiomes. Two decorated spongiomes, presumably involved in water sequestration, radiate as 5-10 bands from unlabeled, circular, 25 microns diameter centers. Two new CVCs arise just anterior to the space occupied by the old spongiomes, the new anterior CVC appearing slightly before the posterior one. Development of the new spongiomes around a 10 microns unlabeled central zone is accompanied by a regression of old spongiome bands until the lengths of these bands in both old and new CVCs are equal just before cell division. After division both old and new spongiome bands grow at equal rates to the same length. Exceptions to the above general scheme, both in number of CVCs in interfission, as well as in position of the new relative to the old CVCs, are also observed.
Subject(s)
Paramecium/ultrastructure , Animals , Antibodies, Monoclonal , Cell Division , Fluorescent Antibody Technique , Microscopy, Immunoelectron , Paramecium/immunology , Vacuoles/immunology , Vacuoles/ultrastructureABSTRACT
Two monoclonal antibodies specific for lipopolysaccharide antigens of Xanthomonas campestris pv. begoniae and pv. pelargonii reacted with all of their respective pathovar strains and not with 130 strains of other xanthomonads or 89 nonxanthomonads tested. These results, as well as previous results, indicate that pathovar-specific monoclonal antibodies were readily generated to strains of X. campestris pathovars that generally infect single hosts.
Subject(s)
Chickens/immunology , Dysgammaglobulinemia/veterinary , Immunity, Cellular , Poultry Diseases/immunology , Animals , Antibody Formation , Complement System Proteins/metabolism , Dysgammaglobulinemia/immunology , Hypersensitivity, Delayed/immunology , IgG Deficiency , Immunologic Memory , Lymphocyte ActivationSubject(s)
Agammaglobulinemia/genetics , Chickens/immunology , Disease Models, Animal , Immunoglobulin G , Agammaglobulinemia/immunology , Animals , Antibodies, Antinuclear/analysis , Autoantibodies/analysis , B-Lymphocytes/immunology , Immunity, Cellular , T-Lymphocytes/immunology , Thyroglobulin/immunologyABSTRACT
We have described an application of a radioimmunoassay (RIA)method, known as radioelectrocomplexing (REC), which involves the anodal migration of antigen and the cathodal migration of antibody in agar electrophoresis. The agar is divided into zones of free antigen (DNP125I-HSA) and antigen bound with anti-DNP. Complete assays of anti-DNP can be performed in 2-4 hr since both immune complex formation and separation of free from bound antigen can be accomplished by electrophoresis in 60-90 min. Estimation of the weight of specifically-purified anti-DNP chicken antibodies in the nanogram range by REC is of the same order as the reported sensitivity of other RIA methods. The method was capable of demonstrating the higher avidity of the 17 S than 7 S antibody. Based on hapten inhibition the relative binding constants of DNP derivatives and anti-DNP were of the same order as reported from more definitive methods.
