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PubMed1979

Isolation, characterization, and biological properties of an endotoxin-like material from the gram-positive organism Listeria monocytogenes.

The bacterial component responsible for the induction of transient cold agglutinin syndrome in rabbits after intravenous injection of heat-killed Listeria monocytogenes type 4B has been purified and biologically and chemically characterized. A purified immunoglobulin M cold agglutinin was prepared from high-titer sera resulting from the immunization of rabbits with heat-killed L. monocytogenes type 4B and was subsequently used to monitor the purification of the bacterial component responsible for its induction. The bacterial component was isolated from a hot phenol-water extract of lyophilized L. monocytogenes type 4B by multiple molecular sieve chromatography. Upon chemical analysis the purified material was found to be strikingly similar in chemical composition to gram-negative lipopolysaccharide endotoxins. The material contained 15% total fatty acid (of which 50% was beta-hydroxymyristic acid), 40 to 45% neutral sugar (glucose, galactose, and rhamnose), 11.5% amino sugar, 12% uronic acid, 2.5% 2-keto-3-deoxyoctonic acid, 2% heptose, 0.87% phosphorus, and 1.6% amino acid, thereby accounting for 85 to 90% of the weight of the component. Electron micrographs of the purified material were similar to those of lipopolysaccharide preparations from gram-negative organisms. The purified material exist in aqueous solutions as large aggregates, but can be dissociated into a single smaller subunit (3.1S) by dialysis against sodium dodecyl sulfate buffer. The listerial component was toxic and pyrogenic to rabbits, producing symptoms typical of gram-negative endotoxins. Activity in the limulus lysate gelation assay and in the carbocyanine dye assay provides a further link of this material with classical gram-negative endotoxins.

Agglutinins↗

PubMed1979

Chemical composition and biological activities of a phenol-water extract from Haemophilus influenzae type a.

Ribonucleic acid was removed from a phenol-water extract of Haemophilus influenzae type a by streptomycin sulfate. This preparation was called purified preparation or PP. It contained neutral sugars (glucose, galactose, mannose, pentose), glucosamine, amino acids, and fatty acids. Heptose and 2-keto-3-deoxyoctonic acid were not present. The biological properties and immunogenicity were compared with the activities of lipopolysaccharide of Escherichia coli or Salmonella typhimurium. Higher doses were necessary to obtain lethality in mice and Sanarelli and Shwartzman reactions with our preparations than were necessary with lipopolysaccharide. The Limulus test and pyrogen assay in rabbits gave the same results with purified preparation and lipopolysaccharide, but pyrogenicity of purified preparation was not destroyed by NaOH treatment. Purified preparation was not as immunogenic at low doeses for rabbits as lipopolysaccharide. The results were different from those obtained with lipopolysaccharide but similar to those known from peptidoglycan studies. The contamination of purified preparation with peptidoglycan was negligible and cannot explain the biological activities of purified preparation. We suggest that the phenol-water extract from H. influenzae is not a classical endotoxin, but rather an endotoxin-like substance.

Animals↗

PubMed1980

Immunochemical studies of the lipopolysaccharides of Vibrio cholerae: constitution of O specific side chain and core polysaccharide.

Lipopolysaccharides from various strains of Vibrio cholerae have been found to consist of distinct O-specific side chain and core polysaccharide regions in their degraded polysaccharides. The major identifiable components in the core polysaccharide were phosphorus, glucose, heptose, fructose, and ethanolamine phosphate, with small amounts or traces of mannose, rhamnose, and D-perosamine. On the other hand, glucose, fructose, mannose, rhamnose, glucosamine, D-quinovosamine, and D-perosamine were identified from O-specific side chain polysaccharide. The amounts of each component have been determined from O-specific side chain and core polysaccharides of the lipopolysaccharides from these bacterial strains.

Chemical Phenomena↗

PubMed1980

Biological and chemical characterization of endotoxin from Capnocytophaga sputigena.

