Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A new method is described for the detection of bacterial immunoglobulin A (IgA) protease which splits IgA into Fab and Fc fragments. The method takes advantage of a recent finding that receptors for IgA fragments occur commonly among type 4 group A streptococci. The bacterial preparation to be tested for protease activity was first incubated with radiolabeled purified IgA1 myeloma protein, and the proportion of radioactivity bound to a standard suspension of the streptococci was then measured. Since isolated Fab fragments do not bind to streptococcal IgA receptors, a decrease in the amount of radioactivity bound to the streptococci, as compared with the amount before digestion, indicates the presence of protease in the test preparation. Using this method, protease activity was detected in Neisseria gonorrhoeae, Neisseria meningitidis, Haemophilus influenzae, Streptococcus pneumoniae, and Streptococcus sanguis, but not in Escherichia coli or Branhamella catarrhalis.
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PMID:New method that uses binding of immunoglobulin A to group A streptococcal immunoglobulin A Fc receptors for demonstration of microbial immunoglobulin A protease activity. 701 17

A patient with chemotherapy-treated multiple myeloma developed overwhelming sepsis and meningoencephalitis with Haemophilus influenzae type f. Typable H. influenzae other than type b has only rarely been reported as a cause of serious disease in adults. The patient's immunosuppressed status presumably predisposed her to this unusual infection.
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PMID:Lethal meningoencephalitis and septicemia caused by Haemophilus influenzae type f in an adult with multiple myeloma. 703 42

A total of 59 infections were encountered in 29/46 patients with multiple myeloma (MM). Most infections arose in the urinary tract (31%), respiratory tract (29%), followed by blood (12%), oropharynx (12%), skin and soft tissue (7%). Gram-negative bacilli were identified in 51% of infections, most common being Enterobacteriaceae and Haemophilus influenzae. Gram-positive organisms were responsible for 7% of infections. 24% of patients with urinary tract infections had signs of cord compression Absolute lymphopenia was common, and was seen in 65% of patients with urinary infections, 75% of respiratory infections, and 86% of septicemic patients. In contrast, granulocytopenia was mainly observed in patients with septicemia (71%), followed by those with respiratory infections (31%). All patients were on cytotoxic chemotherapy, and most were hypoglobulinemic. About one third of septicemias, and one half of urinary and respiratory infections, respectively, were hospital-acquired. Results indicate that the current pattern of infections in MM seems to favor gram-negative organisms. The role of predisposing factors in the pathogenesis of infections in these patients is discussed.
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PMID:Changing patterns of infections in patients with multiple myeloma. 706 64

A murine monoclonal antibody, MAHI 3 (immunoglobulin G2b), that is broadly reactive with Haemophilus influenzae lipopolysaccharides (LPSs) but nonreactive with all enterobacterial LPSs tested was generated by fusing mouse myeloma cells with spleen cells of BALB/c mice immunized with azide-killed H. influenzae RM.7004. MAHI 3 bound to all H. influenzae, all other human Haemophilus spp., all Bordetella pertussis and Bordetella parapertussis, and all Aeromonas spp. tested but not to any Neisseria or Moraxella catarrhalis strains, as determined by enzyme immunoassay, colony dot immunoblotting, and immunoblotting. In an inhibition enzyme immunoassay, MAHI 3 reacted with all 45 H. influenzae LPSs tested but not with the LPS from the rough mutant I69 Rd-/b+, which has only 3-deoxy-D-manno-octulosonic acid (P) [Kdo(P)] and lipid A. The antibody was not inhibited by H. influenzae lipid A or lipid-free polysaccharide isolated after mild acid hydrolysis. Only native LPSs show positive inhibitory activity, indicating that part of lipid A is involved in the binding of MAHI 3. From the results, it is indicated that the structural element recognized by MAHI 3 is Hep alpha 1-->2Hep alpha 1-->3Hep alpha 1-->Kdo together with part of lipid A, including the phosphate.
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PMID:The tetrasaccharide L-alpha-D-heptose1-->2-L-alpha-D-heptose1--> 3-L-alpha-D-heptose1-->(3-deoxy-D-manno-octulosonic acid) and phosphate in lipid A define the conserved epitope in Haemophilus lipopolysaccharides recognized by a monoclonal antibody. 754 87

