Complement resistance in Branhamella (Moraxella) catarrhalis

Hol, Cees; Verduin, C. M.; Dijke, EtienneVan; Verhoef, J.; Dijk, HansVan

doi:10.1016/0140-6736(93)91185-o

Cited by 29 publications

(23 citation statements)

References 8 publications

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“…Recently, Verduin et al have reported that 89% of M. catarrhalis strains isolated from adults with lower respiratory disease are completely or partially resistant to the bactericidal action of serum (54). In contrast, it has been reported that 58% of M. catarrhalis isolates carried in the pharynges of asymptomatic, healthy children are serum sensitive and do not appear to cause disease (23,24,54).…”

Section: Discussionmentioning

confidence: 95%

“…Multiple studies have demonstrated that resistance to complement-mediated killing is an important virulence factor for M. catarrhalis infections. Hol et al reported in two studies that 156 of 179 (87%) and 124 of 200 (62%) clinical isolates from adult patients with pulmonary infections were serum resistant (23,24). Recently, Verduin et al have reported that 89% of M. catarrhalis strains isolated from adults with lower respiratory disease are completely or partially resistant to the bactericidal action of serum (54).…”

Section: Discussionmentioning

confidence: 99%

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Lipooligosaccharide P ^k (Galα1-4Galβ1-4Glc) Epitope of Moraxella catarrhalis Is a Factor in Resistance to Bactericidal Activity Mediated by Normal Human Serum

Zaleski¹,

Scheffler

Densen

et al. 2000

Infect Immun

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Moraxella catarrhalis is a respiratory pathogen responsible for acute bacterial otitis media in children and exacerbation of chronic bronchitis in adults. M. catarrhalis strains are frequently resistant to the bactericidal activity of normal human serum. In order to determine if the lipooligosaccharide (LOS) of M. catarrhalis has a role in serum resistance, the UDP-glucose-4-epimerase (galE) gene was identified, cloned, and sequenced and a deletion/insertion mutation was introduced into M. catarrhalis strain 2951. GalE enzymatic activity, measured in whole-cell lysates, was ablated in M. catarrhalis 2951 galE. Mass spectrometric analysis of LOS isolated with hot phenol-water confirmed that strain 2951 produced a type A LOS. These studies showed that the LOS from 2951 galE had lost two hexose residues due to the galE mutation and that the resultant LOS structure lacked the (Gal␣1-4Gal␤1-4Glc) P k epitope found on M. catarrhalis 2951. Wild-type M. catarrhalis 2951 is resistant to complement-mediated serum bactericidal activity. In contrast, a greater than 2-log 10 -unit reduction in CFU occurred after incubation of 2951 galE in either 50 or 25% pooled human serum (PNHS), and CFU in 10% PNHS decreased by about 1 log 10 unit. These studies suggest that the P k epitope of the LOS may be an important factor in the resistance of M. catarrhalis to the complement-mediated bactericidal effect of normal human serum.Moraxella catarrhalis is a human respiratory pathogen that is currently the third leading cause of otitis media along with Streptococcus pneumoniae and Haemophilus influenzae (10). Studies from various centers in the United States, Europe, and Asia used tympanocentesis to demonstrate that 15 to 20% of the middle-ear infections occurring in young children were caused by M. catarrhalis (10,15,16,18,46). M. catarrhalis has also been implicated as an important cause of respiratory disease in adults with predisposing conditions (41). Studies from several centers have reported clusters of nosocomial outbreaks of M. catarrhalis, most of which occurred in pulmonary care units (43,45). Although multiple studies have described specific bacterial components considered potential virulence factors, the steps involved in the pathogenesis of M. catarrhalis colonization and infection remain elusive (28, 41). One feature of this organism which has stimulated the interest of a number of investigators is its resistance to killing by normal human serum. Recent studies have focused on components of the bacterial outer membrane, as these structures would most likely be available for interaction with the host immune response. One prominent bacterial surface component, implicated as a potential virulence factor, is the lipooligosaccharide (LOS).The LOS is similar to those of other airway pathogens such as H. influenzae, Neisseria meningitidis, and Bordetella pertussis in lacking O antigens typical of the enteric gram-negative bacilli. There are three M. catarrhalis serotypes (A, B, and C) based on chemically defined differences in the ...

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Section: Discussionmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

Lipooligosaccharide P ^k (Galα1-4Galβ1-4Glc) Epitope of Moraxella catarrhalis Is a Factor in Resistance to Bactericidal Activity Mediated by Normal Human Serum

