Economic Impact of Pertussis

Pichichero, Michael E.; Treanor, John J.

doi:10.1001/archpedi.1997.02170380039006

Cited by 49 publications

(18 citation statements)

References 26 publications

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“…Most patients will be treated as outpatients and will use other health care services, such as office and emergency department visits, and antibiotics. Neither those costs nor indirect costs have been considered in this analysis; however, a study examining pertussis cases in one New York county over a six year period from 1989–1994 [38] reporting inpatient and outpatient care costs noted that the cost of hospitalization represented one of the two largest contributing costs associated with pertussis. Furthermore, this study and another [39] by the same author, also examined indirect costs related to pertussis and found that work-related (e.g., lost work days, decrease in productivity) costs were responsible for more than 60% of the overall cost of pertussis when both direct and indirect costs were considered.…”

Section: Discussionmentioning

confidence: 99%

Hospitalization for pertussis: profiles and case costs by age

O’Brien¹,

Jaime

2005

BMC Infect Dis

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Section: Discussionmentioning

confidence: 99%

Hospitalization for pertussis: profiles and case costs by age

O’Brien¹,

Jaime

2005

BMC Infect Dis

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“…Bordetella pertussis and Bordetella parapertussis cause whooping cough in humans (23)(24)(25)(26)(27), and B. parapertussis is also found in ovine species (28 -30). Bordetella bronchiseptica infects many mammals and is commonly associated with atrophic rhinitis in pigs, snuffles in rabbits, and kennel cough in dogs (31)(32)(33)(34).…”

Section: Lipopolysaccharide (Lps)mentioning

confidence: 99%

Relaxed Acyl Chain Specificity of Bordetella UDP-N-acetylglucosamine Acyltransferases

Sweet¹,

Preston²,

Toland³

et al. 2002

Journal of Biological Chemistry

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Lipid A (endotoxin) is a major structural component of Gram-negative outer membranes. It also serves as the hydrophobic anchor of lipopolysaccharide and is a potent activator of the innate immune response. Lipid A molecules from the genus Bordetella are reported to exhibit unusual structural asymmetry with respect to the acyl chains at the 3-and 3-positions. These acyl chains are attached by UDP-N-acetylglucosamine acyltransferase (LpxA). To determine the origin of the acyl variability, the single lpxA ortholog present in each of the genomes of Bordetella bronchiseptica (lpxA Br ), Bordetella parapertussis (lpxA Pa ), and Bordetella pertussis (lpxA Pe ) was cloned and expressed in Escherichia coli. In contrast to all LpxA proteins studied to date, LpxA Br and LpxA Pe display relaxed acyl chain length specificity in vitro, utilizing C 10 OH-ACP, C 12 OH-ACP, and C 14 OH-ACP at similar rates. Furthermore, hybrid lipid A molecules synthesized at 42°C by an E. coli lpxA mutant complemented with lpxA Pe contain C 10 OH, C 12 OH, and C 14 OH at both the 3-and 3-positions, as determined by matrix-assisted laser desorption/ionization time-offlight mass spectrometry. In contrast, LpxA from B. parapertussis did not display relaxed specificity but was selective for C 10 OH-ACP. This study provides an enzymatic explanation for some of the unusual acyl chain variations found in Bordetella lipid A. Lipopolysaccharide (LPS)1 is the major glycolipid molecule present on the cell surface of Gram-negative bacteria. Early understanding of LPS has come from studies in the Enterobacteriaceae (1, 2). In these organisms the molecule consists of the following three domains: the lipid A, the core oligosaccharide, and the O-antigen polysaccharide. Lipid A, the hydrophobic anchor of LPS, is generally an acylated and phosphorylated disaccharide of glucosamine (reviewed by Rick and Raetz (3)). The structure, biosynthesis, and biological properties of LPS have been extensively studied in a wide variety of systems, although the molecule is best understood in Escherichia coli (reviewed by Raetz (4)). The minimal LPS structure required for full viability of E. coli under laboratory conditions is lipid A bearing two 2-keto-3-deoxy-D-manno-octulosonic acid (Kdo) residues (Fig. 1). In addition, Kdo 2 -lipid A, or Re endotoxin, is a fully active agonist of the TLR-4 receptor-mediated inflammatory response (5-7).The first step in Kdo 2 -lipid A biosynthesis in E. coli (Fig. 1) is the transfer of an acyl chain to the glucosamine 3-position of UDP-N-acetylglucosamine (UDP-GlcNAc). This acylation is performed by UDP-GlcNAc acyltransferase, encoded by the gene lpxA (8, 9). This acylated UDP-GlcNAc is then de-acetylated at the 2-position by LpxC (10) before another primary hydroxyacyl chain is added at this position by LpxD (11). Next UMP is removed from a portion of the UDP-2,3-diacylglucosamine pool by LpxH (12), before the tetra-acylated glucosamine disaccharide is formed by LpxB (9). Kdo 2 -lipid A biosynthesis is completed through 4Ј-phosphorylation ...

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“…Complications in adults include pneumonia, rib fracture, and incontinence. The morbidity and health economic costs associated with pertussis disease in all age-groups are sizeable (De Serres et al 2000;Lee et al 2004;Pichichero and Treanor 1997). Pertussis vaccines have been available since early in the twentieth century and have been highly effective in reducing childhood morbidity and mortality due to pertussis, as illustrated by longitudinal data from the UK (Fig.…”

Section: Pertussis: Overview Of Bacteriology and Pathologymentioning

confidence: 99%