Moraxella (Branhamella) Catarrhalis

2013 ◽  
pp. 917-920
Author(s):  
Lisa S. Hodges ◽  
Joseph A. Jr. Bocchini
Keyword(s):  
Branhamella Catarrhalis

Improved tween 80 hydrolysis method for identification ofMoraxella (Branhamella)catarrhalis

1991 ◽  
Vol 10 (6) ◽  
pp. 531-533 ◽  
Author(s):  
J. A. García Rodríguez ◽  
J. E. García Sánchez ◽  
J. L. Muñoz Bellido ◽  
E. García Sánchez
Keyword(s):  
Tween 80 ◽  
Hydrolysis Method ◽  
Branhamella Catarrhalis

Bacterial tracheitis caused by Branhamella catarrhalis

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

Comparative analysis of the transferrin and lactoferrin binding proteins in the family Neisseriaceae

1989 ◽  
Vol 35 (3) ◽  
pp. 409-415 ◽  
Author(s):  
Anthony B. Schryvers ◽  
B. Craig Lee
Keyword(s):  
Binding Proteins ◽  
Solid Phase ◽  
Bacterial Species ◽  
Binding Activity ◽  
Intact Cells ◽  
Human Transferrin ◽  
Affinity Isolation ◽  
Lactoferrin Receptor ◽  
Solid Phase Binding ◽  
Branhamella Catarrhalis

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.

scholarly journals Tissue culture adherence and haemagglutination characteristics ofMoraxella (Branhamella) catarrhalis

1999 ◽  
Vol 24 (1) ◽  
pp. 105-114 ◽  
Author(s):  
Margaret Fitzgerald ◽  
Susan Murphy ◽  
Riona Mulcahy ◽  
Conor Keane ◽  
Davis Coakley ◽  
...  
Keyword(s):  
Tissue Culture ◽  
Branhamella Catarrhalis
Sign in / Sign up

Export Citation Format

Share Document