An endotoxin was isolated from Capnocytophaga sputigena strain 4 by a modification of the hot phenol-water method. The extraction procedure yielded a lipopolysaccharide which accounted for approximately 1.5% of the dry weight of the cells. The material was composed of 18.6% lipid (as C(15) fatty acid), 46.5% neutral sugar including 9.6% hexose, 18.3% 6-deoxy sugar, 1.0% 2-keto-3-deoxy sugar, and 4.8% heptose. Hexosamine, protein, and phosphorus were found in quantities amounting to 9.0, 2.9, and 2.0% of the dry weight, respectively. No pentose or nucleic acid was detected. Acid hydrolysis resulted in the release of the constituent sugars and the formation of an insoluble precipitate. The lipopolysaccharide was tested for numerous biological activities characteristic of endotoxins. The pyrogenicity was relatively low; the fever index 40 was 17 mug, and 10 mug was required to give the characteristic biphasic fever response. The toxicity of the extract was very low, with a 50% chicken embryo lethal dose of 15.6 mug and a 50% mouse embryo lethal dose of greater than 8 mg. Similarly, the C. sputigena endotoxin had modest effects on leukocytes when compared with endotoxin standards from other organisms. The extract exhibited little or no mitogenicity when tested on mouse spleen lymphocytes. It was not toxic to human peripheral polymorphonuclear leukocytes and caused the release of only a small (13%) portion of lysosomal enzymes. Although the C. sputigena lipopolysaccharide caused significant activation of mouse peritoneal macrophages, the dose required was twice that of an Escherichia coli endotoxic standard. However, the Limulus amoebocyte lysate clotting activity of the lipopolysaccharide was comparable to that of an Serratia marcescens lipopolysaccharide standard, and passive hemagglutination tests revealed that 1 mug of the lipopolysaccharide was capable of sensitizing 1 ml of a 2% sheep erythrocyte suspension for agglutination with an antiserum prepared against C. sputigena whole cells.

Animals↗

PubMed1980

Chemical structure and inhalation toxicity of lipopolysaccharides from bacteria on cotton.

Lipopolysaccharides from different bacteria isolated from cotton were purified and chemically analyzed. Their pulmonary toxicity to animals was tested in inhalation tests. Lipopolysaccharides from Agrobacterium and Xanthomonas were shown to differ from the others in that they contained no heptose and no non-hydroxylated fatty acids with a chain length of 12, 14, or 16 carbon atoms. Lipopolysaccharides from Pseudomonas putida, Enterobacter agglomerans, and Klebsiella oxytoca were found to cause an influx of polymorphonuclear leukocytes into the airways. Lipopolysaccharides from Agrobacterium sp. and Xanthomonas sinensis caused no significant invasion. The data point to substances in both the lipid A part and the core part of the lipopolysaccharides being responsible for the capacity to induce leukocyte invasion into the airways.

Animals↗

PubMed1981

Monoclonal antibody analysis of lipopolysaccharide from Neisseria gonorrhoeae and Neisseria meningitidis.

A hybridoma produced by the polyethylene glycol fusion of the NS-1 variant of the P3x63Ag8 BALB/c plasmacytoma to splenocytes harvested from a BALB/c mouse immunized with whole gonococci was found to be producing antibody to a common region on gonococcal lipopolysaccharide (LPS). Enzyme-linked immunosorbent assay inhibition systems were established by utilizing this antibody, designated 3F11, and 100% inhibition occurred with both LPS and the LPS-LPS and LPS-derived polysaccharides partially inhibited the enzyme-linked immunosorbent assay, whereas similar preparations isolated from Escherichia coli O:111, the J-5 mutant of this strain, and Salmonella minnesota Re595 failed to inhibit the assay. Studies utilizing whole gonococcal strains 4505 and the isogenic variant 4505r, which lacks both the LPS serotype and common determinants as inhibitors, demonstrated that the determinant recognized by the 3F11 antibody was present on the surface of 4505 and absent on 4505r. Inhibition studies were performed with beta-glucose, beta-galactose, D-glucosamine, D-galactosamine, heptose, 2-keto-3-deoxyoctanoate, N-acetylglucosamine, N-acetylgalactosamine, alpha-lactose, and beta-lactose. Complete inhibition of the enzyme-linked immunosorbent assay occurred with D-galactosamine, and partial inhibition was achieved with both alpha-lactose and beta-lactose. Based on these observations, the 3F11 antibody recognizes a site common to gonococcal LPS which is partially shared by meningococcal LPS. The chemical structure of the determinant appears to be a D-galactosamine-O-D-galactopyranosyl-(1-4)-D-glucopyranose. Additional specificity may be conferred by the steric relationship of the determinant on the intact LPS.

