BRANHAMELLA CATARRHALIS BACTEREMIA IN CHILDREN

1988 ◽  
Vol 7 (10) ◽  
pp. 738 ◽  
Author(s):  
William A. Bonadio
1991 ◽  
Vol 10 (6) ◽  
pp. 531-533 ◽  
Author(s):  
J. A. García Rodríguez ◽  
J. E. García Sánchez ◽  
J. L. Muñoz Bellido ◽  
E. García Sánchez

1989 ◽  
Vol 5 (3) ◽  
pp. 171-172 ◽  
Author(s):  
JOEL L. BASS ◽  
SARAH M. AXEL ◽  
KISHOR A. MEHTA ◽  
LAWRENCE I. BENNETT

1989 ◽  
Vol 35 (3) ◽  
pp. 409-415 ◽  
Author(s):  
Anthony B. Schryvers ◽  
B. Craig Lee

Intact cells of several bacterial species were tested for their ability to bind human transferrin and lactoferrin by a solid-phase binding assay using horseradish peroxidase conjugated transferrin and lactoferrin. The ability to bind lactoferrin was detected in all isolates of Neisseria and Branhamella catarrhalis but not in isolates of Escherichia coli or Pseudomonas aeruginosa. Transferrin-binding activity was similarly detected in most isolates of Neisseria and Branhamella but not in E. coli or P. aeruginosa. The expression of transferrin- and lactoferrin-binding activity was induced by addition of ethylenediamine di-o-phenylacetic acid and reversed by excess FeCl3, indicating regulation by the level of available iron in the medium. The transferrin receptor was specific for human transferrin and the lactoferrin receptor had a high degree of specificity for human lactoferrin in all species tested. The transferrin- and lactoferrin-binding proteins were identified after affinity isolation using biotinylated human transferrin or lactoferrin and streptavidin–agarose. The lactoferrin-binding protein was identified as a 105-kilodalton protein in all species tested. Affinity isolation with biotinylated transferrin yielded two or more proteins in all species tested. A high molecular mass protein was observed in all isolates, and was of similar size (approximately 98 kilodaltons) in all species of Neisseria but was larger (105 kilodaltons) in B. catarrhalis.Key words: iron, Neisseria, transferrin, lactoferrin, receptor.


1999 ◽  
Vol 24 (1) ◽  
pp. 105-114 ◽  
Author(s):  
Margaret Fitzgerald ◽  
Susan Murphy ◽  
Riona Mulcahy ◽  
Conor Keane ◽  
Davis Coakley ◽  
...  

1999 ◽  
Vol 67 (3) ◽  
pp. 1310-1316 ◽  
Author(s):  
Dexiang Chen ◽  
Vicki Barniak ◽  
Karl R. VanDerMeid ◽  
John C. McMichael

ABSTRACT The UspA1 and UspA2 proteins from Moraxella catarrhalisshare antigenic epitopes and are promising vaccine candidates. In this study, the levels and bactericidal activities of antibodies in sera from healthy adults and children toward UspA1 and UspA2 from the O35E strain were measured. Human sera contained antibodies to both proteins, and the levels of immunoglobulin G (IgG) antibodies were age dependent. Adult sera had significantly higher titers of IgG than child sera (P < 0.01). The IgG3 titers to the UspA proteins were higher than the IgG1 titers in the adults’ sera, while the IgG1 titers were higher than the IgG3 titers in the children’s sera (P < 0.05). The IgG antibodies in the sera from 2-month-old children appeared to be maternally derived, since the mean titer was significantly higher than that in sera from 6- to 7-month-old children (P < 0.05). Serum IgA antibodies to both UspA1 and UspA2 were low during the first 7 months of age but thereafter gradually increased along with the IgG titers. Analysis of sera absorbed with UspA1 or UspA2 showed that the antibodies to UspA1 and UspA2 were cross-reactive with each other and associated with serum bactericidal activity. Examination of affinity-purified human antibodies confirmed that naturally acquired antibodies to UspA1 and UspA2 were bactericidal and cross-reactive. These results support using UspA1 and UspA2 in a vaccine to prevent M. catarrhalisinfections.


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