Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The earliest preparations of immunoglobulins (Ig) decreased the susceptibility of agammaglobulinemic patients to infections caused by pneumococci, Haemophilus influenzae, meningococci, streptococci, and Pseudomonas aeruginosa. Intramuscular administration of such preparations was painful and traumatic, especially for children. Ethanol-fractionated Ig could not be administered intravenously (IV) because the IgG molecules tended to aggregate and thus were more likely to produce anaphylactoid reactions. New Ig preparations, isolated at low pH (e.g., pH 4) in the presence of traces of pepsin to inhibit reaggregation, were well tolerated when administered IV. Thus a new era of treatment and prophylaxis of disease using IV Ig (IVIG) was launched. The IVIG preparations revolutionized the management of virtually all immunodeficiency syndromes characterized by failure of antibody responses. Amelioration of antibody deficiency secondary to certain chronic diseases or surgical trauma can be achieved with these preparations. Newer uses of IVIG include treatment of some autoimmune diseases; in some conditions, the beneficial influences may be attributable to antiidiotype antibodies present in the IVIG. Another likely explanation is that IVIG inhibits damage to cells and tissues by antibody-mediated cellular cytotoxicity or blocks phagocytosis that is facilitated by Fc receptor mechanisms. The value of IVIG in preventing infection in patients undergoing bone marrow or organ transplantation and in the treatment and prophylaxis of life-threatening infections in neonates and premature infants also is reviewed.
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PMID:Historic aspects of intravenous immunoglobulin therapy. 187 38

A library of genomic DNA fragments from Haemophilus influenzae type b (Hib) DL42 was constructed in plasmid pBR322, transformed into Escherichia coli strain RR1, and screened for recombinant clones with haemin-binding activity by plating onto haemin-containing agar. Expression of haemin-binding activity by clones correlated with the expression of a protein with an apparent molecular weight of 51,000 (51K) that was also recognized by anti-Hib strain DL42 serum in immunoblots. One recombinant clone, designated pHM2, with the smallest DNA insert (3.62 kb) was characterized further. Ethanol inhibition of expression of pHM2 in minicells revealed that the 51K protein was the result of a processing event involving a larger precursor. E. coli RR1(pHM2) adsorbed haemin in liquid suspensions as well as from solid media. Subcloning of a 2.6 kb fragment of pHM2 into a shuttle vector permitted the construction of a recombinant Hib clone, DL42(pHM1002), which overexpressed the 51K haemin-binding protein. This 51K protein appears to be peripherally associated with the inner, and possibly outer, membranes of Hib. Affinity chromatography on haemin-agarose was utilized to purify the haemin-binding protein from both E. coli RR1(pHM2) and Hib DL42(pHM1002) to near homogeneity. The use of the antibiotic globomycin in a minicell expression system and radioimmunoprecipitation analysis of Hib proteins intrinsically radiolabelled with [3H]-palmitate indicated that the 51K haemin-binding protein is a lipoprotein.
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PMID:Molecular cloning, partial purification, and characterization of a haemin-binding lipoprotein from Haemophilus influenzae type b. 204 70

An in vitro antimicrobial activity and phytochemical analysis of various extracts of Indigofera trita L. viz. petroleum ether, chloroform, acetone, ethanol and aqueous extracts were carried out. A total of 21 microorganisms (19 bacteria and 2 fungal strains) were used for antimicrobial activity by disc diffusion method and a standard procedure was used to identify the phytochemical constituents. Petroleum ether extract showed moderate inhibitory activity against Staphylococcus aureus (14.40 mm), S. epidermidis (14.20 mm), Salmonella paratyphi A (12.80 mm), Streptococcus mutans (12.20 mm), Escherichia coli, Proteus vulgaris, S. typhi and Burkholderia cepacia (12.00 mm). The chloroform extract also showed antimicrobial activity against S. epidermidis (14.20 mm), S. typhimurium (12.60 mm), S. paratyphi A, S. brunei and Yersinia enterocolitica (12.00 mm). The acetone extract of I. trita showed considerable inhibitory activity against S. epidermidis (18.20 mm), S. typhimurium (14.60 mm), S. infantis (13.80 mm), S. aureus (13.40 mm), Y. enterocolitica (13.00 mm) and Enterobacter aerogenes (12.00 mm) were documented. Ethanol extract showed significant antimicrobial activity against S. epidermidis (18.60 mm), S. paratyphi A (14.60 mm), Y. enterocolitica (13.40 mm), S. typhi (12.40 mm), S. aureus, E. aerogenes, S. typhimurium and S. infantis (12.00 mm). Aqueous extract of I. trita considerably inhibited S. epidermidis (13.80 mm), S. paratyphi A and Y. enterocolitica (12.20 mm), E. aerogenes and Haemophilus parahaemolyticus (12.00 mm). All the five extracts showed a minimal antifungal activity when compared to antibacterial activity. The result revealed that the antimicrobial properties of I. trita might be associated with the presence of phenolic compounds, flavonoids, tannins, glycosides, saponins, phytosterols and alkaloids.
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PMID:Antimicrobial efficacy and phytochemical analysis of Indigofera trita Linn. 2414 83