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PubMed1998

Combined fluorescent in situ hybridisation and immunolabelling of Bacteroides fragilis.

We have demonstrated that pure cultures of Bacteroides fragilis can be riboprobed with the oligoprobes BAC303 and EUB338, whilst simultaneously immunolabelled with either the mAb QUBF7, or polyclonal antiserum specific for a common antigen of B. fragilis. We were also able to distinguish between pure cultures of B. fragilis and Escherichia coli, by means of combined immunolabelling and riboprobing. The success of the combined technique is critically dependent on the size of the bacterial capsules, bacterial growth phase, antibody diluent and the length of the washing steps. The combined FISH and immunolabelling of bacteria has potential applications in studies of bacteria of medical and veterinary importance, as well as bacteria from other environments, as it yields information about both the identity and antigen expression of individual bacterial cells.

Antibodies, Bacterial↗
PubMed2004

Capsule polysaccharide mediates bacterial resistance to antimicrobial peptides.

The innate immune system plays a critical role in the defense of areas exposed to microorganisms. There is an increasing body of evidence indicating that antimicrobial peptides and proteins (APs) are one of the most important weapons of this system and that they make up the protective front for the respiratory tract. On the other hand, it is known that pathogenic organisms have developed countermeasures to resist these agents such as reducing the net negative charge of the bacterial membranes. Here we report the characterization of a novel mechanism of resistance to APs that is dependent on the bacterial capsule polysaccharide (CPS). Klebsiella pneumoniae CPS mutant was more sensitive than the wild type to human neutrophil defensin 1, beta-defensin 1, lactoferrin, protamine sulfate, and polymyxin B. K. pneumoniae lipopolysaccharide O antigen did not play an important role in AP resistance, and CPS was the only factor conferring protection against polymyxin B in strains lacking O antigen. In addition, we found a significant correlation between the amount of CPS expressed by a given strain and the resistance to polymyxin B. We also showed that K. pneumoniae CPS mutant bound more polymyxin B than the wild-type strain with a concomitant increased in the self-promoted pathway. Taken together, our results suggest that CPS protects bacteria by limiting the interaction of APs with the surface. Finally, we report that K. pneumoniae increased the amount of CPS and upregulated cps transcription when grown in the presence of polymyxin B and lactoferrin.

Antimicrobial Cationic Peptides↗
PubMed1999

Surface antigen exposure by bismuth dimercaprol suppression of Klebsiella pneumoniae capsular polysaccharide.

The bacterial capsule is an important virulence determinant in animal and plant disease. Bacterial capsule and slime can be inhibited by bismuth compounds, especially when complexed with lipophilic thiol chelators. Bismuth dimercaprol (BisBAL) at 1 ppm of Bi3+ repressed Klebsiella pneumoniae capsule expression in defined medium by nearly 90%, which exposed subsurface structures. The phagocytic index for BisBAL-treated bacteria increased from <10 to 360 bacteria per 100 neutrophils in the presence of complement and anticapsular or anti-O antigen antiserum. BisBAL treatment also enhanced the reactivity of monoclonal antibodies (MAbs) specific for the O1-antigen lipopolysaccharide (LPS) or the LPS core in a dose-dependent manner as indicated by the results of enzyme-linked immunosorbent assays. When anti-O1 MAb was used, the reactivity increased significantly for fully encapsulated O1:K1 or O1:K2 cells but not for O1:K- cells. Deposition of C3b also increased significantly for BisBAL-treated O1:K1 or O1:K2 cells but not for O1:K- cells. Survival of a serum-sensitive strain was <0.1% when nonimmune human serum absorbed with O1:K1 cells was used and 107% when BisBAL-treated cells were used for absorption. Outer membrane proteins were also more accessible on the surface of K. pneumoniae after BisBAL treatment. Thus, at subinhibitory levels, BisBAL inhibited capsule expression, which promoted phagocytosis, enhanced the reactivity of specific antibodies for LPS O antigen, LPS core epitopes, or outer-membrane proteins, and enhanced complement interaction with encapsulated K. pneumoniae. By unmasking bacterial surface structures and enhancing the immune system reactivity to bacteria, bismuth thiols may prove useful as adjuncts for vaccination.

