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)

In vitro susceptibilities of bacterial pathogens to beta-lactam antibiotics were determined. Bacterial pathogens examined included various isolates from the patients of respiratory tract infections at the hospitals of Kyoto-Shiga area in 1981 and 1983. Major organisms isolated from clinical specimens were Haemophilus spp., Klebsiella spp., Pseudomonas spp., S. aureus and Streptococcus spp. An increase in the isolation frequency of P. aeruginosa, a decrease in the isolation frequency of H. influenzae and no change in the isolation frequency of the other organisms were observed between the years 1981 and 1983. Data from susceptibility tests of clinical isolates confirmed that cefazolin (CEZ) and cefotiam (CTM) showed good antibacterial activity against S. aureus and cefmenoxime (CMX) was highly effective on Streptococcus spp., but that the susceptibilities of both organisms to CEZ, CTM, and cefmetazole (CMZ) in 1983 were lower than in 1981. Although CMX also showed good antibacterial activity against Klebsiella spp., there were no changes in the effectiveness of CTM, CMZ, and CEZ between the years 1981 and 1983. The in vitro antibacterial activities of CMX and cefoperazone against Haemophilus spp. were superior to those of the other beta-lactams tested, but there was a decline in the efficacy for CEZ. Although cefsulodin and piperacillin were highly active against Pseudomonas spp., declines in their effectiveness was observed between the years 1981 and 1983.
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PMID:[In vitro susceptibility of bacterial isolates from patients with respiratory tract infections to beta-lactam antibiotics]. 373 68

In vitro susceptibilities of bacterial pathogens to beta-lactam antibiotics were determined. Bacterial pathogens examined included various isolates from patients of respiratory tract infections at hospitals of Kyoto-Shiga area in 1984. Major organisms isolated from clinical specimens were Pseudomonas spp., Klebsiella spp., Haemophilus spp., Staphylococcus aureus and Streptococcus spp. An increase in the isolation frequency of Pseudomonas spp., a decrease in the isolation frequency of S. aureus, and no change in the isolation frequency of other organisms were observed between the years 1981, 1983 and 1984. Data from susceptibility tests of clinical isolates confirmed that cefazolin (CEZ), cefamandole and cefotiam (CTM) showed good antibacterial activity against S. aureus and cefmenoxime (CMX) was highly active against Streptococcus spp., but their susceptibilities to CEZ in 1984 were lower than in 1983. Susceptibilities of Klebsiella spp. to CMX, cefbuperazone, latamoxef, CTM, cefoperazone (CPZ) were better than those to other beta-lactam antibiotics tested, but there was a decline in the susceptibility to CEZ, cefmetazole and CTM. Further, CMX, CPZ and LMOX also showed good antibacterial activity against Haemophilus spp. Although gentamicin, cefsulodin, cefpiramide and piperacillin were highly active against Pseudomonas spp., resistant organisms were present for all the beta-lactam antibiotics tested.
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PMID:[In vitro susceptibility, of bacterial isolates from patients with respiratory tract infections, to beta-lactam antibiotics II]. 382 May 70

Four murine monoclonal antibodies (MAbs) reactive with the outer-core region of the lipopolysaccharide (LPS) from Haemophilus influenzae were generated after immunization with azide-killed H. influenzae RM.7004 AH1-2 and their epitope specificities studied. The monoclonal antibodies: MAHI 6 (IgM), MAHI 5 (IgG2a), MAHI 8 (IgG3), and MAHI 11 (IgG2b) bound to synthetic glycoconjugates or glycolipids with terminal galabiosyl (Gal alpha 1-->4Gal beta 1-) or globotriaosyl (Gal alpha 1-->4Gal beta 1 1-->4GLc) residues as evaluated in enzyme immunoassays (EIA). Glycoconjugates or glycolipids with internally placed galabiose elements were not active, indicating selectively of the MAbs for recognition of the epitope. Nine LPSs from H. influenzae inhibited the binding of the four MAbs. The presence of the galabiosyl disaccharide element in these nine LPSs was evidence by the binding of 125I-labeled Shiga toxin isolated from the bacterium Shigella dysenteriae type 1, reported to have as receptor the Gal alpha 1-->4Gal beta disaccharide (Lindberg et al., J Biol Chem, 1987, 262: 1779-85). Structural studies of these H. influenzae LPSs were also in accord with the presence of the galabiosyl disaccharide, in addition 1H-NMR spectroscopy showed the presence of O-acetyl groups in the RM.7004 AH1-2 LPS. However, differential binding specificities of the MAbs to modified RM.7004 AH1-2 LPSs were observed. MAHI 6 and MAHI 11 bound equally well to LPS, polysaccharides obtained after mild acidic treatment, and dephosphorylated LPS samples as shown in inhibition EIA. In contrast, both dephosphorylated LPS samples and polysaccharides were poorer inhibitors of the binding of MAHI 5 and MAHI 8 to native RM.7004 AH1-2 LPS. Neither the de-O-acylated nor the de-O,N-acylated LPSs were effective inhibitors of any of the four MAbs. These results suggest that the MAbs recognition involves Gal alpha 1-->4Gal and O-acetyl and other saccharide residue(s) from the oligosaccharide moiety of the LPS. The epitopes are also expressed and accessible to recognition in clinical isolates coming from different sources of Neisseria spp., Haemophilus spp., and Moraxella catarrhalis, but not in Bordetella spp., Aeromonas spp. or Enterobacteriaceae as evaluated by whole-bacteria EIA and colony-dot-immunoblotting.
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PMID:Binding specificity for four monoclonal antibodies recognizing terminal Gal alpha 1-->4Gal residues in Haemophilus influenzae lipopolysaccharide. 855 43

Enterobacterial GATC-specific DNA adenine methyltransferase (Dam) plays an essential role in regulation of DNA replication, methyl-directed mismatch repair, transposition and gene expression. In Salmonella typhimurium it has been shown to directly control virulence. In this paper we report cloning and expression of the dam gene from the Shiga toxin-producing VT2-Sa prophage of enterohemorrhagic Escherichia coli O157. Comparisons of the predicted amino acid sequence indicates that Dam methyltransferases of E. coli phages VT2-Sa, 933W, T1 and Haemophilus influenzae phage HP1 make up a separate subgroup of adenine-N6 methyltransferases. These proteins are similar to the gamma subfamily of amino-methyltransferases in respect to the linear order of sequence motifs and the presence of the hallmark "NPPY" tetrapeptide. However, they apparently lack an autonomous target-recognizing domain at the C-terminus of the catalytic domain and therefore we propose to dub them as a "mini-gamma" subfamily.
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PMID:Cloning of enterohemorrhagic Escherichia coli phage VT-2 dam methyltransferase. 1172 Mar 11