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PubMed1988

Anti-Klebsiella K30 phospholipid antibodies in systemic lupus erythematosus: antigen cross-reactions and idiotypic sharing with antibodies to DNA and Klebsiella K30 polysaccharide.

Patients with systemic lupus erythematosus were examined for the presence of serum antibodies reactive with phospholipids (PL) extracted from the membranes of Klebsiella K30 (K30PL). Affinity-purified anti-K30PL antibodies were tested for their ability to cross-react with other PL antigens or DNA and for the presence of idiotypic markers known to be associated with anti-DNA antibodies or antibodies to Klebsiella K30 polysaccharide (K30p). Affinity-purified antibodies to K30PL, phosphatidylserine (PS), or phosphatidylinositol (PL) uniformly cross-reacted with each other. Analysis of the PL preparations by thin-layer chromatography and reversed-phase high-performance liquid chromatography (HPLC) showed the presence of several components. Lupus sera reacted with one component mainly in the HPLC-fractionated K30PL preparation, although this component appeared to be present in the other PL preparations. Direct-binding and inhibition studies showed that affinity-purified antibodies to the K30PL extract, PS, or PI reacted poorly with DNA. However, the anti-K30PL antibodies possessed a prominent anti-DNA idiotypic marker (AM Id) in 61% of the patients and an anti-K30p idiotypic marker (SP Id) in 94% of the patients. The results thus show that anti-K30PL antibodies are idiotypically related to anti-DNA and anti-K30p antibody subpopulations, although they do not share the same antigen-binding characteristics.

Antibodies, Antinuclear↗

PubMed1986

Depolymerization of the capsular polysaccharide from Klebsiella K19 by the glycanase associated with particles of Klebsiella bacteriophage luminal diameter 19.

The site of cleavage of the capsular polysaccharide from Klebsiella K19 by the endoglycanase associated with particles of Klebsiella bacteriophage luminal diameter 19 was determined. The specific cleavage of the bond Rhap-(1----2)-Rhap provided a series of oligosaccharides having rhamnose at the reducing end. The enzyme is thus an alpha-rhamnosidase. Structural studies on the oligomers confirmed the sequence of the repeating unit of the polysaccharide from K19. The 1H- and 13C-n.m.r. spectra of the homologous series of oligosaccharides corresponding to one, two, three, and four repeat-units exhibit important differences that denot variation of conformation with chain length. The bacteriophage acted on modified forms of K19 polysaccharide to provide a series of linear oligomers, and emphasized the essential role of the negative charge on the uronic acid in the action of the glycanase.

Bacteriophages↗

PubMed1988

A murine monoclonal antibody against Klebsiella capsular polysaccharide is opsonic in vitro and protects against experimental Klebsiella pneumoniae infection.

Murine monoclonal antibodies (mAb) of the immunoglobulin M class specific for the K2 capsular polysaccharide (CPS) of Klebsiella were isolated. One such mAb, termed III/5-1, was selected for further study. This mAb promoted the uptake and killing of Klebsiella pneumoniae K2 strains by human granulocytes and activated complement after contact with the bacteria. The efficiency of mAb-mediated phagocytosis and complement activation was inversely related to the amount of capsular material produced by the test strain. MAb III/5-1 was found to be effective at preventing fatal experimental K. pneumoniae K2 sepsis when administered prophylactically, the degree of protection being dependent upon the amount of CPS produced by the challenge strain.

Animals↗

PubMed1983

Klebsiella-induced LIF response in Klebsiella infection and ankylosing spondylitis.

Lymphocyte transformation and leucocyte migration inhibition was studied in Klebsiella-sensitized patients, ankylosing spondylitis patients and healthy controls. The results show that mononuclear cells from ankylosing spondylitis patients respond more vigorously to Klebsiella, one of the 'trigger' bacteria, than do mononuclear cells from healthy persons, either with or without HLA-B27.

Adult↗

PubMed1999

Comparative in vitro activities of ciprofloxacin, clinafloxacin, gatifloxacin, levofloxacin, moxifloxacin, and trovafloxacin against Klebsiella pneumoniae, Klebsiella oxytoca, Enterobacter cloacae, and Enterobacter aerogenes clinical isolates with alterations in GyrA and ParC proteins.