Mouse monoclonal antibodies (MAbs) DP8 [immunoglobulin G1(kappa)] and DH24 [immunoglobulin M(kappa)], which are specific for Haemophilus ducreyi lipopolysaccharide (LPS), were generated by fusing mouse myeloma NS0 cells with spleen cells of BALB/c mice immunized with a total membrane preparation of H. ducreyi. MAb DP8 reacted in whole-cell enzyme immunoassay (EIA) and colony dot immunoblotting with all 50 strains of H. ducreyi but not with any other bacteria tested, which suggests an exposed and species-specific epitope on the H. ducreyi cell surface. This conclusion was supported by the finding that DP8 bound to all six H. ducreyi LPSs tested but not to any of the Haemophilus influenzae or enterobacterial LPSs or synthetic glycoconjugates. The MAb DH24 bound to 43 of 50 strains of H. ducreyi and to few strains of H. influenzae, Neisseria gonorrhoeae, and Neisseria meningitidis, as evaluated by whole-cell EIA and colony dot immunoblotting. The MAb DH24 reacted with five of the six H. ducreyi LPSs tested and with the lacto-N-neotetraose (Gal beta 1-->4GlcNAc beta 1-->3Gal beta 1-->4Glc) series of synthetic glycoconjugates, as determined by EIA. By using polysaccharides obtained after both mild acidic hydrolysis and strong alkali treatment and dephosphorylated samples as inhibitors of the MAbs binding to H. ducreyi LPS antigens, it could be shown that phosphate groups were essential for the binding of DP8 to LPS but that they did not affect antigenic recognition by DH24. None of the MAbs bound to isolated lipid A, but aggregation caused by the fatty acids of lipid A was essential for epitope recognition.
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PMID:Monoclonal antibodies against Haemophilus lipopolysaccharides: clone DP8 specific for Haemophilus ducreyi and clone DH24 binding to lacto-N-neotetraose. 779 83

Monoclonal antibodies to polyribosylribitolphosphate (PRP), the capsular polysaccharide of Haemophilus influenzae type b (Hib), are useful tools in the investigation of the molecular and cellular mechanisms causing Hib meningitis. A better understanding of these mechanisms may lead to improved therapeutic strategies. A number of different in vivo immunization techniques in BALB/c mice were used, which did not however reveal detectable serum levels of antibodies to PRP. Therefore a modified in vitro immunization technique, originally established for in vitro immunization of human B lymphocytes, was used for this weak immunogen in mice. After 5 days of in vitro stimulation with purified PRP the splenic lymphocytes of BALB/c mice were fused with the mouse myeloma line P3-X63-Ag8.653. One hybridoma produced an IgM antibody (12E7) which recognized the capsular polysaccharide in ELISA and specifically labelled all tested Hib strains in immune fluorescent microscopy. The blotted polysaccharide PRP was immunostained with monoclonal antibody 12E7. Preincubation of Hib with this antibody enhanced the oxygen radical metabolism of polymorphnuclear leucocytes in a chemiluminescence assay. There was no cross-reactivity with the supernatants of other Haemophilus influenzae serotypes and other bacterial species, as shown by counterimmunoelectrophoresis.
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PMID:Characterization of a monoclonal antibody to the capsule of Haemophilus influenzae type b, generated by in vitro immunization. 782 41

Protein D is a surface-exposed lipoprotein of the gram-negative bacterium Haemophilus influenzae with affinity for human immunoglobulin D myeloma protein. The gene encoding protein D (hpd) in a serotype b strain of H. influenzae was cloned. Escherichia coli carrying the hpd gene bound human myeloma immunoglobulin D. Nucleotide sequence analysis identified an 1,092-bp open reading frame that was more than 99% identical to the hpd gene from a nontypeable H. influenzae strain. In the deduced amino acid sequences for protein D, only 2 of 364 amino acid residues differed. The restriction fragment length polymorphism of the hpd region in different strains was analyzed by Southern blot analyses of PstI- or EcoRI-digested genomic DNA from 100 H. influenzae strains. The analysis was performed by using isolated fragments of the cloned hpd gene, originating from the nontypeable H. influenzae 772, as probes. All strains tested had DNA sequences with a high degree of homology to the hpd probes. The analysis also showed that restriction endonuclease sites within the gene were more conserved than sites adjacent to the hpd gene. An interesting difference between type b strains and unencapsulated strains was observed. The majority of type b strains seem to have a 1.4-kbp DNA fragment upstream of the hpd gene that is absent in nontypeable strains. On the basis of the high degree of conservation of the hpd gene among H. influenzae strains, we conclude that protein D is a possible vaccine candidate.
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PMID:Limited diversity of the protein D gene (hpd) among encapsulated and nonencapsulated Haemophilus influenzae strains. 810 99

