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.

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 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 EsiB, a Novel Pathogenic Escherichia coli Secretory Immunoglobulin A-Binding Protein Impairing Neutrophil Activation

mBio ◽  
2013 ◽  
Vol 4 (4) ◽  
Author(s):  
Ilaria Pastorello ◽  
Silvia Rossi Paccani ◽  
Roberto Rosini ◽  
Rossella Mattera ◽  
Mario Ferrer Navarro ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protective Antigen ◽  
Immunoglobulin A ◽  
Distribution Analysis ◽  
Secretory Immunoglobulin A ◽  
Content Type ◽  
E Coli ◽  
Novel Strategy ◽  
Tract Infections ◽  
Secretory Immunoglobulin

ABSTRACTIn this study, we have characterized the functional properties of a novelEscherichia coliantigen named EsiB (E. colisecretoryimmunoglobulin A-binding protein), recently reported to protect mice from sepsis. Gene distribution analysis of a panel of 267 strains representative of differentE. colipathotypes revealed thatesiBis preferentially associated with extraintestinal strains, while the gene is rarely found in either intestinal or nonpathogenic strains. These findings were supported by the presence of anti-EsiB antibodies in the sera of patients affected by urinary tract infections (UTIs). By solving its crystal structure, we observed that EsiB adopts a superhelical fold composed of Sel1-like repeats (SLRs), a feature often associated with bacterial proteins possessing immunomodulatory functions. Indeed, we found that EsiB interacts with secretory immunoglobulin A (SIgA) through a specific motif identified by an immunocapturing approach. Functional assays showed that EsiB binding to SIgA is likely to interfere with productive FcαRI signaling, by inhibiting both SIgA-induced neutrophil chemotaxis and respiratory burst. Indeed, EsiB hampers SIgA-mediated signaling events by reducing the phosphorylation status of key signal-transducer cytosolic proteins, including mitogen-activated kinases. We propose that the interference with such immune events could contribute to the capacity of the bacterium to avoid clearance by neutrophils, as well as reducing the recruitment of immune cells to the infection site.IMPORTANCEPathogenicEscherichia coliinfections have recently been exacerbated by increasing antibiotic resistance and the number of recurrent contagions. Attempts to develop preventive strategies againstE. colihave not been successful, mainly due to the large antigenic and genetic variability of virulence factors, but also due to the complexity of the mechanisms used by the pathogen to evade the immune system. In this work, we elucidated the function of a recently discovered protective antigen, named EsiB, and described its capacity to interact with secretory immunoglobulin A (SIgA) and impair effector functions. This work unravels a novel strategy used byE. colito subvert the host immune response and avoid neutrophil-dependent clearance.

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 P fimbriae and aerobactin as intestinal colonization factors for Escherichia coli in Pakistani infants

2001 ◽  
Vol 126 (1) ◽  
pp. 19-23 ◽  
Author(s):  
F. NOWROUZIAN ◽  
A. E. WOLD ◽  
I. ADLERBERTH
Keyword(s):  
Escherichia Coli ◽  
Virulence Factors ◽  
Western Europe ◽  
Carriage Rate ◽  
E Coli ◽  
Colonization Factors ◽  
P Type ◽  
K1 Capsule ◽  
Fimbrial Adhesin

The carriage rate of a range of virulence genes was compared between resident and transient Escherichia coli strains obtained from the rectal flora of 22 home-delivered Pakistani infants 0–6 months old. Genes for the following virulence factors were assessed using multiplex PCR: P, type 1 and S fimbriae, three P fimbrial adhesin varieties, Dr haemagglutinin, K1 and K5 capsule, haemolysin and aerobactin. The E. coli strains examined here differed from those previously obtained from hosts in Western Europe in a lower prevalence of genes for P, S and type 1 fimbriae, K1 capsule and haemolysin. Nevertheless, genes for P fimbriae, the class II variety of papG adhesin, and aerobactin were significantly more common among resident than transient strains, as previously observed in a Swedish study. The results suggest that P fimbriae and aerobactin, previously implicated as virulence factors for urinary tract infection, might contribute to persistence of E. coli in the normal intestinal microflora.

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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