BIOMAT Database Logo BIOMAT Database Logo

Detection of human Toxoplasma-specific immunoglobulins A, M, and G with a recombinant Toxoplasma gondii rop2 protein. 1998

V Martin, and M Arcavi, and G Santillan, and M R Amendoeira, and E De Souza Neves, and G Griemberg, and E Guarnera, and J C Garberi, and S O Angel
Departamento de Parasitología, ANLIS Dr. Carlos G. Malbran, Buenos Aires, Argentina.

The Toxoplasma gondii rhoptry protein Rop2 was expressed in Escherichia coli as a fusion protein containing 44 kDa of the 55-kDa mature Rop2, supplied with six histidyl residues at the N-terminal end (Rop2196-561). Humoral response during Toxoplasma infection of humans was analyzed by immunoglobulin G (IgG), IgA, and IgM enzyme-linked immunosorbent assay with Rop2196-561 as the antigen substrate. The analyzed sera were divided according to T. gondii-specific serological tests (IgG, IgA, or IgM indirect immunofluorescence and IgA or IgM immunosorbent agglutination assay) as group A (IgG+ IgA- IgM-; n = 35), group B (IgG+ IgA+ IgM+; n = 21), group C (IgG+ IgA+ IgM-; n = 5), and group D (IgG+ IgA- IgM+; n = 16). Twenty-six T. gondii-seronegative sera from individuals with other infections were also included (group E). Anti-Rop2 IgG antibodies were detected in 82.8% of group A sera and in 97.6% of the sera with acute-phase marker immunoglobulins (groups B, C, and D). The percentage of IgA antibody reactivity against Rop2196-561 was 17.1% in group A, 50% in group D, and 80.8% in groups B and C. The percentage of IgM antibody reactivity was 0% in groups A and C and 62% in groups B and D. Sera from group E failed to show IgA, IgM, or IgG antibody reactivity. Since T. gondii Rop2 elicits a strong humoral response from an early stage of infection, it is suggested that recombinant Rop2196-561 would be suitable for use in diagnostic systems, in combination with other T. gondii antigens, to detect specific IgG, IgA, and IgM antibodies.

UI MeSH Term Description Entries
D007070 Immunoglobulin A Represents 15-20% of the human serum immunoglobulins, mostly as the 4-chain polymer in humans or dimer in other mammals. Secretory IgA (IMMUNOGLOBULIN A, SECRETORY) is the main immunoglobulin in secretions. IgA,IgA Antibody,IgA1,IgA2,Antibody, IgA
D007074 Immunoglobulin G The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B. Gamma Globulin, 7S,IgG,IgG Antibody,Allerglobuline,IgG(T),IgG1,IgG2,IgG2A,IgG2B,IgG3,IgG4,Immunoglobulin GT,Polyglobin,7S Gamma Globulin,Antibody, IgG,GT, Immunoglobulin
D007075 Immunoglobulin M A class of immunoglobulin bearing mu chains (IMMUNOGLOBULIN MU-CHAINS). IgM can fix COMPLEMENT. The name comes from its high molecular weight and originally was called a macroglobulin. Gamma Globulin, 19S,IgM,IgM Antibody,IgM1,IgM2,19S Gamma Globulin,Antibody, IgM
D007114 Immunization Deliberate stimulation of the host's immune response. ACTIVE IMMUNIZATION involves administration of ANTIGENS or IMMUNOLOGIC ADJUVANTS. PASSIVE IMMUNIZATION involves administration of IMMUNE SERA or LYMPHOCYTES or their extracts (e.g., transfer factor, immune RNA) or transplantation of immunocompetent cell producing tissue (thymus or bone marrow). Immunologic Stimulation,Immunostimulation,Sensitization, Immunologic,Variolation,Immunologic Sensitization,Immunological Stimulation,Sensitization, Immunological,Stimulation, Immunologic,Immunizations,Immunological Sensitization,Immunological Sensitizations,Immunological Stimulations,Sensitizations, Immunological,Stimulation, Immunological,Stimulations, Immunological,Variolations
D007136 Immunoglobulins Multi-subunit proteins which function in IMMUNITY. They are produced by B LYMPHOCYTES from the IMMUNOGLOBULIN GENES. They are comprised of two heavy (IMMUNOGLOBULIN HEAVY CHAINS) and two light chains (IMMUNOGLOBULIN LIGHT CHAINS) with additional ancillary polypeptide chains depending on their isoforms. The variety of isoforms include monomeric or polymeric forms, and transmembrane forms (B-CELL ANTIGEN RECEPTORS) or secreted forms (ANTIBODIES). They are divided by the amino acid sequence of their heavy chains into five classes (IMMUNOGLOBULIN A; IMMUNOGLOBULIN D; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M) and various subclasses. Globulins, Immune,Immune Globulin,Immune Globulins,Immunoglobulin,Globulin, Immune
D008297 Male Males
D010957 Plasmids Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS. Episomes,Episome,Plasmid
D011247 Pregnancy The status during which female mammals carry their developing young (EMBRYOS or FETUSES) in utero before birth, beginning from FERTILIZATION to BIRTH. Gestation,Pregnancies
D011993 Recombinant Fusion Proteins Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes. Fusion Proteins, Recombinant,Recombinant Chimeric Protein,Recombinant Fusion Protein,Recombinant Hybrid Protein,Chimeric Proteins, Recombinant,Hybrid Proteins, Recombinant,Recombinant Chimeric Proteins,Recombinant Hybrid Proteins,Chimeric Protein, Recombinant,Fusion Protein, Recombinant,Hybrid Protein, Recombinant,Protein, Recombinant Chimeric,Protein, Recombinant Fusion,Protein, Recombinant Hybrid,Proteins, Recombinant Chimeric,Proteins, Recombinant Fusion,Proteins, Recombinant Hybrid
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs

Related Publications

V Martin, and M Arcavi, and G Santillan, and M R Amendoeira, and E De Souza Neves, and G Griemberg, and E Guarnera, and J C Garberi, and S O Angel
Development of specific immunoglobulins G, M, and A following primary Toxoplasma gondii infection in pregnant women.
October 1998, Journal of clinical microbiology,
V Martin, and M Arcavi, and G Santillan, and M R Amendoeira, and E De Souza Neves, and G Griemberg, and E Guarnera, and J C Garberi, and S O Angel
Evaluation of Recombinant SAG1 Protein for Detection of Toxoplasma gondii Specific Immunoglobulin M by ELISA Test.
January 2012, Iranian journal of parasitology,
V Martin, and M Arcavi, and G Santillan, and M R Amendoeira, and E De Souza Neves, and G Griemberg, and E Guarnera, and J C Garberi, and S O Angel
Subcellular localization and quantitative analysis of Toxoplasma gondii target antigens of specific immunoglobulins G, M, A, and E.
October 1994, Microscopy research and technique,
V Martin, and M Arcavi, and G Santillan, and M R Amendoeira, and E De Souza Neves, and G Griemberg, and E Guarnera, and J C Garberi, and S O Angel
Immuno-electron microscopic localization of antigenic sites for specific immunoglobulins G and M on Toxoplasma gondii surface.
March 1980, Bollettino dell'Istituto sieroterapico milanese,
V Martin, and M Arcavi, and G Santillan, and M R Amendoeira, and E De Souza Neves, and G Griemberg, and E Guarnera, and J C Garberi, and S O Angel
Recombinant antigens to detect Toxoplasma gondii-specific immunoglobulin G and immunoglobulin M in human sera by enzyme immunoassay.
March 2000, Journal of clinical microbiology,
V Martin, and M Arcavi, and G Santillan, and M R Amendoeira, and E De Souza Neves, and G Griemberg, and E Guarnera, and J C Garberi, and S O Angel
Anti-Toxoplasma gondii immunoglobulins A and G in human saliva and serum.
April 1997, Journal of oral pathology & medicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology,
V Martin, and M Arcavi, and G Santillan, and M R Amendoeira, and E De Souza Neves, and G Griemberg, and E Guarnera, and J C Garberi, and S O Angel
Immunoblot analysis of Toxoplasma gondii antigens by human immunoglobulins G, M, and A antibodies at different stages of infection.
July 1984, Journal of clinical microbiology,
V Martin, and M Arcavi, and G Santillan, and M R Amendoeira, and E De Souza Neves, and G Griemberg, and E Guarnera, and J C Garberi, and S O Angel
Expression of a recombinant Toxoplasma gondii ROP2 fragment as a fusion protein in bacteria circumvents insolubility and proteolytic degradation.
December 1999, Protein expression and purification,
V Martin, and M Arcavi, and G Santillan, and M R Amendoeira, and E De Souza Neves, and G Griemberg, and E Guarnera, and J C Garberi, and S O Angel
Epitopes recognized by human T lymphocytes in the ROP2 protein antigen of Toxoplasma gondii.
September 1996, Infection and immunity,
V Martin, and M Arcavi, and G Santillan, and M R Amendoeira, and E De Souza Neves, and G Griemberg, and E Guarnera, and J C Garberi, and S O Angel
Genetic immunization with plasmid DNA coding for the ROP2 protein of Toxoplasma gondii.
January 2001, Parasitology research,
Copied contents to your clipboard!