MUCOID PSEUDOMONAS qRUGINOSA IN PATIENTS WITH CHRONIC ILLNESSES

Doggett, R.; Harrison, Gunyon M.; Carter, R.E.

doi:10.1016/s0140-6736(71)90973-1

Cited by 70 publications

(44 citation statements)

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“…4a and b The amorphous layer observed outside E. coli cell surfaces in a study published by Shands (40) was clearly reported as a capsular layer when the cells were grown in in vivo conditions. P. aeruginosa clinical isolates from cystic fibrosis patients often produce alginatelike, mucoid exopolysaccharides (11). This alginate material is not a tight capsule (8) and can be described as a loose slime which is easily sloughed off into the growth medium or the surrounding environment (24).…”

Section: Discussionmentioning

confidence: 99%

Visualization of Pseudomonas aeruginosa O antigens by using a protein A-dextran-colloidal gold conjugate with both immunoglobulin G and immunoglobulin M monoclonal antibodies

Lam¹,

Lam²,

MacDonald³

et al. 1987

J Bacteriol

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Two lipopolysaccharide 0-antigen-specific monoclonal antibodies, MA1-8 (an immunoglobulin Gl [IgGl]) and MF15-4 (an IgM), were used to localize the 0 antigen of the lipopolysaccharide of Pseudomonas aeruginosa PAO1. A protein A-dextran-gold conjugate with an average particle diameter of 12.5 nm was used to label bacterial cells treated-with MA1-8, while a second antibody (goat anti-mouse IgM) was required before the same probe could interact with cells treated with the IgM antibody MF15-4. Both antibodies resulted in exclusive labeling of the surface of P. aeruginosa PAO1 but not that of an isogenic 0-antigen-lacking rough mutant. When the monoclonal antibodies became attached to the cell surface of P. aeruginosa PAO1, resulting in an even coating, the foldings and other topographic details could not be discerned by negative staining. In thin sections of monoclonal-antibody-treated bacteria, a 20-and a 30-to 40-nm thick amorphous layer was observed around the outside of the outer membrane when MA1-8 (IgG) and MF15-4 (IgM) plus goat anti-mouse IgM antibodies were used, respectively. This amorphous layer presumably resulted from the stabilization of the lipopolysaccharide structure by the monoclonal antibodies which prevented the long 0-antigen chains from collapsing owing to dehydration.Bacterial cell surface studies were initiated to generate knowledge of how microorganisms function as well as how they interact with an animal host or with the environment. In the past, much effort has been spent to improve highresolution electron microscopy (20) and the techniques for surface antigen localization. Some of these localization methods for studying microorganisms involve the use of an enzyme and its end-product depositions (1, 28) or the use of polyclonal antibodies conjugated to an electron-dense marker, such as ferritin (28,34,40,41). More recently, monodispersed colloidal gold has emerged as the most versatile marker for cell-labeling studies. The advantages of using colloidal gold versus the use of other markers have been described in detail in several recent reviews (14,21,38). With the development of hybridoma technology by Kohler and Milstein (23), monoclonal antibodies have been rapidly replacing polyclonal antibodies as the immunological reagent in in situ antigen detection studies because of their qualities of specificity, availability, and reproducibility.Lipopolysaccharide (LPS) plays an important role as a structural component of the cell walls of gram-negative bacteria. This macromolecule has also been implicated as a potential virulence factor of some organisms (9). In the past two decades, many LPS localization studies involving Escherichia coli and Salmonella typhimurium have been reported (3,(32)(33)(34)40). Although data from these studies provided information on the distribution of LPS in the outer membrane, the architectural relationship between the LPS molecules and the cell surface has not been thoroughly examined. We produced monoclonal antibodies of both immunoglobulin G (IgG) and IgM isotype...

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Section: Discussionmentioning

confidence: 99%

Visualization of Pseudomonas aeruginosa O antigens by using a protein A-dextran-colloidal gold conjugate with both immunoglobulin G and immunoglobulin M monoclonal antibodies

Lam¹,

Lam²,

MacDonald³

et al. 1987

J Bacteriol

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“…This phenotype often occurs coincidently with the establishment of chronic infection and becomes stabilized by regulatory mutations as described earlier. The mucoid form of P. aeruginosa is associated with 90% of P. aeruginosa CF infections compared to only 2% of P. aeruginosa non-CF infections (Doggett, 1969;Doggett, Harrison, & Carter, 1971). This phenotype is often coordinately regulated with a loss of flagella by the alternative sigma factor AlgT (Tart, Wolfgang, & Wozniak, 2005).…”