Animals↗
PubMed1993

Higher-titer antisera from patients with periodontal disease inhibit bacterial capsule-induced bone breakdown.

Solubilized surface-associated material (SAM) from a number of periodontopathogenic bacteria have been shown to be potent stimulators of bone resorption in vitro in the murine calvarial bone culture assay. Antibodies to the constituents of SAM are also found in patients with periodontal diseases. Serum from patients with severe generalized periodontitis (SGP) containing high titers of antibodies to the SAM of Porphyromonas gingivalis completely inhibited the bone resorption induced by SAM from this organism. In contrast, serum from patients with low titers of antibodies to SAM from P. gingivalis failed to inhibit bone resorption. High-titer sera (containing antibodies to SAM from Actinobacillus actinomycetemcomitans) from patients with localized juvenile periodontitis (LJP) were added to calvarial cultures stimulated with SAM from A. actinomycetemcomitans. Of 6 high-titer sera tested, only 4 inhibited bone breakdown, the other 2 sera having no effect on resorption. Low-titer sera were also ineffective at blocking bone resorption. This suggests that the antibody response to SAM may have a protective effect in patients with periodontal disease.

Aggregatibacter actinomycetemcomitans↗
PubMed1990

Visualization of the bacterial polysaccharide capsule.

The highly hydrated capsule of E. coli strains is composed of a large number of polysaccharide fibers of which the thinnest measure about 2 nm in width. The fibers may span the entire distance from the outer membrane to the outer rim of the capsule and show a propensity to associate with each other to form thicker filaments. Presence of thick filaments may also indicate a partial collapse of the capsular organization due to removal of water. The in vivo capsule represents a relatively open structure with the negatively charged polysaccharide fibers permitting the binding of large quantities of water and ions, and providing intracellular space for diffusing molecules to access the envelope membranes even in conditions of high cell density. Negative charge and steric hindrance of the polysaccharide strands protect the cells against attack by a large variety of harmful macromolecules and against infection by most bacteriophages. Two types of procedure have been most successful in maintaining the size and overall structure of the capsule: (a) the interaction of cationic molecules with the in vivo capsule, and (b) the use of antibody to stabilize capsules for subsequent dehydration and plastic embedding. A further type of potentially useful procedure, cryofixation and cryosubstitution, has shown interesting results in a number of cases. These techniques are expected to play a significant role in structural studies in the near future. The sites of export of capsular antigen have been described in earlier conventional electron microscopic studies. Data obtained from the recent technique of "on-section" labeling support the model that both the capsular antigen and the O antigen are assembled at junctions of the inner and outer membrane. It is anticipated that one will be able to discern in greater ultrastructural detail the membranes at which the antigen is translocated. Novel membrane fixation and isolation techniques will have to be established and employed in a combination of sensitive microscopic techniques and immuno- and enzyme localization methods. These developments will make it possible to explore questions pertaining to the maintenance and structural organization of microbial capsules and the functional interaction of polysaccharides with natural surfaces, man-made substances and drugs.

Antigens, Bacterial↗
PubMed1989

Bacterial polysaccharide capsule synthesis, export and evolution of structural diversity.

Elaboration of a capsule composed of one of a range of acidic polysaccharides is a common feature of many bacteria, particularly those capable of causing serious infections in humans. Biochemical and genetical analyses of capsule biogenesis in Escherichia coli are beginning to reveal new aspects of polysaccharide biosynthesis. Genes have been identified which are thought to encode products responsible for the translocation of these high molecular-weight polysaccharides across the cytoplasmic and outer membranes, and the organization of exported polysaccharide into a capsule. Their further analysis should provide new insights into membrane biology, particularly since the genes in question are absent from the often used laboratory strains of E. coli. Genetic analysis of capsule diversity is beginning to suggest possible mechanisms for the generation of the structural diversity of polysaccharides.

Antigens, Bacterial↗
PubMed2001

Vaccines against meningococcal disease: current and future technologies.

