Navegando por Palavras-chave "MONOCLONAL ANTIBODIES"

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    CHARACTERIZATION OF GLYCOPROTEIN GP43, THE MAJOR LAMININ-BINDING PROTEIN OF PARACOCCIDIOIDES-BRASILIENSIS
    (Assoc Bras Divulg Cientifica, 1994-09-01) Lopes, Jose Daniel [UNIFESP]; Campos, Maria Cecilia Reis de Moura [UNIFESP]; Vicentini, A. P.; Gesztesi, Jean-Luc [UNIFESP]; Desouza, W.; Camargo, Zoilo Pires de [UNIFESP]; Universidade Federal do Rio de Janeiro (UFRJ); Universidade Federal de São Paulo (UNIFESP)
    We have demonstrated that laminin mediates the adhesion of P. brasiliensis to monolayers of epithelial cells through specific binding to the surface glycoprotein gp43. This binding seems to be related to the fungal pathogenesis. We now report the confirmation of these findings by scanning electron microscopy and show that some isolates that do not secrete gp43 do express the protein as seen by studying whole cell extracts. These results confirm the ability of these strains to produce paracoccidioidomycosis but should not be used for serological purposes since the absence of gp43 in exoantigens may lead to false negative results.
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    IMMUNOCHEMICAL CHARACTERIZATION OF CARBOHYDRATE ANTIGENS FROM FUNGI, PROTOZOA AND MAMMALS BY MONOCLONAL-ANTIBODIES DIRECTED TO GLYCAN EPITOPES
    (Assoc Bras Divulg Cientifica, 1995-08-01) Straus, Anita Hilda [UNIFESP]; Suzuki, E.; Toledo, Marcos Sergio de [UNIFESP]; Takizawa, C. M.; Takahashi, Helio Kiyoshi [UNIFESP]; Universidade Federal de São Paulo (UNIFESP)
    Cell surface carbohydrates constitute the major antigenic determinants of fungi and protozoa. Glycoconjugates also represent a large variety of antigens or markers present in mammals such as histo-blood groups ABO, differentiation and heterophile antigens, among others. This article focuses on the general properties of glycoconjugate antigens and production and characterization of the anti-carbohydrate monoclonal antibodies (MoAbs). It describes the specificity and some properties of monoclonal antibodies directed against carbohydrate epitopes present in tumor-associated glycoproteins, in glycosaminoglycans of higher eukaryotes and in glycolipid antigens of protozoa and fungi. The epitopes recognized by the anti-carbohydrate MoAbs range from one sugar unit up to ten sugar units. Although most anti-carbohydrate MoAbs are directed predominantly toward terminal sugar residues, a few MoAbs are also reactive with internal sugar residues. The fine structure of the carbohydrate epitopes has been chemically defined by [H-1] NMR, GC/MS of alditol acetates of partially permethylated compounds, (-)FAB/MS, degradation with exoglycosidases and inhibition with different methyl-glycosides and oligosaccharides.
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    PRODUCTION AND CHARACTERIZATION OF MONOCLONAL-ANTIBODIES TO SHARK CARTILAGE PROTEOGLYCAN
    (Assoc Bras Divulg Cientifica, 1994-09-01) Alves, MLM; Straus, Anita Hilda [UNIFESP]; Takahashi, Helio Kiyoshi [UNIFESP]; Michelacci, Yara Maria [UNIFESP]; Universidade Federal de São Paulo (UNIFESP)
    1. Two proteoglycans, PG1 and PG2, have been isolated from shark cartilage. Both are highly polydisperse and large (molecular mass: 1-10 X 10(6) Daltons) and contain chondroitin sulfate and keratan sulfate side chains, but PG2 is somewhat smaller than PG1 and contains less keratan sulfate.2. Monoclonal antibodies were raised against PG1. Many antibodies were obtained and one of them, MST1, was subcloned and further characterized. This monoclonal antibody reacts with PG1 and PG2 from shark cartilage and also with aggrecan from bovine trachea cartilage. Chondroitinase AC-treated proteoglycans react with MST1, indicating that the antibody does not recognize chondroitin sulfate. MST1 also recognizes aggrecan from human cartilage and a proteoglycan from bovine brain (neurocan) but it does not recognize proteoglycans from rat Walker tumor, fetal calf muscle and decorin from human myoma.3. Using MST1 we were able to demonstrate that both PG1 and PG2 aggregate with hyaluronic acid.