The in vitro activities of ciprofloxacin, clinafloxacin, gatifloxacin, levofloxacin, moxifloxacin, and trovafloxacin were tested against 72 ciprofloxacin-resistant and 28 ciprofloxacin-susceptible isolates of Klebsiella pneumoniae, Klebsiella oxytoca, Enterobacter cloacae, and Enterobacter aerogenes. Irrespective of the alterations in GyrA and ParC proteins, clinafloxacin exhibited greater activity than all other fluoroquinolones tested against K. pneumoniae and E. aerogenes.

Anti-Infective Agents↗

PubMed1980

Identification of the major adherence ligand of Klebsiella pneumoniae in the receptor for coliphage T7 and alteration of Klebsiella adherence properties by lysogenic conversion.

We have studied the adherence of both laboratory and wild-type Klebsiella pneumoniae strains, isolated from sputum, urine, and stool samples, to human buccal and intestinal and urinary tract epithelial cells. Of 32 unencapsulated strains, 30 adhered to all epithelial cells tested. Four K. pneumoniae strains lysogenic for AP3, a phage which causes conversion to resistance of coliphages T3, T7, and phi I, were all unable to adhere to epithelial cells. One of these strains was cured from phage infection and became capable of adhering, Spontaneous mutants resistant to coliphage T7, as well as K. pneumoniae K59-sensitive cells preadsorbed with inactivated T7 particles, did not adhere to epithelial cells. All strains capable of adhering were able to adsorb coliphage T7 and T3, whereas all nonadhesive strains were not. AP3-like prophages were induced from 7 of 12 nonadhesive Klebsiella strains. A laboratory strain which was able to adhere was lysogenized with 2 of these phages. In both cases, the strain lost its ability to adsorb coliphages T3, T7, and phi I and to adhere to human epithelial cells. All K. pneumoniae adhesive strains agglutinated yeast cells, whereas the nonadhesive strains did not. Competition studies have shown that D-mannose and concanavalin A prevented adherence to human epithelial cells, yeast agglutination, and adsorption of coliphage T7 to K. pneumoniae cells. It is concluded that in K. pneumoniae adherence to epithelial cells is mediated by the receptor for coliphages T7 (and T3), which in turn recognizes D-mannose in the receptors it binds.

Cell Adhesion↗

PubMed1983

Hemagglutinins of Klebsiella pneumoniae and Klebsiella oxytoca.

The occurrence and characteristics of hemagglutinins were investigated in 310 Klebsiella strains (195 K. pneumoniae- and 115 K. oxytoca-strains). Mannose-sensitive (MS)-hemagglutinins as well as Mannose-resistant (MR/K)-hemagglutinins could be demonstrated, only 13 Klebsiella-strains were not able to hemagglutinate. MS-hemagglutinins were much more often found in K. pneumoniae- than in K. oxytoca-strains, whereas the MR/K-hemagglutinin-frequency was equally high. Features (resistance to formaldehyde, trypsin, pronase, glycosidases, sodium metaperiodate and heating) and pathogenic significance of these hemagglutinins (fimbriae) were discussed.

Hemagglutination Tests↗

PubMedDate not supplied

[Additional anti-Klebsiella phages used in lysotyping of Klebsiella strains].

In order to increase the efficiency of lysotyping as a method for differentiating Klebsiella strains the authors tested the activity of 10 additional phages isolated, prepared and studied in the laboratory and compared to the Slopek-Milch set. A number of 734 Klebsiella strains were isolated in different clinical and epidemiological conditions and lysotyped. The phage type was determined in 64.60% of the strains examined, using 15 phages of the Slopek-Milch set. By using additional autochtonous phages the proportion of lysotypable strains reached 77.80%; therefore, 13.20% were sensitive only to the additional phages.

Bacteriophage Typing↗

PubMed1982

Immunochemical properties of oligosaccharide-protein conjugates with Klebsiella-K2-specificity. II. Protective capacity of the conjugates and anti-conjugate antibodies against infection with Klebsiella pneumoniae 01:K2 in mice.