This article reports a case of pyogenic arthritis with Hemophilus influenzae in a previously healthy woman. This infection was the initial manifestation of an underlying serious systemic illness, multiple myeloma. Certain laboratory parameters as well as the causative organism suggested the underlying disease. Although infections are common in patients with known multiple myeloma, certain infections can provide a hint to concomitant serious systemic diseases and thus facilitate their early diagnosis.
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PMID:Multiple myeloma presenting with Hemophilus influenzae septic arthritis: case report and review of the literature. 837 Dec 86

A new, efficient procedure for the generation of human monoclonal antibodies has been developed. The procedure is based on the activation of human B cells in microwells by murine thymoma EL4B5 cells. This mode of B cell stimulation leads to proliferation of at least one per eight of human B cells and to a high rate of antibody production. Subsequently, supernatants of the microwells are screened by ELISA for the presence of antibody of the desired specificity and B cells from selected wells are hybridized by electroporation. To optimize the procedure, the kinetics of the B cell expansion induced by EL4B5 cells were analysed. Counting and phenotyping of cultured cells at different time points indicated that the peak of B cell expansion occurred at day 5 for tonsil B cells (16-fold increase) and at day 7 for peripheral blood B cells (20-fold increase). The B cells did not merely proliferate but also differentiated, as indicated by loss of CD20 expression and increase of CD38 expression. At the peak of B cell expansion, B cells could be hybridized efficiently with myeloma cells. The majority of the resultant hybridomas secreted human immunoglobulin. The efficiency of the procedure is exemplified by the generation of hybridomas secreting human IgG against Haemophilus influenzae from limited numbers of either human tonsil B lymphocytes or peripheral blood B lymphocytes.
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PMID:An efficient procedure for the generation of human monoclonal antibodies based on activation of human B lymphocytes by a murine thymoma cell line. 845 Feb 31

Mouse monoclonal antibodies MAHI 4 and MAHI 10 reactive with Haemophilus influenzae lipopolysaccharide (LPS), were generated by fusing mouse myeloma cells with spleen cells of mice immunized with H. influenzae strain RM.7004-XP-1. The antibody MAHI 4 reacted in whole-cell enzyme immunoassay (EIA) and colony-dot-immunoblotting with 20 of 123 H. influenzae strains and to a few other human Haemophilus spp. and Neisseria spp., but not to any Bordetella pertussis, B. parapertussis, Aeromonas spp. or Moraxella catarrhalis strains tested. This suggests a specific epitope accessible to recognition in just a few strains. This conclusion was supported by the data on binding of MAHI 4 to only three of 18 H. influenzae LPSs tested, but not to any Haemophilus ducreyi or enterobacterial LPSs. The antibody MAHI 10 bound to 80 of 123 strains of H. influenzae and to a few strains of Neisseria spp. and M. catarrhalis as evaluated by EIA and colony-dot-immunoblotting, which suggests an epitope accessible to recognition in 65% of the H. influenzae strains tested. The antibody MAHI 10 reacted with 10 of 18 H. influenzae LPSs as determined by EIA. By using polysaccharides, obtained after both mild acidic hydrolysis, strong alkali treatment, and dephosphorylation, as inhibitors of the antibodies binding to H. influenzae LPS antigens it was shown that phosphate groups were essential for the binding of MAHI 10 to LPS but they did not affect antigenic recognition by MAHI 4. None of the monoclonal antibodies bound to isolated lipid A, but the aggregation caused by the fatty acids of lipid A was essential for optimum epitope recognition. Enzymatic treatment of homologous LPSs with galactose-oxidase led to products which were between 20 to 30 times less effective as inhibitors of the binding of the MAHI 4 than the native LPSs. Taken together the results indicate that MAHI 4 has the following pentasaccharide as the epitope Gal beta 1-->2 Hep alpha 1-->2Hep alpha 1-->3Hep alpha 1--> Kdo(P). These results emphasize the importance of the terminal beta-Gal residue in the definition of the MAHI 4 specificity, and of the terminal phosphorylated saccharide residues of some of the Haemophilus LPSs for the MAHI 10 specificity.
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PMID:Monoclonal antibodies against Haemophilus influenzae lipopolysaccharides: clone MAHI 4 binding to a pentasaccharide containing terminal beta-Gal residues and clone MAHI 10 recognizing terminal phosphorylated saccharide residues. 893 39


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