scholarly journals High-molecular-weight proteins of nontypeable Haemophilus influenzae mediate bacterial adhesion to cellular proteoglycans.

1994 ◽  
Vol 62 (9) ◽  
pp. 4028-4033 ◽  
Author(s):  
G J Noel ◽  
D C Love ◽  
D M Mosser
2005 ◽  
Vol 73 (2) ◽  
pp. 1221-1225 ◽  
Author(s):  
I. Zafer Ecevit ◽  
Kirk W. McCrea ◽  
Carl F. Marrs ◽  
Janet R. Gilsdorf

ABSTRACT High-molecular-weight proteins of Haemophilus influenzae mediate attachment to epithelial cells. Previous reports describe several allelic versions of hmwA genes that have different adherence properties. Here we report three new alleles of hmwA (hmwA from strain AAr96, hmwA from strain AAr105, and hmwA from strain G822), demonstrating the high degree of DNA variation of these genes among different strains.


1973 ◽  
Vol 72 (2) ◽  
pp. 235-242 ◽  
Author(s):  
A. M. Reuter ◽  
J. C. Hendrick ◽  
J. Sulon ◽  
P. Franchimont

ABSTRACT The percentage of LH* bound to antibodies that have been covalently bound to cellulose is diminished in the presence of LH-free human serum and sera from various species of animals. Serum fractionation studies on Sephadex G 200 show that the greatest interference comes from the proteins eluted in the void volume i. e. the high molecular weight proteins. Specifically, the gamma M globulins and the α2-macroglobulins appear to play an important role, as demonstrated by tests in which these proteins were neutralized by gamma M and α2-macroglobulin antisera.


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