Antibodies, Bacterial↗

PubMed1971

Uridinediphosphogalactose-4-epimerase deficiency in Salmonella typhimurium and its correction by plasmoid-borne galactose genes of Escherichia coli K-12: effects on mouse virulence, phagocytosis, and serum sensitivity.

The synthesis of smooth lipopolysaccharide (LPS) in relation to mouse virulence and resistance to serum bactericidal activity in vitro and to rapid intravenous clearance in vivo was studied in Salmonella typhimurium by using a virulent [median lethal dose (LD(50)) = 10(2)], smooth, and genetically marked strain, a uridinediphosphogalactose epimerase-deficient mutant of it which was, therefore, rough, and a derivative of the mutant made smooth again by acquisition of the galactose-positive genes of Escherichia coli. The mutant was of reduced virulence (LD(50) = 10(6)) but the smooth derivative regained the virulence character typical of the parent. The non-smooth phenotype also made the mutant, but not the smooth relatives (parent and derivative), susceptible to serum bactericidal activity and also to rapid intravenous clearance by phagocytosis by the liver. The mutant was similarly treated by germ-free mice (expected to be relatively free of opsonizing antibodies). The clearance of the mutant could be impaired by prior intravenous inoculation of homologous bacteria or their LPS but was reversible by preopsonization of the second inoculum with nonimmune mouse serum, suggesting that the initial inoculum preempted the opsonizing antibodies. Independent evidence of clearance specificity was also provided in mixed inoculum experiments on impaired mice by the rapid clearance of an antigenically unrelated heptose-deficient mutant while maintaining the decelerated clearance of the epimerase mutant. The latter, however, was converted to accelerated clearance by the intravenous inoculation during the impaired state of anti-epimerase mutant immune mouse serum.

Animals↗

PubMed1984

Isolation and characterization of the outer membrane and lipopolysaccharide from Eikenella corrodens.

The chemical composition of the outer membrane fractions (OMFs) of Eikenella corrodens strains 23834 and 470 as well as the strain 23834 lipopolysaccharide (LPS) was determined. The OMFs were obtained by Triton X-100 treatment of the heavier membrane fraction from sucrose density centrifugation of the total membrane fraction. The resulting OMFs of strains 23834 and 470, free of cytoplasmic membrane components, were found to contain 69.6 and 75.0% (wt/wt) protein, 4.8 and 9.2% lipid, 4.6 and 4.7% carbohydrate, and 2.0 and 4.6% muramic acid, respectively. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis both OMFs contained one major peptide determined to be 33,500 daltons for the strain 23834 OMF, and 37,500 daltons for the strain 470 OMF. Analysis of the OMF fatty acids revealed hexadecanoic, hexadecenoic, octadecenoic, and lesser amounts of octadecanoic acids. Transmission electron microscopic examination of the OMFs revealed typical large sheets of membrane. Structures (10 nm in diameter) resembling pores were also evident. The E. corrodens LPS was found to be composed of 34.5% (wt/wt) carbohydrate and 25.0% lipid A. Only minute amounts of 2-keto-3-deoxyoctonate and heptose could be detected. Fatty acid analysis revealed primarily octadecanoic and hexadecanoic acids, with lesser amounts of octadecenoic acid. No hydroxy fatty acids were detected. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed the E. corrodens LPS to resemble other smooth-type LPSs. Transmission electron microscopic examination revealed a vesicle-like morphology. The E. corrodens LPS appears not to be a "classical," i.e., enteric, type of LPS.

Bacterial Outer Membrane Proteins↗

PubMed1985

Biochemical and immunobiological properties of lipopolysaccharide (LPS) from Bacteroides gingivalis and comparison with LPS from Escherichia coli.

Lipopolysaccharides (LPSs) were isolated from Bacteroides gingivalis and Escherichia coli by the phenol-water and butanol-water procedures. The phenol-water-extracted LPS from B. gingivalis 381 was composed of 46% carbohydrate, 23% hexosamine, 18% fatty acid, and 5% protein. The major component sugars of this preparation were glucose, glucosamine, rhamnose, galactose, galactosamine, and mannose, and their molecular ratio was 1:0.9:0.7:0.6:0.6:0.4, respectively. Neither heptose nor 2-keto-3-deoxyoctonate was detected. The butanol-water-extracted LPS from this strain was composed of 76% glucose, 7% fatty acid, and 13% protein, and it was associated with a number of polypeptides (13 to 56 kilodaltons). The main fatty acid of both LPS preparations was palmitic acid. It was found that biological activities of LPS from B. gingivalis were comparable to those of LPS from E. coli in terms of activation of the clotting enzyme of Limulus amebocyte lysate, mitogenicity, polyclonal B cell activation, and stimulation of interleukin 1 production in BALB/c mice. Furthermore, LPS-nonresponsive C3H/HeJ spleen cells were found to yield good mitogenic responses to both phenol-water-extracted LPS and butanol-water-extracted LPS from B. gingivalis or butanol-water-extracted LPS from E. coli. On the other hand, spleen cells from LPS-responsive C3H/HeN mice responded well to all these LPS preparations.

