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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Nine monoclonals against human Ig lambda chains were produced, 4 antibodies react with C-domain, 5--with V-domain of the lambda chain. Anti-C lambda domain antibodies recognize not less than 3 epitopes and one of them is expressed only on the isolated chain. Anti-V lambda antibodies bind both isolated lambda chain and intact IgG, IgM, IgA. Four epitopes are expressed by few lambda Bence Jones proteins of the III subgroup, the immunogen possessing the same isotype. The 4 mentioned epitopes represent private idiotypic determinants. The epitope 3E10 is characteristic of 50% Bence Jones proteins of the II and III V lambda-subgroups thus representing a common idiotypic determinant. Using anti-V lambda antibodies germ line variability of V lambda III proteins was analysed and the similarity of antigenic structure of normal and myeloma human Ig lambda chains was demonstrated.
Mol Biol (Mosk)
PMID:[Study of the antigenic structure of human immunoglobulin lambda-chain using monoclonal antibodies]. 169 12

Alphafetoprotein (AFP), an oncofetal antigen, plays very important roles in the early embryonic life and oncogenesis. Under various physiological and pathological conditions AFP exhibits microheterogeneity, probably as a result of differential expression of its epitopes. To analyse the epitopes we have developed a panel of monoclonal antibodies against human AFP purified by a new and efficient method using an immunoadsorbent consisting of polyclonal antibodies immobilized on cyanogen bromide activated Sepharose. Clones producing antibodies of various isotypes, e.g. IgG1, IgG2a, IgG2b, IgA and IgM have been subcloned and characterized. The antibodies showed high avidity for AFP (with half-maximal binding concentrations between 0.012 and 3.87 nM). Mutual inhibition efficiencies of a panel of 14 monoclonal antibodies were determined by RIA. Based on these inhibition data a computer program was used to group these antibodies with respect to their "epitope specificity distance". As a result of this grouping, clones have been identified which can recognize at least five different epitopes on AFP. This panel of antibodies may be very useful for analysis of the epitopic variation of AFP under various physiological and pathological conditions.
Mol Immunol 1991 Jul
PMID:Epitope analysis of the oncofetal antigen alphafetoprotein using monoclonal antibodies. 171 94

Protein 511, a murine IgA protein described previously by Robinson and Appella [Proc. natn. Acad. Sci. U.S.A. 77, 4909-4913 (1980)] which lacks 36 amino acids in the C alpha 3 domain, was tested for its ability to bind to radiolabelled secretory component (125I-rat SC) and to be transported from blood to bile in the rat, a function described previously to be mediated by the poly Ig receptor (pIg R). When compared to other mouse pIgA proteins, the naturally occurring mutant protein 511 bound 125I-rat SC and was transported from blood to bile in a manner indistinguishable from wild-type pIgA protein. We conclude that the region of Fc alpha which is missing in protein 511, is not involved in mediating the binding of pIgA to the pIg R.
Mol Immunol 1992 Jan
PMID:Binding of secretory component to protein 511, a pIgA mouse protein lacking 36 amino acid residues of the C alpha 3 domain. 173 Nov 89

The utility of biodegradable and biocompatible microspheres as a vaccine delivery system for the induction of systemic and disseminated mucosal antibody responses was investigated. Intraperitoneal (ip) injection into mice of 1-10 microns microspheres, constructed of the copolymer poly(DL-lactide-coglycolide) (DL-PLG) which contained approximately 1% by weight a formalinized toxoid vaccine of staphylococcal enterotoxin B (SEB), dramatically potentiated the circulating IgG anti-toxin antibody response as compared to the free toxoid. The initiation of vaccine release was delayed in larger microspheres, and a mixture of 1-10 and 20-50 microns microspheres stimulated both a primary and an anamnestic secondary anti-toxin response following a single injection. However, neither free nor microencapsulated SEB toxoid induced a detectable mucosal IgA anti-toxin response following systemic injection. In contrast, three peroral immunizations with toxoid-microspheres stimulated circulating IgM, IgG and IgA anti-toxin antibodies and a concurrent mucosal IgA response in saliva, gut washings and lung washings. Systemic immunization with microencapsulated toxoid primed for the induction of disseminated mucosal IgA responses by subsequent oral or intratracheal (it) boosting in microspheres, while soluble toxoid was ineffective at boosting. These results indicate that biodegradable and biocompatible microspheres represent an adjuvant system with potentially widespread application in the induction of both circulating and mucosal immunity.
Mol Immunol 1991 Mar
PMID:Biodegradable microspheres as a vaccine delivery system. 201 98