Section: Adaptation Occurring During Chronic Infectionmentioning

confidence: 99%

Pseudomonas aeruginosa – Pathogenesis and Pathogenic Mechanisms

Alhazmi

2015

IJB

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Pseudomonas aeruginosa is a common bacterium, Gram-negative opportunistic pathogen capable of infecting humans with compromised natural defenses and causing severe pulmonary disease. It is one of the leading pathogen associated with nosocomial infections. It has a vast arsenal of pathogenicity factors that are used to interfere with host defenses. Pathogenesis in P. aeruginosa facilitates adhesion, modulate or disrupt host cell pathways, and target the extracellular matrix. The propensity of P. aeruginosa to form biofilms further protects it from antibiotics and the host immune system. P. aeruginosa is intrinsically resistant to a large number of antibiotics and can be acquired resistance to many others, making treatment difficult. P. aeruginosa provokes a potent inflammatory response during the infectious process. The majority of mortalities in immunocompromised patients; cystic fibrosis, can be attributed to the progressive decline of lung function resulting from chronic infection by pathogens such as P. aeruginosa. Antibiotic treatment of chronic P. aeruginosa infections may temporarily suppress symptoms; however, they do not eradicate the pathogen. Lung diseases caused by P. aeruginosa are a leading cause of death in immunocompromised individuals as well as in children. Although immunocytes recruitment is critical to augment the host defense, excessive neutrophil accumulation results in life-threatening diseases, such as acute lung injury, as well as acute respiratory distress syndrome. Several virulence factors have been studied for their roles as potential vaccine candidate, although there is currently no clinically accepted vaccine. Understanding host-pathogen interaction is critical for the development of effective therapeutic strategies to control the damage in the lung.

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“…Alginate is an exopolysaccharide produced by P. aeruginosa strains which cause persistent pulmonary infections in patients with cystic fibrosis (9,11). The majority of P. aeruginosa strains isolated from cystic fibrosis patients have a mucoid colony morphology due to the production of alginate, whereas nonmucoid strains of P. aeruginosa are generally isolated from patients with other types of infections (4). Alginate-producing (Alg+) strains of P. aeruginosa produce lower levels of extracellular proteolytic activity than isogenic nonmucoid strains (15).…”

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confidence: 99%

“…Alginate-producing (Alg+) strains of P. aeruginosa produce lower levels of extracellular proteolytic activity than isogenic nonmucoid strains (15). The initial colonization of the respiratory tract of cystic fibrosis patients is believed to occur with typical Alg-strains which eventually convert to the Alg+ form in vivo (4). Protease production may be important for the initial colonization of the respiratory tract of cystic fibrosis patients (8).…”

mentioning

confidence: 99%

Cloning and transcriptional regulation of the elastase lasA gene in mucoid and nonmucoid Pseudomonas aeruginosa

Goldberg¹,

Ohman²

1987

J Bacteriol

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The lasA gene (whose product is involved in the production of extracellular elastolytic activity) was isolated from a genomic bank containing DNA from Pseudomonas aeruginosa FRD1. Recombinant plasmid pELAl, containing the lasA gene, complemented the temperature-sensitive elastase mutation (lasAl) in P. aeruginosa PAO-E64. The kaA gene was physically mapped on plasmid pELAl by deletion analysis and transposon mutagenesis. The direction of transcription of lasA was determined with a promoterless chloramphenicol acetyltransferase cartridge. The lasA-chloramphenicol acetyltransferase plasmid was transferred to isogenic mucoid and nonmucoid strains of P. aeruginosa FRD; the transcription of laA-chloramphenicol acetyltransferase was slightly higher in the nonmucoid strain.

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MUCOID PSEUDOMONAS qRUGINOSA IN PATIENTS WITH CHRONIC ILLNESSES

Cited by 70 publications

References 0 publications

Visualization of Pseudomonas aeruginosa O antigens by using a protein A-dextran-colloidal gold conjugate with both immunoglobulin G and immunoglobulin M monoclonal antibodies

Visualization of Pseudomonas aeruginosa O antigens by using a protein A-dextran-colloidal gold conjugate with both immunoglobulin G and immunoglobulin M monoclonal antibodies

Pseudomonas aeruginosa – Pathogenesis and Pathogenic Mechanisms

Cloning and transcriptional regulation of the elastase lasA gene in mucoid and nonmucoid Pseudomonas aeruginosa

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