Amino Acids↗

PubMed1985

Monoclonal antibodies to enterobacterial common antigen and to Escherichia coli lipopolysaccharide outer core: demonstration of an antigenic determinant shared by enterobacterial common antigen and E. coli K5 capsular polysaccharide.

We established hybridoma cell lines producing monoclonal antibodies against enterobacterial common antigen (ECA) and a substructure of the outer core of different Escherichia coli lipopolysaccharides (LPSs). Anti-ECA antibodies 865 and 898 reacted with ECA in extracts of heated E. coli and with ECA-bound R1 and R4 core-containing LPS preparations, as well as with a purified sample of ECA from Salmonella montevideo. Antibody 865, but not antibody 898, cross-reacted with K5 capsular polysaccharide, suggesting that 4-linked alpha-N-acetylglucosamine is part of an antigenic determinant shared by both K5 polysaccharide and ECA. Anti-LPS antibody 786 recognized an outer core structure common to E. coli K-12, B, R2, and R4 core type LPS, but not to R1 and R3 core type LPS. Its most probable target is the trisaccharide sequence Hexp(1----2)-alpha-D -Glcp(1----3) alpha-D-Glcp----(Hepp) (where Hex is hexose, p is phosphate, Glc is glucose, and Hep is heptose), the first glucose being the immunodominant moiety. These monoclonal antibodies may be used not only for the detection of ECA, K5, and LPS core structures but also for analysis of the molecular forms resolved on polyacrylamide gels (banding patterns) of both ECA and LPS, independently of one another.

Antibodies, Monoclonal↗

PubMed1985

A 28,000-dalton protein of normal mouse serum binds specifically to the inner core region of bacterial lipopolysaccharide.

Normal mouse serum was found to contain a protein, referred to here as factor, which binds to the inner core region of lipopolysaccharides (LPSs) of various bacterial families. Since factor-LPS interactions resulted in activation of guinea pig complement, factor activity could be assayed by a passive hemolysis test with sheep erythrocytes coated with LPS or lipid A from Acinetobacter calcoaceticus (which was found earlier to bind particularly well to factor). Factor was purified by G-50 and hydroxyapatite chromatography whereby the specific hemolytic activity was enriched 1,675-fold. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions revealed the presence of a 28,000-dalton protein as the main band. The identity of this band was determined by absorption experiments with LPS-coated sheep erythrocytes or latex beads, whereby the 28,000-dalton band disappeared after specific absorption and could be recovered from the absorbent. The binding specificity of factor was determined in a passive hemolysis inhibition assay with defined oligosaccharides representative for the inner core region of LPS. Thus, the di- and trisaccharides alpha-D-mannoheptopyranosyl-(1----5)-2-keto-3-deoxy-D-mannoocto nic acid and alpha-D-mannoheptopyranosyl-(1----3)-alpha-D-mannoheptopyranosy l-(1----5)-2- keto-3-deoxy-D-mannooctonic acid, respectively, were able to inhibit binding of factor to LPS. The results are in accordance with our earlier observation that the heptose-2-keto-3-deoxy-D-mannooctonic acid region represents a common antigen of bacterial LPS. Rabbit hyperimmune serum directed against this common antigen and purified factor was found to exhibit the same specificity for LPS. Factor activity was followed in mice in vivo after injection of LPS; it disappeared completely 15 min after the injection of LPS and reappeared within 1 h.

Animals↗

PubMed1986

Morphological and biochemical comparison of virulent and avirulent isolates of Haemophilus pleuropneumoniae serotype 5.