Development of the meningococcal serogroup C conjugate vaccine and its national implementation in the UK has been a major breakthrough in the prevention of meningococcal disease. New technologies are increasing the likelihood that research towards a vaccine against group B meningococcus will be successful. This review covers the recent development of vaccines against meningococcal disease and examines future vaccine candidates. The development of meningococcal polysaccharide vaccines was based on the virulence of the bacterial capsule components. The immunogenicity of these vaccines has been improved by covalent linkage to proteins in the new meningococcal C conjugate vaccines. However, the most promising developments for serogroup B disease have stemmed from other virulence determinants such as outer membrane proteins (OMPs) and lipopolysaccharides (LPS). New genome sequencing technology promises a way forward to developing a broadly cross-protective vaccine for this important pathogen.

Adolescent↗
PubMed1992

Capsules of Escherichia coli, expression and biological significance.

Escherichia coli may cause intestinal or extraintestinal infections. Generally, extraintestinal E. coli are encapsulated. The capsules are important virulence determinants, which enable the pathogenic bacteria to evade or counteract the unspecific host defense during the early (preimmune) phase of infection. They interfere with the action of complement and phagocytes. This effect is generally transient and overcome by capsule-specific antibodies in the immune phase of the host defense. In some cases, capsules are not or only poorly immunogenic, as a result of structural relationship or identity with host material. Strains with such capsules (e.g., K1 or K5) are very virulent. Bacterial capsules consist of acidic polysaccharides, which are made up from oligosaccharide repeating units. The capsules of E. coli are divided into two groups, which differ in chemistry, biochemistry, and genetic organization. All capsular polysaccharides are chromosomally determined: those of group I close to his and those of group II close to serA. The biosynthesis and surface expression have been extensively studied with representatives of group II capsular polysaccharides. It could be shown that their biosynthesis is directed from a gene block that determines the synthesis of the polysaccharide, its translocation across the cytoplasmic membrane, as well as its surface expression in a coordinate process. The chemical nature of group II capsular polysaccharides, as well as the mechanism(s) of their biosynthesis and expression, is presented.

Animals↗
PubMed2003

Supramolecular organization in streptococcal pericellular capsules is based on hyaluronan tertiary structures.

Supramolecular organization involving a polyanionic glycan in a bacterial capsule (hyaluronan, HA, in streptococcal capsules) is revealed, for the first time, by electron-histochemical methodology previously used to elucidate ultrastructure in extracellular matrix. Capsular HA filaments thereby revealed closely resemble aligned linear structures demonstrated by similar technology in HA solution. These parallel arrays, spontaneously formed, are based on HA tertiary structures (beta sheet-like) which are stabilized by hydrophobic and hydrogen bonds. HA tertiary structures in aqueous solutions resist shear stress as shown by rheo-NMR. Thus, supramolecular HA wrapping covering many cells probably stabilizes chains of bacteria. Streptococci possibly templated the ordered structures since eukaryotic B6 cell HA did not produce similarly organized envelopes. Supramolecular organization in streptococcal and pneumococcal capsules are compared. Their glycans are very similar but the potential for HA-like tertiary structures is not present in the pneumococcal type 3 polysaccharide and chains of cells are not formed to the same extent by pneumococci. We suggest that the streptococcal capsule exemplifies a simple extracellular matrix analogous to those in animal connective tissues, which contain glycans (chondroitin, keratan, and dermochondan sulfates) of the HA family, capable of undergoing aggregation to similar tertiary structures.

Bacterial Capsules↗
PubMedDate not supplied

Polysaccharide antigens of Escherichia coli.

The major surface antigens of Escherichia coli are the cell wall lipopolysaccharides (LPS; O antigens) and the capsular polysaccharides (PS; K antigens). These polysaccharides are synthesized at the cytoplasmic membrane of the bacteria; the LPS are transported to the outer membrane, where they reside, whereas the PS are secreted into capsules. The LPS consist of lipid A covalently linked to the core oligosaccharide, which itself is covalently linked to the O-specific polysaccharide. The latter, which determines the O specificity of the bacteria may be neutral or contain negative charges (carboxyl groups or phosphate). The relatedness of E. coli to other genera (e.g., Klebsiella or Shigella) frequently is borne out by structural identity. This intergeneric relation is paralleled by similar pathogenic properties of the bacteria in question. The capsular antigens of E. coli are acidic polysaccharides, which can be divided into groups (I and II) on the basis of molecular size, nature of the acidic component, coexpression with O antigens, and temperature regulation of their biosynthesis. The major acidic components are hexuronic acid (mainly of Klebsiella-like group I) as well as 2-keto-3-deoxy-D-mannooctulonic acid, N-acetylneuraminic acid, or phosphate (mainly in Neisseria- and Haemophilus-like group II). Relatedness of encapsulated E. coli to encapsulated bacteria of other genera (Neisseria, Haemophilus, Klebsiella) is based on structural identity or similarity of the respective capsules. Identity not only refers to structure and serology of these capsules but also to the pathogenicity of the respective bacteria (e.g., E. coli K1 and Neisseria meningitidis b). Bacterial pathogenicity may be caused by the host's inability to raise an immune response to bacterial capsules (E. coli K1 and K5) because of the identity of the capsular polysaccharides and the host carbohydrates. This can be described as camouflage used by the bacteria as a strategem for bacterial virulence.