Oligosaccharide subunits from Klebsiella pneumoniae B5055 capsular polysaccharide, covalently linked to protein carriers, the native polysaccharide, and killed whole bacteria, were compared with respect to their immunogenicity in mice and their capacity to protect mice against bacterial infection. The protection was studied (a) by active immunization and (b) by passive administration of antisera raised in rabbits using the different immunogens. The results were as follows: in the active protection experiments the octa- and dodecasaccharide conjugates were as effective as the polysaccharide in increasing the LD50 by a factor of 10(5) as compared to nonimmunized animals. Thus, these antigens were only slightly less effective than killed bacteria. In contrast the tetrasaccharide conjugate was at least 1000-fold less effective than all other antigens used. In the passive protection experiments these results were paralleled in that the antiserum against the tetrasaccharide conjugate also showed the lowest degree of protection, though, for methodical reasons, the differences in the LD50s were less pronounced. The drastically lower efficiency of the tetrasaccharide in comparision to its higher oligomers is in agreement with serological findings previously published (see first communication), which showed that two repeating units are the minimum requirement for a substantial representation of polysaccharide serological specificity.

Animals↗

PubMed2004

Recurrent Klebsiella pneumoniae mycotic aneurysm in a diabetic patient and emergence of an extended-spectrum beta-lactamase (CTX-M-24)-containing Klebsiella pneumoniae strain after prolonged treatment with first-generation cephalosporins for mycotic aneurysm.

A 68-year-old diabetic woman suffered from mycotic aneurysm due to Klebsiella pneumoniae over her abdominal aorta; she received surgical intervention, followed by treatment with first-generation cephalosporins for 6 months. She was hospitalized again 11 months later because of another episode of mycotic aneurysm caused by K. pneumoniae on her thoracic aorta. Fingerprinting generated by pulsed-field gel electrophoresis and infrequent-restriction-site polymerase indicated K. pneumoniae isolates of the identical clonal strain were responsible for these two mycotic-aneurysm episodes. Unfortunately, nosocomial pneumonia developed at the second hospitalization; blood and purposefully sampled feces specimen cultures both grew CTX-M-24-producing K. pneumoniae, which were of the same strain and genetically nonrelated to the K. pneumoniae strain causing mycotic aneurysms earlier. This is the first report on infection due to CTX-M-24-producing K. pneumoniae. It is unclear whether the prolonged use of first-generation cephalosporins in this case selected a strain of enteric organism possessing the ESBL in question, which was capable of passing this ESBL plasmid to the K. pneumoniae strain causing the nosocomial infection. This report suggests that further observation is needed before one can draw a conclusion on the possibility of the selection of ESBL enteric organism by extensive exposure to first-generation cephalosporins.

Aneurysm↗

PubMed1976

Klebsiella L-forms: effect of growth as L-form on virulence of reverted Klebsiella pneumoniae.

A strain of Klebsiella pneumoniae virulent for mice was serially passaged in vitro as a penicillin-induced L-form. Periodically, the L-form was reverted to the bacterial form by removal of penicillin, and the revertant was tested for virulence. Virulence was gradually reduced, and after 109 passages the revertant was totally avirulent. Virulence was not restored by 40 passages of the revertant through mouse peritoneum. The revertant grew less vigorously and did not infect mice when inoculated subcutaneously; in contrast, the parental form was found in all tissues examined. After phagocytosis in vitro or in vivo, the revertant survived but did not increase in numbers, whereas the parental form did increase in numbers. The revertant had a much smaller capsule than did the parental form. Immunization with the live revertant resulted in type-specific protection against infection with the parental form.

Animals↗

PubMed1984

Vaccination against 77 capsular types of Klebsiella aerogenes with polyvalent Klebsiella vaccines.

A method is described for producing monovalent and polyvalent vaccines from culture filtrates of Klebsiella aerogenes. With a single injection, each monovalent vaccine protected mice against lethal intraperitoneal challenge by more than 30 capsular types; and polyvalent vaccines containing 2-12 monovalent components protected against 46-61 of the 77 capsular types of K. aerogenes. One vaccine with 12 components, administered in two doses, induced full protection against 71 types and protected half of the mice challenged with the other six types.

Animals↗

PubMed2000

A novel complex mutant beta-lactamase, TEM-68, identified in a Klebsiella pneumoniae isolate from an outbreak of extended-spectrum beta-lactamase-producing Klebsiellae.