Capsular structure and biochemical composition varied between two isolates (virulent and avirulent) of Haemophilus pleuropneumoniae serotype 5. The presence of capsule was determined by transmission electron microscopy with glutaraldehyde-osmium, ruthenium red, alcian blue, and phosphotungstic acid staining procedures. The virulent isolate of H. pleuropneumoniae had a distinct, adherent capsule. The avirulent isolate had a fragile, easily removed capsule. Capsular material (CM) and a lipopolysaccharide (LPS) were isolated from each bacterial isolate and were compared biochemically and biologically. CM from both isolates contained carbohydrates, no detectable protein, and no detectable to trace amounts of lipid A. Each LPS contained heptose, hexose, galactose, glucosamine, 2-keto-3-deoxyoctonate, and lipid A. Biological responses to CM and LPS from both isolates were demonstrated in the proclotting enzyme of Limulus polyphemus amebocyte lysate activation and in serological cross-reactions by immunofluorescence and immunodiffusion precipitation. The virulent isolate contained approximately 10 mg of LPS per g more on an original dry weight basis than the avirulent isolate. LPS from the virulent isolate contained approximately 13 times more galactose than LPS from the avirulent isolate. The differences of capsular structure and biochemical composition may contribute to the role of CM in porcine H. pleuropneumoniae infections.

Animals↗

PubMed1986

Biological and chemical characterization of lipopolysaccharide from Selenomonas spp. in human periodontal pockets.

Pure lipopolysaccharide extracted from Selenomonas spp. isolated from human periodontal pockets was composed of 23.7% carbohydrate, 16.5% hexosamine, 1.2% 2-keto-3-deoxyoctonate, 0.7% heptose, 26.0% lipid, 1.8% protein, and 1.3% phosphorus. It was shown to be quite lethal, to have very active pyrogenicity, to give a typical biphasic-fever response, and to produce a positive local Shwartzman reaction.

Animals↗

PubMed1987

Deficiency of peptidoglycan and lipopolysaccharide components in Rickettsia tsutsugamushi.

Analyses of chemical composition in whole cells of Rickettsia tsutsugamushi were performed and compared with those of the other rickettsiae and gram-negative bacteria. The results indicated that R. tsutsugamushi does not contain detectable amounts of 3-deoxy-D-mannooctulosonic acid, heptose, muramic acid, or glucosamine (less than 2, less than 2, less than 3, and less than 3 nmol/mg, respectively). The microorganism was found to contain four kinds of fatty acids (16:0, 18:0, 18:1, and 18:2), but not hydroxy fatty acids. Furthermore, in analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by silver or Coomassie blue staining, lipopolysaccharide bands were not detected in preparations treated with proteinase K. It is concluded that R. tsutsugamushi has little or no peptidoglycan or lipopolysaccharide.

Bacterial Proteins↗

PubMed1988

Purification and characterization of lipooligosaccharides from four strains of "Haemophilus somnus".

Lipooligosaccharides (LOSs) from four strains of "Haemophilus somnus" were purified and their electrophoretic profile, composition, endotoxic activity, and antigenic properties were analyzed. The LOSs were most efficiently purified by enzyme digestion, hot aqueous phenol extraction, and ultracentrifugation. Each LOS could be separated into two to six distinct bands with apparent Mrs of 3280 to 4960, following electrophoresis in polyacrylamide gels. Each LOS contained dodecanoic, tetradecanoic, and 3-hydroxytetradecanoic fatty acids; a high proportion of hexose, 3-deoxy-D-manno-octulosonic acid, and phosphate; and a small amount of heptose; glucosamine was present in both the oligosaccharide and the lipid A. Each "H. somnus" LOS demonstrated endotoxic activity, as determined by gelation of Limulus ameobocyte lysate, the dermal Schwartzman reaction, and mouse lethality. Antiserum to purified "H. somnus" LOS cross-reacted with all strains of "H. somnus" tested by enzyme-linked immunosorbent assay (ELISA), but not to any Enterobacteriaceae, Pseudomonas, or Pasteurella species tested. "H. somnus" LOS was a poor immunogen, but inhibition, dot blot, and sandwich ELISA data indicated that antibodies made to LOS were predominantly, though not exclusively, to lipid A. Monoclonal antibodies directed to "H. somnus" LOS confirmed that lipid A and non-lipid A determinants were present.

Animals↗

PubMed1988

Suppression of murine macrophage interleukin-1 release by the polysaccharide portion of Haemophilus actinomycetemcomitans lipopolysaccharide.