Antigens, Bacterial↗
PubMed2003

A 39 kDa protein mediates adhesion of avian Pasteurella multocida to chicken embryo fibroblast cells.

To clarify the role of avian Pasteurella multocida capsule in pathogenesis, adhesion of capsulated strains P-1059, X-73 and Pm-18, and noncapsulated strains P-1059B, Pm-1 and Pm-3 to chicken embryo fibroblast (CEF) cells was compared. Number of adherent organisms of the capsulated strains to CEF cells were approximately three times as much as noncapsulated strains indicating that adhesive properties were enhanced by the presence of bacterial capsule. Pretreatments of the bacterial cells with heat, trypsin, or with antiserum caused a marked decrease in adhesion of capsulated strain P-1059 and its noncapsulated variant P-1059B. However, depolymerization of capsular hyaluronic acid with high dose of hyaluronidase enhanced adhesion of these strains. Combined treatments of the bacterial cells with both hyaluronidase and trypsin significantly (P < 0.05) inhibited the adherence of strain P-1059 as compared to the treatment only with trypsin, but strain P-1059B was not affected. SDS-PAGE profiles of crude capsular extract (CCE) prepared from capsulated strain P-1059 and its noncapsulated variant P-1059B grown on dextrose starch agar (DSA) plates by heating at 56 degrees C in a 2.5% NaCl solution demonstrated eight protein bands of 28, 34, 36, 39, 52, 56, 63 and 93 kDa. The 28, 34 and 36 kDa proteins were commonly major for both strains, and the 39 kDa protein was major only for strain P-1059 but poor in strain P-1059B. Outer membrane protein (OMP) profiles were identical with a major protein at 34 kDa and four minor proteins between the two strains. The adhesion of strain P-1059 and strain P-1059B to CEF cells was inhibited significantly (P < 0.01) by treatment with rabbit antisera against P-1059, P-1059B, CCE or 39 kDa protein of strain P-1059 as compared to the treatment with either PBS or with normal rabbit serum. These results indicated that an antigenic 39 kDa protein in the capsule may be responsible for adhesion of avian P. multocida type A strains to CEF cells as a virulence factor.

Animals↗
PubMed2003

The effects of Escherichia coli capsule, O-antigen, host neutrophils, and complement in a rat model of Gram-negative pneumonia.

Gram-negative enteric bacilli are agents of life-threatening pneumonia. The role of the bacterial capsule and O-antigen moiety of lipopolysaccharide in the pathogenesis of Gram-negative pneumonia was assessed. In a rat model of pneumonia the LD(50) of a wild-type extraintestinal pathogenic Escherichia coli strain (CP9) was significantly less than its isogenic derivatives deficient in capsule (CP9.137), O-antigen (CP921) or both capsule and O-antigen (CP923) (P< or =0.003). Studies using complement depleted or neutropenic animals established that both neutrophils and complement are important for the pulmonary clearance of E. coli. Data from these studies also support that capsule and O-antigen serve, at least in part, to counter the complement and neutrophil components of the pulmonary host defense response. Lastly, the contribution of E. coli versus neutrophils in causing lung injury was examined. Findings suggest that E. coli virulence factors and/or non-neutrophil host factors are more important mediators of lung injury than neutrophils. These findings extend our understanding of Gram-negative pneumonia and have treatment implications.

Animals↗