Twenty-two Klebsiella pneumoniae and two K. oxytoca extended-spectrum beta-lactamase (ESBL)-producing isolates were collected in 1996 from patients in two pediatric wards of the University Hospital in Wrocław, Poland. Molecular typing has revealed that the K. pneumoniae isolates represented four different epidemic strains. Three kinds of enzymes with ESBL activity (pI values of 5.7, 6.0, and 8.2) were identified. The pI 6.0 beta-lactamases belonged to the TEM family, and sequencing of the bla(TEM) genes amplified from representative isolates revealed that these enzymes were TEM-47, previously identified in K. pneumoniae isolates from pediatric hospitals in Lódz and Warsaw. One of the TEM-47-producing strains from Wrocław was very closely related to the isolates from the other cities, and this indicated countrywide spread of the epidemic strain. The pI 5.7 beta-lactamase was produced by a single K. pneumoniae isolate for which, apart from oxyimino-beta-lactams, the MICs of beta-lactam-inhibitor combinations were also remarkably high. Sequencing revealed that this was a novel TEM beta-lactamase variant, TEM-68, specified by the following combination of mutations: Gly238Ser, Glu240Lys, Thr265Met, and Arg275Leu. The new enzyme has most probably evolved from TEM-47 by acquiring the single substitution of Arg275, which before was identified only twice in enzymes with inhibitor resistance (IR) activity. TEM-68 was shown to be a novel complex mutant TEM beta-lactamase (CMT-2) which combines strong ESBL activity with relatively weak IR activity and, when expressed in K. pneumoniae, is able to confer high-level resistance to a wide variety of beta-lactams, including inhibitor combinations. This data confirms the role of the Arg275Leu mutation in determining IR activity and documents the first isolation of K. pneumoniae producing the complex mutant enzyme.

Disease Outbreaks↗

PubMed2004

Comparison of pyogenic liver abscess caused by non-Klebsiella pneumoniae and Klebsiella pneumoniae.

From January 1996 to April 2002, a total of 248 patients with pyogenic liver abscess were enrolled in this study. Abscesses caused by Klebsiella pneumoniae accounted for 69% (171) of cases. Abscesses caused by K. pneumoniae were more strongly associated with diabetes mellitus or impaired fasting glucose than liver abscesses caused by non-K. pneumoniae (70.2% vs 32.5%). Solitary abscess and monomicrobial isolates were more frequent in the K. pneumoniae group than that in the non-K. pneumoniae group. A total of 42 patients were treated with antibiotics alone. Antibiotics treatment was combined with other procedures, including single aspiration in 23 patients, percutaneous drainage in 176 and surgical drainage in 7. A higher incidence of metastatic infections occurred in the K. pneumoniae group than in the non-K. pneumoniae group (14.6% vs 3.8%). By contrast, the mortality rate of the K. pneumoniae group was lower than that of non-K. pneumoniae group (4.1% vs 20.8%). There was no significant difference in the relapse rate between these 2 groups (6.5% vs 6.4%). We also found that the presence of respiratory symptoms (including cough, dyspnea, or chest distress), size of abscess > or =5 cm in diameter and non-K. pneumoniae pathogens were significant prognostic factors for mortality.

Adolescent↗

PubMed2006

[Hydrolytic and haemolytic activity of Klebsiella pneumoniae and Klebsiella oxytoca].

Hydrolytic enzymes and haemolysins are important extracellular substances produced by many bacteria. We investigated 57 K. pneumoniae strains and 40 K. oxytoca strains isolated from clinical materials. We estimated the ability to produce: proteases hydrolyzing milk powder, caseinase, gelatinase, elastase, lecithinase, lipases, DNase and haemolysins on human, sheep and horse erythrocytes on TSA medium with or without 5% Egg Yolk. We detected that K. oxytoca strains produced proteases hydrolyzing milk powder (37.5%), caseinase (15.0%) and gelatinase (17.5%) more frequently than K. pneumoniae strains (respectively 21.0%, 5.3%, 8.9%). None of the analysed Klebsiella spp. strains produced elastase. Only K. pneumoniae strains produced lecithinase (5.3%). Lipases hydrolyzing Tween were produced from 3.5% (for Tween 60 and 80) to 7.0% (for Tween 20). Among K. oxytoca strains only one (2.5%) hydrolyzing Tween 20. DNase was produced by 38.6% of K. pneumoniae strains and by 27.5% K. oxytoca strains. Haemolytic properties on human erythrocytes were detected in 5.3% K. pneumoniae strains on TSA medium and 29,8% on medium with Egg Yolk. In K. oxytoca strains haemolytic properties on human erythrocytes were detected only on medium with Egg Yolk (12.5%). Haemolytic properties on sheep erythrocytes were detected respectively in 21.0% and 22.8% K. pneumoniae strains and in 7.5% K. oxytoca strains on each medium. Haemolytic properties on horse erythrocytes were detected respectively in 33.4% and 52.6% K. pneumoniae strains and in 15.0% and 20.0% K. oxytoca strains.