The peptide regulatory factors (PRFs), variously termed cytokines, lymphokines, interleukins, colony stimulating factors, interferons, etc., play a key role in the quantitative and qualitative regulation of protective responses--both in initiating immunological and inflammatory responses and in mediating and controlling the effector mechanisms that protect the body against micro-organisms. The process of immunization--involving antigen-presentation, lymphocyte-activation and clonal proliferation--depends on the action of a variety of PRFs. The function of accessory cells--the dendritic cells, macrophages, etc.--is stimulated by PRFs such as interferon-gamma, IL-1, TNF, GM-CSF and IL-4. The activation and expansion of T-lymphocytes requires IL-1, IL-2, IL-4, interferon-gamma, IL-6 and probably IL-7. Likewise, the activation and expansion of B-lymphocytes is regulated by PRFs such as IL-1, IL-2, IL-4, IL-5, IL-6, IL-7 and interferon-gamma. It is likely, although unproven, that PRFs also regulate the differentiation of B-cells to memory cells. Successful vaccination requires the immune system to be primed in such a way that natural challenge with a micro-organism or its products evokes an immune response that has the qualitative and the quantitative characteristics of both the humoral and cellular responses. Antibody class is critically influenced by particular PRFs, e.g. interferon-gamma regulates IgG2a; IL-4, IgE and IgG1; IL-5 and TGF-beta, IgA. PRFs are both produced by and regulate the T-lymphocytes which have key roles in protective responses--either directly, viz. the cytotoxic T-lymphocytes important in protection against certain viruses, or indirectly through the secretion of PRFs that regulate the speed, magnitude and quality of antibody cellular responses. The recruitment and enhanced production and function of granulocytic and phagocytic cells involves a number of T-lymphocyte PRFs including GM-CSF, IL-3, IL-5, IL-4, and IL-6. We do not have a good understanding of the fine-tuning of cellular responses nor of how infection with different pathogens results in different types of inflammatory responses; it is clear, however, that certain cellular responses are due to the action of specific PRFs, e.g. IL-3 induces a mastocytosis and IL-5 an eosinophilia. There is increasing evidence that the relative levels of different PRFs are important determinants of the effectiveness of responses.(ABSTRACT TRUNCATED AT 400 WORDS)
Mol Immunol 1991 Mar
PMID:Peptide regulatory factors and optimization of vaccines. 201 99

The discovery of jacalin, a group of lectins from jackfruit seeds (Artocarpus heterophyllus), has attracted considerable attention due to its numerous interesting immunological properties as well as its usefulness in the isolation of various serum proteins. We have further identified a similar lectin from the seeds of Champedak (Artocarpus integer) which we refer to as lectin-C and performed comparative studies with two types of jacalin isolated from different batches of the Malaysian jackfruit seeds (jacalin-M1 and jacalin-M2). The three purified lectins demonstrated equivalent apparent Mr of about 52,500, each of which comprised of a combination of two types of non-covalently-linked subunits with apparent Mr of approximately 13,300 and 16,000. The lectins demonstrated equal haemagglutinating activity against human erythrocytes of blood groups A, B, AB and O. Our data also demonstrated that lectin-C, jacalin-M1 and jacalin-M2 are similar by selectively precipitating human serum IgA1 and colostral sIgA but not IgA2, IgD, IgG and IgM. When immunoelectrophoresis was performed on normal human sera and reacted with the lectins, single precipitin arcs corresponding to IgA immunoprecipitates were detected with lectin-C and jacalin-MI. Jacalin-M2, however, exhibited two closely associated precipitin arcs. The binding of these lectins with IgA was pronouncedly inhibited in the presence of p-nitrophenyl-beta-D-galactopyranoside, 1-o-methyl-alpha-D-galactopyranoside, D-melibiose, N-acetyl-D-galactosamine and D-galactose. The data therefore provide evidence on the differential specificity of IgA binding lectins isolated from seeds of similar as well as distinct Artocarpus species.
Mol Immunol
PMID:IgA binding lectins isolated from distinct Artocarpus species demonstrate differential specificity. 206 19

