Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0519030 (Klebsiella)
 21,988 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We purified and characterized a new fimbria termed KPF-28 (Klebsiella pneumoniae fimbria with a fimbrin molecular mass of 28 kDa) involved in K. pneumoniae adherence to the human carcinoma cell line Caco-2. Electron microscopy of bacterial surface protein preparations and immunogold labeling of bacterial cells showed that KPF-28 was a long, thin, and flexible fimbria about 4 to 5 nm in diameter and 0.5 to 2 microm long. The N-terminal amino acid sequence of the KPF-28 major fimbrial subunit showed no homology with type 1 and type 3 pili of K. pneumoniae but showed 61.7% identity with residues 6 to 19 of the N-terminal amino acid sequence of PapA, the Pap major pilus subunit expressed by uropathogenic Escherichia coli strains. Total amino acid content determination showed that the KPF-28 major subunit composition was close to that of the GVVPQ fimbrial family major subunits expressed by pathogenic E. coli strains. The study of the prevalence of KPF-28 among K. pneumoniae strains involved in nosocomial infections revealed that KPF-28 was found in the great majority of the K. pneumoniae strains producing the CAZ-5/SHV-4 extended-spectrum beta-lactamase. As shown by curing and mating experiments, the R plasmid encoding the CAZ-5/SHV-4 enzyme was found to be involved in but not solely responsible for KPF-28 expression. Hybridization experiments using an oligonucleotide probe corresponding to the N-terminal part of the 28-kDa protein revealed that the structural gene encoding the KPF-28 major subunit was localized on this R plasmid. KPF-28 is a putative colonization factor of the human gut, since the ceftazidine-sensitive derivative strain CF914-1C no longer adhered and since the Fab fragments of antibodies raised against KPF-28 inhibited adhesion of K. pneumoniae CF914-1 to the Caco-2 cell line.
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PMID:A new fimbrial antigen harbored by CAZ-5/SHV-4-producing Klebsiella pneumoniae strains involved in nosocomial infections. 867 36

From whole-cell DNA of an enterobacterial Erwinia persicina reference strain that displayed a penicillinase-related antibiotic-resistant phenotype, a beta-lactamase gene was cloned and expressed in Escherichia coli. It encoded a clavulanic-acid-inhibited Ambler class A beta-lactamase, ERP-1, with a pI value of 8.1 and a relative molecular mass of ca. 28 kDa. ERP-1 shared 45 to 50% amino acid identity with the most closely related enzymes, the chromosomally encoded enzymes from Citrobacter koseri, Kluyvera ascorbata, Kluyvera cryocrescens, Klebsiella oxytoca, Proteus vulgaris, Proteus penneri, Rahnella aquatilis, Serratia fonticola, Yersinia enterocolitica, and the plasmid-mediated enzymes CTX-M-8 and CTX-M-9. The substrate profile of the noninducible ERP-1 was similar to that of these beta-lactamases. ERP-1 is the first extended-spectrum beta-lactamase from an enterobacterial species that is plant associated and plant pathogenic.
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PMID:Identification of a chromosome-borne expanded-spectrum class a beta-lactamase from Erwinia persicina. 1238 42

The 3 murine monoclonal antibodies, Yps1, Yps2 and Yps3 reactive to Y. pseudotuberculosis can be stabilized and all were found to be of IgG type. Monoclonal antibody, Yps1, recognized a glycoprotein antigen of the organism with reactivity at the 55-75 kDa region, while Yps2 and Yps3 recognized protein antigens of Y. pseudotuberculosis 65 kDa and 26-28 kDa molecular weight regions, respectively. The specificity of monoclonal antibodies was tested using dot ELISA and Western blotting with whole cell organisms or whole cell sonicated soluble antigens of different Yersinia species, Salmonella typhi, Klebsiella pnemoniae, Streptococcus abortus-equi and Escherichia coli. Monoclonal antibody, Yps1 exhibited cross-reactivity with soluble antigens and whole cell preparations of Y. pestis. Yps2 cross-reacted to soluble antigens of all the tested bacteria. Reactivity of monoclonal antibody, Yps3 was restricted to Y. pseudotuberculosis and Y. pestis with soluble antigen preparations. No reaction was observed with Yps2 and Yps3 to whole cell organism preparations from tested bacteria including Y. pseudotuberculosis. The co-agglutination reagent prepared by sensitizing staphylococcal cells with Yps1 monoclonal antibody produced a positive agglutination with all the 4 Y. pseudotuberculosis isolates and the 3 Y. pestis strains tested. Sandwich dot ELISA using monospecific antisera as a capture antibody and a monoclonal antibody, and Yps3 as a revealing antibody had a high level of specificity in detecting Y. pseudotuberculosis antigens.
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PMID:Characterization and utilization of monoclonal antibodies reactive to Yersinia pseudotuberculosis. 1511 97

A Swedish patient of Indian origin traveled to New Delhi, India, and acquired a urinary tract infection caused by a carbapenem-resistant Klebsiella pneumoniae strain that typed to the sequence type 14 complex. The isolate, Klebsiella pneumoniae 05-506, was shown to possess a metallo-beta-lactamase (MBL) but was negative for previously known MBL genes. Gene libraries and amplification of class 1 integrons revealed three resistance-conferring regions; the first contained bla(CMY-4) flanked by ISEcP1 and blc. The second region of 4.8 kb contained a complex class 1 integron with the gene cassettes arr-2, a new erythromycin esterase gene; ereC; aadA1; and cmlA7. An intact ISCR1 element was shown to be downstream from the qac/sul genes. The third region consisted of a new MBL gene, designated bla(NDM-1), flanked on one side by K. pneumoniae DNA and a truncated IS26 element on its other side. The last two regions lie adjacent to one another, and all three regions are found on a 180-kb region that is easily transferable to recipient strains and that confers resistance to all antibiotics except fluoroquinolones and colistin. NDM-1 shares very little identity with other MBLs, with the most similar MBLs being VIM-1/VIM-2, with which it has only 32.4% identity. As well as possessing unique residues near the active site, NDM-1 also has an additional insert between positions 162 and 166 not present in other MBLs. NDM-1 has a molecular mass of 28 kDa, is monomeric, and can hydrolyze all beta-lactams except aztreonam. Compared to VIM-2, NDM-1 displays tighter binding to most cephalosporins, in particular, cefuroxime, cefotaxime, and cephalothin (cefalotin), and also to the penicillins. NDM-1 does not bind to the carbapenems as tightly as IMP-1 or VIM-2 and turns over the carbapenems at a rate similar to that of VIM-2. In addition to K. pneumoniae 05-506, bla(NDM-1) was found on a 140-kb plasmid in an Escherichia coli strain isolated from the patient's feces, inferring the possibility of in vivo conjugation. The broad resistance carried on these plasmids is a further worrying development for India, which already has high levels of antibiotic resistance.
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PMID:Characterization of a new metallo-beta-lactamase gene, bla(NDM-1), and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India. 1977 Feb 75