Animals↗

PubMed1982

Action of iron and iron-complexes on Klebsiella pneumoniae (Klebsiella aerogenes).

Iron In the Fe(III) oxidation state had a negligible effect on the growth of Klebsiella pneumoniae even at the highest concentration (0.45 mM) obtainable without precipitation in a minimal medium containing glucose and inorganic salts together with Tris as the buffer and glycerol 2-phosphate as the phosphorus source. Nevertheless in its presence the toxic action of Cd2+, Zn2+ and Cu2+ was antagonized while that of Co2+ and Ni2+ was potentiated. Higher iron levels were obtained by supplementing the minimal medium with fructose, glycine, gluconate, tartrate and citrate at a range of concentrations. With fructose and glycine all of the resulting solutions were red-brown and non-toxic. This was also found with the other complexing agents when the ligand:iron were low, but at higher ligand:iron ratios the solutions were green and toxic. Iron-citrate systems were especially toxic but resistance developed and was of the graded type. The results are discussed with particular reference to earlier physico-chemical studies by other workers and it is concluded that the red-brown colour is characteristic of the presence of polymers of high molar mass and that the green colour signifies the formation of low molar mass species.

Drug Interactions↗

PubMed2005

Crystal structures of Mycobacteria tuberculosis and Klebsiella pneumoniae UDP-galactopyranose mutase in the oxidised state and Klebsiella pneumoniae UDP-galactopyranose mutase in the (active) reduced state.

Uridine diphosphogalactofuranose (UDP-Galf) is the precursor of the d-galactofuranose sugar found in bacterial and parasitic cell walls, including those of many pathogens. UDP-Galf is made from UDP-galactopyranose by the enzyme UDP-galactopyranose mutase. The enzyme requires the reduced FADH- co-factor for activity. The structure of the Mycobacterium tuberculosis mutase with FAD has been determined to 2.25 A. The structures of Klebsiella pneumoniae mutase with FAD and with FADH- bound have been determined to 2.2 A and 2.35 A resolution, respectively. This is the first report of the FADH(-)-containing structure. Two flavin-dependent mechanisms for the enzyme have been proposed, one, which involves a covalent adduct being formed at the flavin and the other based on electron transfer. Using our structural data, we have examined the two mechanisms. The electron transfer mechanism is consistent with the structural data, not surprisingly, since it makes fewer demands on the precise positioning of atoms. A model based on a covalent adduct FAD requires repositioning of the enzyme active site and would appear to require the isoalloxazine ring of FADH- to buckle in a particular way. However, the FADH- structure reveals that the isoalloxazine ring buckles in the opposite sense, this apparently requires the covalent adduct to trigger profound conformational changes in the protein or to buckle the FADH- opposite to that seen in the apo structure.

Amino Acid Sequence↗

PubMed2001

The structure of the core region of the lipopolysaccharide from Klebsiella pneumoniae O3. 3-deoxy-alpha-D-manno-octulosonic acid (alpha-Kdo) residue in the outer part of the core, a common structural element of Klebsiella pneumoniae O1, O2, O3, O4, O5, O8, and O12 lipopolysaccharides.

The structure of lipid A-core region of the lipopolysaccharide (LPS) from Klebsiella pneumoniae serotype O3 was determined using NMR, MS and chemical analysis of the oligosaccharides, obtained by mild acid hydrolysis, alkaline deacylation, and deamination of the LPS: [carbohydrate structure see text] where P is H or alpha-Hep; J is H or beta-GalA; R is H or P (in the deacylated oligosaccharides). Screening of the LPS from K. pneumoniae O1, O2, O4, O5, O8, and O12 using deamination showed that they also contain alpha-Hep-(1-->4)-alpha-Kdo-(2-->6)-GlcN and alpha-Kdo-(2-->6)-GlcN fragments.

Carbohydrate Sequence↗