A cell surface receptor that binds to the Fc region of IgA is expressed by certain strains of group A streptococci. The physico-chemical properties and binding characteristics of this receptor, called protein Arp, were studied. Like bacterial receptors that bind IgG, protein Arp has an elongated shape and no disulfide bonds. The affinity constant of protein Arp for three different molecular forms of IgA was determined, and was found to be more than ten-fold higher for serum IgA than for two complexed forms of IgA: secretory IgA and IgA bound to alpha 1-microglobulin. Cleavage of protein Arp with CNBr resulted in a peptide corresponding to the region located outside the cell wall, except for the N-terminal 52 amino acids. This CNBr-fragment did not bind IgA, which strongly suggests that the IgA-binding region of protein Arp is located in the N-terminal part of the molecule. In addition to the binding of IgA, protein Arp also binds to IgG weakly. The pH-dependence of these two types of binding is different, with maximal binding of IgA at neutral pH (5-7) and maximal binding of IgG at acidic pH (3-5). Both for IgA and IgG, protein Arp shows strong specificity for immunoglobulins of human origin.
Mol Immunol
PMID:Binding properties of protein Arp, a bacterial IgA-receptor. 206 17

Cross-reactive idiotypes (CRI) on human rheumatoid factors (RF), which are identified by murine monoclonal antibodies (mAb), have proved useful in defining both the incidence and the structural characteristics of these autoantibodies. In this study, a new murine anti-idiotypic reagent, mAb B6, has been used to identify and define the expression of a distinct heavy chain CRI. The B6 CRI was found on 20% of monoclonal IgM (16 of 81), but on only 5% of monoclonal IgA (1 of 20) and on no monoclonal IgG. In addition, this CRI was expressed exclusively on a subset of Ig derived from the VHIII protein variable region subgroup. In immunoblotting experiments, the mAb B6 bound directly to the heavy (H) chains of CRI positive proteins. The B6 CRI was found frequently on monoclonal IgM-RF molecules, and the mAb B6 could inhibit the binding of the RF to its IgG antigen. It was also demonstrated that Staphylococcus aureus protein A (SpA), which has recently been shown to bind to the F(ab) region of VHIII molecules, could block the interaction of some B6 CRI positive IgM to the anti-CRI. These experiments suggest that the B6 CRI is a marker for one or a few VHIII genes and that it is expressed commonly on IgM paraproteins, many of which have RF activity.
Mol Immunol 1990 Jan
PMID:The incidence of a new human cross-reactive idiotype linked to subgroup VHIII heavy chains. 210 94

Forty-eight group A streptococcal strains of different M types were screened for binding of human radiolabeled IgG. Three of the strains bound more than 80% of the added radioactivity and one of them, an M protein type 1 strain designated AP1, was selected for further analysis. Attempts were made to solubilize the IgG binding bacterial molecule, and small amounts of an IgG binding protein with a mol. wt of 40 kDa could be solubilized with mutanolysin, a muramolytic agent. The gene encoding this streptococcal protein was cloned and expressed in E. coli, and the E. coli-produced protein was purified in a single step by affinity chromatography on IgG-Sepharose. When tested with IgGs from different species, the molecule was found to bind human IgG almost exclusively. The N-terminal amino acid sequence was determined and showed no homology with previously isolated Ig binding proteins, and the name protein H (as in human IgG) is suggested for this novel Ig binding bacterial protein. Protein H showed preferential affinity for heavy chains and Fc fragments of human IgG, and did not bind Ig light chains. The affinity constant, determined by Scatchard plots, between protein H and human polyclonal IgG was 1.6 x 10(9). No binding was observed between protein H and IgM, IgA, IgD, or IgE. Finally, when tested against several additional proteins and human plasma, protein H only showed weak binding to alpha 2-macroglobulin, a proteinase inhibitor.
Mol Immunol 1990 Jun
PMID:Protein H--a novel IgG binding bacterial protein. 219 20

Two synthetic peptides corresponding to overlapping sequences from the C-terminus of the B chain of Shiga toxin were prepared and characterized. These peptides consisted of residues 54-67 and 57-67 in the protein sequence. This region coincides with the major peak of surface area residues, as predicted from a computer-derived plot. For the purpose of immunization, the peptides were either conjugated with a protein or a synthetic carrier, or were polymerized. Polyclonal antibodies against these peptides derivatives, induced in rabbits, recognized the homologous peptides and cross-reacted with the intact toxin. These antibodies were capable of neutralizing the various biological activities of the toxin, namely the cytotoxic, enterotoxic and neurotoxic activities. Active immunization of mice with the peptide derivatives protected them from the lethal effect of the toxin. Moreover, oral immunization of rats led to inhibition of fluid secretion in ligated ileal loops into which toxin was injected. This effect was paralleled by the induction of high levels of specific anti-peptide IgA antibodies in the serum after bile duct ligation.
Mol Immunol 1990 Jul
PMID:Carboxy-terminal peptides from the B subunit of Shiga toxin induce a local and parenteral protective effect. 220 62


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