Lipopolysaccharide (LPS) was extracted from whole cells of Haemophilus actinomycetemcomitans Y4 by the hot phenol-water procedure. LPS was cleaved into its lipid A and polysaccharide moieties by hydrolysis in 1% acetic acid. The major component sugars of the polysaccharide were glucose, heptose, rhamnose, galactose, and fucose. LPS and lipid A from H. actinomycetemcomitans induced the release of interleukin-1 (IL-1) by LPS-responsive C3H/HeN murine peritoneal macrophages and cell line macrophages (P388D1 and J744.1), but not by LPS-nonresponsive C3H/HeJ peritoneal macrophages. The polysaccharide was unable to induce the release of IL-1. It suppressed the IL-1 release from LPS- and lipid A-stimulated macrophages, but not the production of cell-associated and intracellular IL-1. The addition of rhamnose, a sugar component of the polysaccharide, abrogated the inhibitory effect of the polysaccharide on IL-1 release. These results suggest the participation of a lectinlike molecule in IL-1 release.

Cell Line↗

PubMed1988

Chemical and biological characterization of the lipopolysaccharide of the oral pathogen Wolinella recta ATCC 33238.

To investigate the potential pathogenic mechanisms of the oral periodontopathogen Wolinella recta ATCC 33238, we have isolated its lipopolysaccharide (LPS) and determined the chemical composition and selected in vitro biological activities of the molecule. Sodium desoxycholate-polyacrylamide gel electrophoresis revealed the W. recta LPS to be an atypical smooth LPS with short O-antigenic side chains. Chemically the LPS consisted of 47.2% lipid A, 19.6% polysaccharide, 9.0% heptose, 8.5% hexosamine, 3.2% phosphate, and 0.6% 2-keto-3-deoxyoctanoate. The major fatty acids were hexadecanoic acid (25.0%), 3-OH tetradecanoic acid (23.8%), tetradecanoic acid (15.4%), 3-OH hexadecanoic acid (11.6%), and octadecenoic acid (10.9%). Rhamnose constituted 87.8% of the carbohydrates generally associated with the O antigen, with smaller amounts of glucose (5.5%), mannose (4.9%), and an unidentified sugar (1.9%). CD-1 and C3H/HeN macrophages (M phi) exposed to 1 microgram of W. recta LPS per ml released 6.0 and 10.5 ng of prostaglandin E per ml of supernatant, representing 625% and 1,306% of prostaglandin E release by the control (without LPS). Maximum prostaglandin E release occurred in CD-1 M phi exposed to 100 micrograms of LPS per ml and was equivalent to 1,542% of release by the control. Interleukin-1 (IL-1) activities in CD-1 and C3H/HeN M phi exposed to 1 micrograms of LPS per ml were 257% and 1,941% of activities in the control, respectively. Maximum IL-1 release in CD-1 M phi occurred in response to 50 micrograms of LPS per ml and represented a 927% increase over release in the control, while 100 micrograms LPS per ml stimulated maximum IL-1 release in C3H/HeN M phi that was greater than 5,000% of release by the control.

Acid Phosphatase↗

PubMed1991

Comparative immunochemistry of lipopolysaccharides from Branhamella catarrhalis strains.

Lipopolysaccharides (LPS) were extracted and purified from the type strain and from a clinical isolate of Branhamella catarrhalis. Chemical analysis revealed the presence of glucose, galactose, and glucosamine in different molar proportions in the LPS from these two isolates, whereas there was no difference between the two isolates in the ratios of ketodeoxyoctonate, phosphate, and the fatty acids C12, 3-OH-C12, and 3-OH-C11 present. Heptose or 3-OH-C14 was not detectable in either preparation. LPS from both strains appeared semirough according to sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis, presenting a core polysaccharide plus one repeating unit. Immunoblotting, passive hemolysis, and hemolysis inhibition assays using anti-LPS antibodies from immunized rabbits demonstrated cross-reactivity between the LPS preparations; however, antigenic dissimilarities were also found, suggesting that more than one serotype may exist. The lipid A isolated from the two LPS was serologically identical and exhibited cross-reactivity with lipid A of members of the family Enterobacteriaceae. The B. catarrhalis LPS were biologically active, causing lethality in D-galactosamine-sensitized C57/BL6 mice and inducing Limulus amoebocyte lysate gelation.

Animals↗