Zaleski¹,

Scheffler

Densen

et al. 2000

Infect Immun

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“…For example, it can block the antibiotic treatment of concomitant infections with more dangerous pathogens (e.g., pneumococci), as experimentally confirmed by Hol et al (14)(15)(16). This, together with the discovery of M. catarrhalis as a pathogen in its own right, has aroused scientific interest in other possible virulence factors.…”

mentioning

confidence: 87%

Production of BRO β-Lactamases and Resistance to Complement in European Moraxella catarrhalis Isolates

et al. 2002

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Of the 419 Moraxella catarrhalis isolates collected during the 1997-1999 European SENTRY surveillance study, 385 (92%) were ␤-lactamase positive. Twenty-two (5.7%) produced BRO-2 ␤-lactamase. Twenty-one new mutations were found in the putative promoter region of the bro genes. Nineteen percent of all isolates tested were complement sensitive. Resistance to ␤-lactams is not linked to the phylogenetic lineages associated with susceptibility to complement.Moraxella catarrhalis was long considered a harmless commensal of the respiratory tract and uniformly susceptible to penicillins. In recent years, however, its pathogenic potential has come to light (9,20,27). The production of a new ␤-lactamase enzyme, designated BRO (from Branhamella and Moraxella), by this bacterium was an event that occurred virtually simultaneously around the world (9,13,19,20). Two distinct BRO ␤-lactamase enzymes, namely, BRO-1 and BRO-2, have since been found in strains of M. catarrhalis. These enzymes are identical in substrate and inhibition profile but differ by a single amino acid (2-5). The increased level of resistance conferred by BRO-1 compared to BRO-2 appears to be related to the relative amount of each enzyme produced by the strains (5). This difference in production may be the result of differences in the promoter strength of the two genes. Bootsma et al. (5) reported a 21-bp deletion in the promoter region of the ␤-lactamase gene from a BRO-2-producing strain. In addition, Richter et al. (22) suggested that additional mutations or deletions or insertions in the promoter sequence might explain the variations seen in antibiotic susceptibilities within the populations of BRO-1-and BRO-2-producing M. catarrhalis isolates.The first goal of this study, therefore, was to characterize the BRO ␤-lactamases and their putative promoter regions in the European M. catarrhalis isolates collected between 1997 and 1999 during the European SENTRY surveillance study. The relative percentages of the two enzyme types were also determined.Besides protecting the bacteria against ␤-lactam antibiotics, ␤-lactamase can also have indirect pathogenic effects. For example, it can block the antibiotic treatment of concomitant infections with more dangerous pathogens (e.g., pneumococci), as experimentally confirmed by . This, together with the discovery of M. catarrhalis as a pathogen in its own right, has aroused scientific interest in other possible virulence factors. One of these virulence factors is the ability of M. catarrhalis to resist the action of complement (9,12,17,20,(24)(25)(26). Based on molecular typing data, i.e., pulsed-field gel electrophoresis and PCR-restriction fragment length polymorphism analysis, it has been suggested that complement-resistant M. catarrhalis isolates form a genetically distinct lineage with a different pathogenic potential within the species (3,26,28). The second aim of this study, therefore, was to determine the percentage of complement-resistant M. catarrhalis isolates in the recent SENTRY surveillance study and t...

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“…Strains which are recovered from patients with infections are more resistant to serum killing than are strains recovered from colonized individuals (87,94). Therefore, serum resistance may be a virulence factor for the bacterium.…”

Section: Systemic Antibody Responsementioning

confidence: 99%

“…Strains of B. catarrhalis vary in their susceptibility to killing by serum (87,94,156,173). Strains which are recovered from patients with infections are more resistant to serum killing than are strains recovered from colonized individuals (87,94).…”

Section: Systemic Antibody Responsementioning

confidence: 99%

Lower respiratory tract infection

Sharland¹

2016

OSH Manual of Childhood Infections

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Complement resistance in Branhamella (Moraxella) catarrhalis

Cited by 29 publications

References 8 publications

Lipooligosaccharide P ^k (Galα1-4Galβ1-4Glc) Epitope of Moraxella catarrhalis Is a Factor in Resistance to Bactericidal Activity Mediated by Normal Human Serum

Lipooligosaccharide P ^k (Galα1-4Galβ1-4Glc) Epitope of Moraxella catarrhalis Is a Factor in Resistance to Bactericidal Activity Mediated by Normal Human Serum

Production of BRO β-Lactamases and Resistance to Complement in European Moraxella catarrhalis Isolates

Lower respiratory tract infection

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Complement resistance in Branhamella (Moraxella) catarrhalis

Cited by 29 publications

References 8 publications

Lipooligosaccharide P k (Galα1-4Galβ1-4Glc) Epitope of Moraxella catarrhalis Is a Factor in Resistance to Bactericidal Activity Mediated by Normal Human Serum

Lipooligosaccharide P k (Galα1-4Galβ1-4Glc) Epitope of Moraxella catarrhalis Is a Factor in Resistance to Bactericidal Activity Mediated by Normal Human Serum

Production of BRO β-Lactamases and Resistance to Complement in European Moraxella catarrhalis Isolates

Lower respiratory tract infection

Contact Info

Product

Resources

About

Lipooligosaccharide P ^k (Galα1-4Galβ1-4Glc) Epitope of Moraxella catarrhalis Is a Factor in Resistance to Bactericidal Activity Mediated by Normal Human Serum

Lipooligosaccharide P ^k (Galα1-4Galβ1-4Glc) Epitope of Moraxella catarrhalis Is a Factor in Resistance to Bactericidal Activity Mediated by Normal Human Serum