Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 3 de 3
Filter
Add more filters










Language
Publication year range
1.
Braz J Med Biol Res ; 33(2): 147-55, 2000 Feb.
Article in English | MEDLINE | ID: mdl-10657055

ABSTRACT

The present paper describes important features of the immune response induced by the Cry1Ac protein from Bacillus thuringiensis in mice. The kinetics of induction of serum and mucosal antibodies showed an immediate production of anti-Cry1Ac IgM and IgG antibodies in serum after the first immunization with the protoxin by either the intraperitoneal or intragastric route. The antibody fraction in serum and intestinal fluids consisted mainly of IgG1. In addition, plasma cells producing anti-Cry1Ac IgG antibodies in Peyer's patches were observed using the solid-phase enzyme-linked immunospot (ELISPOT). Cry1Ac toxin administration induced a strong immune response in serum but in the small intestinal fluids only anti-Cry1Ac IgA antibodies were detected. The data obtained in the present study confirm that the Cry1Ac protoxin is a potent immunogen able to induce a specific immune response in the mucosal tissue, which has not been observed in response to most other proteins.


Subject(s)
Antibodies, Bacterial/biosynthesis , Bacillus thuringiensis/immunology , Bacterial Proteins/immunology , Bacterial Toxins/immunology , Endotoxins/immunology , Immunoglobulin G/biosynthesis , Intestinal Mucosa/immunology , Animals , Antibodies, Bacterial/blood , Bacillus thuringiensis Toxins , Enzyme-Linked Immunosorbent Assay , Female , Hemolysin Proteins , Immunoglobulin G/blood , Immunoglobulin M/biosynthesis , Immunoglobulin M/blood , Mice , Mice, Inbred BALB C
2.
Braz. j. med. biol. res ; 33(2): 147-55, Feb. 2000.
Article in English | LILACS | ID: lil-252291

ABSTRACT

The present paper describes important features of the immune response induced by the Cry1Ac protein from Bacillus thuringiensis in mice. The kinetics of induction of serum and mucosal antibodies showed an immediate production of anti-Cry1Ac IgM and IgG antibodies in serum after the first immunization with the protoxin by either the intraperitoneal or intragastric route. The antibody fraction in serum and intestinal fluids consisted mainly of IgG1. In addition, plasma cells producing anti-Cry1Ac IgG antibodies in Peyer's patches were observed using the solid-phase enzyme-linked immunospot (ELISPOT). Cry1Ac toxin administration induced a strong immune response in serum but in the small intestinal fluids only anti-Cry1Ac IgA antibodies were detected. The data obtained in the present study confirm that the Cry1Ac protoxin is a potent immunogen able to induce a specific immune response in the mucosal tissue, which has not been observed in response to most other proteins


Subject(s)
Animals , Female , Antibodies, Bacterial/biosynthesis , Bacillus thuringiensis/immunology , Bacterial Proteins/immunology , Bacterial Toxins/immunology , Immunoglobulin G/biosynthesis , Intestinal Mucosa/immunology , Antibodies, Bacterial/blood , Bacterial Proteins/administration & dosage , Bacterial Toxins/administration & dosage , Enzyme-Linked Immunosorbent Assay , Immunization , Immunoglobulin G/blood , Immunoglobulin M/biosynthesis , Immunoglobulin M/blood , Intestinal Mucosa/metabolism , Mice, Inbred BALB C
3.
Biochem Mol Biol Int ; 45(5): 1011-20, 1998 Aug.
Article in English | MEDLINE | ID: mdl-9739466

ABSTRACT

Cry proteins from Bacillus thuringiensis have insecticidal properties. The function of domains I and II has been described but domain III has so far eluded understanding. Domain III from Cry1Ab and Cry1Ac has been cloned, expressed in E. coli and injected to rabbits with the aid of characterizing them immunologically. Interestingly, polyclonal antibodies against Cry1Ab fragment did not recognize either the native Cry1Ab toxin or the Cry1Ac fragment while those against the latter did recognize either the native Cry1Ac toxin or the Cry1Ab protein fragment. A combination of information from sequence comparison and hydrophobicity profile indicates that these protein fragments possibly adopt different spatial dispositions within the respective toxins.


Subject(s)
Bacillus thuringiensis/chemistry , Bacterial Proteins/chemistry , Bacterial Toxins/chemistry , Endotoxins/chemistry , Bacillus thuringiensis Toxins , Bacterial Proteins/genetics , Bacterial Proteins/immunology , Bacterial Toxins/genetics , Bacterial Toxins/immunology , Cloning, Molecular , Endotoxins/genetics , Endotoxins/immunology , Enzyme-Linked Immunosorbent Assay , Hemolysin Proteins , Protein Structure, Secondary , Recombinant Proteins/chemistry , Solubility
SELECTION OF CITATIONS
SEARCH DETAIL
...