Interactions between Mouse Immunoglobulins and Staphylococcal Protein A

Chalon, M.P.; Milne, Ross W.; Vaerman, Jean‐Pierre

doi:10.1111/j.1365-3083.1979.tb03174.x

Cited by 49 publications

(11 citation statements)

References 21 publications

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“…Because of the unavailability ofmouse PAP, these studies either employed relatively insensitive immunofluorescence or, when the PAP technique was used (24), detected mouse hybridoma antibodies by staphylococcal protein A and rabbit PAP. However, protein A possesses only low affinity for mouse IgG1 (25). The relatively low sensitivity of immunocytochemical detection of antibodies required the use of cultured cells, frozen sections, or fixed whole mounts.…”

Section: Discussionmentioning

confidence: 99%

Neurotypy: regional individuality in rat brain detected by immunocytochemistry with monoclonal antibodies.

Sternberger¹,

Harwell²,

Sternberger³

1982

Proc. Natl. Acad. Sci. U.S.A.

107

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Hybridomas from spleen cell fusions of six BALB/c mice immunized with-hypothalamus were analyzed by immunocytochemistry for antibodies reactive with paraffin sections of fixed rat brain. In a total of 135 antibody producers, 60% were brain specific. Among these, 54% reacted with glial elements, pituitary cells, or basal lamina of intracerebral capillaries, with little variation among individual hybridomas in each of these groups. Forty-six percent ofbrain-specific antibodies reacted with neuronal structures, localizing on nerve fibers, neurofibrils, or perikarya. Neuron-specific hybridomas could be classified into groups that localized in anatomically defineable overall patterns. Within these patterns individual hybridomas exhibited extensive qualitative localization diversity ("neurotypy"). Conceivably, the genetic message for a common "proantigen" within an overall pattern may be slightly modified during differentiation of a neuron, thus leading to minor variability in antigenic expression. During antibody formation, similar minor changes occur in the differentiation of the genetic message for the antibody variable region. Apparently, minor changes in the antibody combining site among groups of hybridomas is reflected in -the detectability of minor neurotypic changes among differentiated neuronal proantigens. If neurotypy proves to be the result of single-base substitutions or of variability in alignment of peptide-coding exons, the Scharrer concept of the fundamental significance of neurosecretion could also become applicable to neuronal specialization.The Scharrer concept of the fundamental biologic role of neurosecretion (1, 2) ushered in the discovery ofan increasing number of neuropeptides in diverse regions of the nervous system (3). The existence of more than one peptide sequence in individual prohormones (4-7) and the coexistence in a single cell of given peptides with a variety of other peptides, unsuspected from the structure of known prohormones (8-11), suggest a great variability in the expression of prohormones among different neurons. On the supposition that such differences may be an expression of the functional diversity of "experienced" neurons, we explored its existence with the use of hybridoma antibodies to whole brain homogenate. Because each monoclonal antibody is reactive with a single antigenic determinant, it defines an antigen even ifit has not been chemically isolated. The only requirement for such application of monoclonal antibodies was the use of a technique for their detection that does not require availability of isolated antigen. Immunocytochemical analysis fulfills this requirement, because it defines an antibody clone by the anatomical distribution of its localization rather than the nature of the antigen with which it reacts. With the use of immunocytochemistry for intracellular antigens, we have found that a large proportion of antibodies to whole brain are brain specific, and that among these a sizeable fraction is neuron specific. MATERIALS AND METHODSSix BALB/c m...

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Section: Discussionmentioning

confidence: 99%

Neurotypy: regional individuality in rat brain detected by immunocytochemistry with monoclonal antibodies.

Sternberger¹,

Harwell²,

Sternberger³

1982

Proc. Natl. Acad. Sci. U.S.A.

107

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“…The reaction of specific MAbs with protein A provides a unique configuration of the immunoglobulin molecule to facilitate its antigen-binding Fab parts to be exposed outward, thus negating any steric hindrance and enabling the antibody to combine with the relevant antigen. Whereas certain isotypes of mouse immunoglobulins bind weakly to protein A, the isotypes IgG2a, IgG2b, and IgG3 have shown a strong binding affinity (3,17). MAb S2 was of the IgG3 isotype, which binds to protein A.…”

Section: Methodsmentioning

confidence: 98%

A Coagglutination Assay with Monoclonal Antibodies for Rapid Laboratory Identification of Mycoplasma synoviae

Morsy

Panangala²,

Gresham³

et al. 1992

Avian Diseases

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An agglutinating monoclonal antibody (MAb S2) specific for a 55,000-molecular-weight surface protein of Mycoplasma synoviae was developed by fusion of spleen cells from immunized BALB/c mice with P3X63 Ag8.653 myeloma cells. Immunogold labeling experiments confirmed the cell surface location of the MAb-recognized antigen. MAb S2-coated Staphylococcus aureus was used in a rapid slide coagglutination assay. Eleven M. synoviae strains, including the type strain WVU 1853, coagglutinated with MAb-coated S. aureus, but five M. gallisepticum strains (PG31, S6, R, F, and A5969) did not.

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“…IgG was separated by applying 2 ml portions of ascitic fluid to a 2 ml column of Protein A-Sepharose CL-4B (Pharmacia) with PBS, pH 7.3, as the starting buffer. After elution of unbound protein, 0.1 M citrate buffer, pH 3.5, was used to elute the antibody-containing IgG into 1 M Tris HC1 buffer, pH 8.5 [7,8]. The pooled fractions were dialysed in 0.9% NaC1 and, where necessary concentrated with Aquacide III (Calbiochem).…”

Section: Preparation Of the Monoclonal Antibodymentioning

confidence: 99%

Characterization of a monoclonal antibody to the group antigen of Chlamydia spp. and its use for antigen detection by reverse passive haemagglutination and indirect immunofluorescence

Thornley

1983

FEMS Microbiology Letters

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Interactions between Mouse Immunoglobulins and Staphylococcal Protein A

Cited by 49 publications

References 21 publications

Neurotypy: regional individuality in rat brain detected by immunocytochemistry with monoclonal antibodies.

Neurotypy: regional individuality in rat brain detected by immunocytochemistry with monoclonal antibodies.

A Coagglutination Assay with Monoclonal Antibodies for Rapid Laboratory Identification of Mycoplasma synoviae

Characterization of a monoclonal antibody to the group antigen of Chlamydia spp. and its use for antigen detection by reverse passive haemagglutination and indirect immunofluorescence

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