<i>Hemophilus influenzae</i>Pneumonia in Adults

Stratton, Charles W.; Hawley, H. Bradford; Horsman, Thomas A.; Tu, Kevin K.; Ackley, Alexander; Fernando, Nirmal K.; Weinstein, Melvin P.

doi:10.1164/arrd.1980.121.3.595

Cited by 21 publications

(4 citation statements)

References 14 publications

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“…In previously published therapeutic trials, cefuroxime has been compared with (1) ampicillin and amoxicillin trihydrate with and without clavulanic acid for uncompli¬ cated gonorrhea (including infections caused by penicillinase-producing organisms),19"22 (2) cefaclor for the therapy for otitis media,23 (3) penicillin V potassium in the treatment of group A streptococcal pharyngitis,24 and (5) cefaclor for skin and skin structure infections25; in each of these trials, cefuroxime was at least as effective as the comparative agent. Cefuroxime has also been found to be effective for urinary infections in a noncomparative trial in elderly patients.26 Side effects, more commonly seen with cefurox¬ ime, were limited to vomiting in children who were treated for otitis media using a previous tablet formulation that lacked a coating.…”

Section: Hours)12mentioning

confidence: 99%

Blinded Comparison of Cefuroxime to Cefaclor for Lower Respiratory Tract Infections

Schleupner

Anthony²,

Tan³

et al. 1988

Arch Intern Med

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Section: Hours)12mentioning

confidence: 99%

Blinded Comparison of Cefuroxime to Cefaclor for Lower Respiratory Tract Infections

Schleupner

Anthony²,

Tan³

et al. 1988

Arch Intern Med

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“…These strains are the second most common cause of otitis media in infants and children after pneumococci (6,7,18,40). Nontypeable H. influenzae is also an important cause of respiratory tract infections in adults, particularly the elderly and patients with chronic bronchitis, and in children in the developing world (5,30,39,41,43,45).…”

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confidence: 99%

Molecular conservation of the P6 outer membrane protein among strains of Haemophilus influenzae: analysis of antigenic determinants, gene sequences, and restriction fragment length polymorphisms

et al. 1991

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Infections caused by Haemophilus influenzae are a major worldwide health problem. In particular, nontypeable strains of H. influenzae are a common cause of otitis media in infants and children. A vaccine to prevent these infections would result in the prevention of substantial morbidity and cost savings. A problem in identifying an appropriate vaccine antigen has been the enormous antigenic heterogeneity among nontypeable strains of H. influenzae. The present study was undertaken to characterize the conservation of the P6 outer membrane protein (approximately 16,000 daltons) among strains of H. influenzae. A total of 20 type b strains and 20 nontypeable strains of diverse geographic and clinical origins was studied. Three approaches were taken. (i) Antigenic determinants recognized by monoclonal and polyclonal antibodies were present on P6 in all 40 strains tested. The molecular weight of P6 was identical in all strains. (ii) Comparison of the DNA sequences of the P6 genes from three epidemiologically and serologically unrelated strains demonstrated 100% homology at the amino acid level and 97 to 99% homology at the nucleotide level. (iii) Restriction fragment length polymorphism analysis demonstrated that the P6 gene and flanking sequences were highly conserved among all strains. These three independent series of experiments indicated that the P6 protein is highly conserved among strains of H. influenzae. P6 should receive serious consideration for inclusion in a vaccine to prevent infections caused by nontypeable H. influenzae.

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“…In children, this bacterium is a common cause of otitis media and sinusitis (4,5,10,33,38). Nontypeable H. influenzae is also an important cause of respiratory tract infections particularly in the elderly, in patients with chronic bronchitis, and in children in the developing world (3,26,32,37,41). Finally, the organism occasionally causes invasive infections such as meningitis and bacteremia, especially in neonates and postpartum women (19,39,40).…”

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confidence: 99%

Strain-specific and immunodominant surface epitopes of the P2 porin protein of nontypeable Haemophilus influenzae

et al. 1991

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The P2 porin protein is the major outer membrane protein of nontypeable Haemophilus influenzae. Five monoclonal antibodies to P2 of four strains of nontypeable H. influenzae were developed by immunizing mice with whole bacterial cells. All five antibodies recognized epitopes on P2 in immunoblot assays of whole organism lysates, purified outer membrane, and purified P2. Competitive enzyme-linked immunosorbent assays and immunoblot assays of cyanogen bromide-digested P2 showed that two antibodies to the P2 protein of strain 1479 recognized different epitopes on the molecule. Immunofluorescence and immunoelectron microscopy demonstrated that each of the five antibodies recognized epitopes that were abundantly expressed on the bacterial surface. Analysis of 120 H. influenzae strains indicated that three of the five antibodies were reactive exclusively with the homologous strain. The remaining two antibodies were reactive with less than 3% of the strains. These studies indicate that the P2 protein expresses a highly strain-specific and immunodominant epitope on the bacterial surface. The expression of strain-specific and immunodominant epitopes on the bacterial surface may represent a mechanism by which the bacterium induces antibodies that will protect against recurrent infection by the homologous strain but will not protect against infection by heterologous strains.

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Hemophilus influenzaePneumonia in Adults

Cited by 21 publications

References 14 publications

Blinded Comparison of Cefuroxime to Cefaclor for Lower Respiratory Tract Infections

Blinded Comparison of Cefuroxime to Cefaclor for Lower Respiratory Tract Infections

Molecular conservation of the P6 outer membrane protein among strains of Haemophilus influenzae: analysis of antigenic determinants, gene sequences, and restriction fragment length polymorphisms

Strain-specific and immunodominant surface epitopes of the P2 porin protein of nontypeable Haemophilus influenzae

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