Secretory Immunoglobulin A Carries Oligosaccharide Receptors for Escherichia coli Type 1 Fimbrial Lectin

1991 ◽  
Vol 59 (7) ◽  
pp. 2513-2513
Keyword(s):  
Escherichia Coli ◽  
Immunoglobulin A ◽  
Secretory Immunoglobulin A ◽  
Secretory Immunoglobulin

scholarly journals Secretory immunoglobulin A carries oligosaccharide receptors for Escherichia coli type 1 fimbrial lectin.

1990 ◽  
Vol 58 (9) ◽  
pp. 3073-3077 ◽  
Author(s):  
A E Wold ◽  
J Mestecky ◽  
M Tomana ◽  
A Kobata ◽  
H Ohbayashi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Immunoglobulin A ◽  
Secretory Immunoglobulin A ◽  
Secretory Immunoglobulin

scholarly journals Reduced Phase Switch Capacity and Functional Adhesin Expression of Type 1-Fimbriated Escherichia coli from Immunoglobulin A-Deficient Individuals

2006 ◽  
Vol 75 (2) ◽  
pp. 932-940 ◽  
Author(s):  
Forough L. Nowrouzian ◽  
Vanda Friman ◽  
Ingegerd Adlerberth ◽  
Agnes E. Wold
Keyword(s):  
Escherichia Coli ◽  
Immunoglobulin A ◽  
Secretory Immunoglobulin A ◽  
Carriage Rate ◽  
E Coli ◽  
Frequent Failure ◽  
Colonic Cells ◽  
Secretory Immunoglobulin ◽  
Carbohydrate Chains

ABSTRACT The mannose-specific adhesin of type 1 fimbriae is the most common adhesin in Escherichia coli. One receptor for this adhesin is the carbohydrate chains of secretory immunoglobulin A (S-IgA), and intestinal E. coli from IgA-deficient individuals has a reduced capacity to adhere to mannose-containing receptors. Here, we investigated the expression of the mannose-specific adhesin and its capacity to switch to the fimbriated phenotype in colonic resident and transient E. coli strains isolated from control (n = 16) and IgA-deficient (n = 17) persons. Resident E. coli strains from IgA-deficient individuals displayed weaker mannose-specific adherence to colonic cells than resident strains from control individuals (21 versus 44 bacteria/cell, P = 0.0009) due to three mechanisms: a lower carriage rate of the fimH gene (90% versus 97%, not significant), more frequent failure to switch on the fim genes (30% versus 6%, P = 0.02), and the reduced adhesive potential of fimH + isolates capable of phase switch (26 versus 46 bacteria/cell, P = 0.02). On the other hand, resident strains from IgA-deficient individuals displayed stronger mannose-resistant adherence than resident strains from control individuals (P = 0.04) and transient strains from IgA-deficient individuals (P = 0.01). The presence of S-IgA appears to favor the establishment of E. coli clones which readily express mannose-specific adhesins in the bowel microbiota.

Inhibition of enteroaggregative Escherichia coli adhesion to HEp-2 cells by secretory immunoglobulin A from human colostrum

2001 ◽  
Vol 20 (7) ◽  
pp. 672-678 ◽  
Author(s):  
ROSELICE MARIO FERNANDES ◽  
SOLANGE BARROS CARBONARE ◽  
MAGDA MARIA SALLES CARNEIRO-SAMPAIO ◽  
LUIZ RACHID TRABULSI
Keyword(s):  
Escherichia Coli ◽  
Immunoglobulin A ◽  
Secretory Immunoglobulin A ◽  
Human Colostrum ◽  
Secretory Immunoglobulin

scholarly journals Fab-Independent Antiadhesion Effects of Secretory Immunoglobulin A on S-Fimbriated Escherichia coli Are Mediated by Sialyloligosaccharides

1998 ◽  
Vol 66 (8) ◽  
pp. 3971-3973 ◽  
Author(s):  
Horst Schroten ◽  
Christoph Stapper ◽  
Ricarda Plogmann ◽  
Henrik Köhler ◽  
Jörg Hacker ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Epithelial Cells ◽  
Human Milk ◽  
Immunoglobulin A ◽  
Secretory Immunoglobulin A ◽  
E Coli ◽  
Human Epithelial Cells ◽  
Early Human ◽  
Secretory Immunoglobulin

ABSTRACT S-fimbriated Escherichia coli strains cause sepsis and meningitis in newborns and are known to recognize the carbohydrate sequence sialyl-(α2-3)-galactoside. We show that adhesion of cloned S-fimbriated E. coli to human epithelial cells is inhibited Fab independently by sialyloligosaccharides on secretory immunoglobulin A (s-IgA). This indicates an anti-infective function of s-IgA (Fc), particularly in early human milk.

scholarly journals Cleavage of the Human Immunoglobulin A1 (IgA1) Hinge Region by IgA1 Proteases Requires Structures in the Fc region of IgA

2003 ◽  
Vol 71 (5) ◽  
pp. 2563-2570 ◽  
Author(s):  
Koteswara R. Chintalacharuvu ◽  
Philip D. Chuang ◽  
Ashley Dragoman ◽  
Christine Z. Fernandez ◽  
Jiazhou Qiu ◽  
...  
Keyword(s):  
Haemophilus Influenzae ◽  
Pathogenic Bacteria ◽  
Immunoglobulin A ◽  
Secretory Immunoglobulin A ◽  
Constant Region ◽  
Wild Type ◽  
Mucosal Surfaces ◽  
Secretory Immunoglobulin

ABSTRACT Secretory immunoglobulin A (IgA) protects the mucosal surfaces against inhaled and ingested pathogens. Many pathogenic bacteria produce IgA1 proteases that cleave in the hinge of IgA1, thus separating the Fab region from the Fc region and making IgA ineffective. Here, we show that Haemophilus influenzae type 1 and Neisseria gonorrhoeae type 2 IgA1 proteases cleave the IgA1 hinge in the context of the constant region of IgA1 or IgA2m(1) but not in the context of IgG2. Both Cα2 and Cα3 but not Cα1 are required for the cleavage of the IgA1 hinge by H. influenzae and N. gonorrhoeae proteases. While there was no difference in the cleavage kinetics between wild-type IgA1 and IgA1 containing only the first GalNAc residue of the O-linked glycans, the absence of N-linked glycans in the Fc increased the ability of the N. gonorrhoeae protease to cleave the IgA1 hinge. Taken together, these results suggest that, in addition to the IgA1 hinge, structures in the Fc region of IgA are required for the recognition and cleavage of IgA1 by the H. influenzae and N. gonorrhoeae proteases.

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