Monoclonal immunoglobulin A antibody directed against serotype-specific epitope of Shigella flexneri lipopolysaccharide protects against murine experimental shigellosis.

Phalipon, Armelle; Kaufmann, M; Michetti, Pierre; Cavaillon, Jean‐Marc; Huerre, Michel; Sansonetti, Philippe J.; Kraehenbuhl, J. P.

doi:10.1084/jem.182.3.769

Cited by 157 publications

(118 citation statements)

References 40 publications

(53 reference statements)

Supporting

Mentioning

111

Contrasting

Order By: Relevance

“…Previous studies of these four pathogens have linked LOS/LPS to adherence/virulence with full-length LOS/LPS for each of these organisms is absolutely required for virulence in animal models (40)(41)(42)(43). S. flexneri LPS O-antigen is a virulence factor whose chain length affects both serum resistance and the function of surface virulence factors; a role for LPS in cell invasion has been reported (11,(44)(45)(46).…”

Section: Discussionmentioning

confidence: 99%

Glycan:glycan interactions: High affinity biomolecular interactions that can mediate binding of pathogenic bacteria to host cells

Day

Tran

Semchenko

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

100

104

View full text Add to dashboard Cite

Cells from all domains of life express glycan structures attached to lipids and proteins on their surface, called glycoconjugates. Cell-tocell contact mediated by glycan:glycan interactions have been considered to be low-affinity interactions that precede highaffinity protein-glycan or protein-protein interactions. In several pathogenic bacteria, truncation of surface glycans, lipooligosaccharide (LOS), or lipopolysaccharide (LPS) have been reported to significantly reduce bacterial adherence to host cells. Here, we show that the saccharide component of LOS/LPS have direct, high-affinity interactions with host glycans. Glycan microarrays reveal that LOS/LPS of four distinct bacterial pathogens bind to numerous host glycan structures. Surface plasmon resonance was used to determine the affinity of these interactions and revealed 66 high-affinity host-glycan:bacterial-glycan pairs with equilibrium dissociation constants (K D ) ranging between 100 nM and 50 μM. These glycan:glycan affinity values are similar to those reported for lectins or antibodies with glycans. Cell assays demonstrated that glycan:glycan interaction-mediated bacterial adherence could be competitively inhibited by either host cell or bacterial glycans. This is the first report to our knowledge of high affinity glycan:glycan interactions between bacterial pathogens and the host. The discovery of large numbers of glycan:glycan interactions between a diverse range of structures suggests that these interactions may be important in all biological systems.H ost surface glycosylation is ubiquitous and is targeted by pathogenic bacteria, viruses, fungi and parasites for adherence and toxin binding and by glycosidases (1). Escherichia coli type 1 fimbriae, FimH, is one of the most widely studied glycanrecognizing protein adhesins, with specificity for monomannose to oligomannose structures with the variability of the mannose structure bound leading to different tissue tropism (2). Other glycan-recognizing adhesins expressed by bacteria include the following: Pseudomonas aeruginosa lectins 1 and 2 (PA-IL and PA-IIL) that have specificity for galactose and fucose, respectively (3); Helicobacter pylori SabA, specific for sialic acid containing glycoconjugates including sialyLewis X; and BabAspecific for fucosylated glycoconjugates including Lewis B (4, 5). Although there are numerous known glycan binding adhesins, the adhesins of some bacteria that interact with host surface glycans remain unknown.Direct interactions between surface glycans (glycan:glycan interactions) have been reported in sea sponges as heterogenous glycan interactions, and in mouse embryo development and cancer where homodimers of Lewis X (LeX) or ganglioside structures play a role in cell adhesion and growth factor receptor interactions (6, 7). Outside of these reports, glycan:glycan interactions, when noted, have generally been considered to be low-affinity, weak interactions (8) that precede high-affinity protein:glycan or protein:protein interactions (1, 2, 5, 9).Interestingly, there...

show abstract

Section: Discussionmentioning

confidence: 99%

Glycan:glycan interactions: High affinity biomolecular interactions that can mediate binding of pathogenic bacteria to host cells

Day

Tran

Semchenko

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

100

104

View full text Add to dashboard Cite

show abstract

“…inoculation of S. flexneri in mice results in an acute bronchopneumonia with alveolitis, characterized by a massive influx of PMN. The invasive and inflammatory properties of S. flexneri in this murine lung model mimic those observed in the infected human intestinal mucosa (36). The in vivo bioactivity of delivered IL-10 and IL-1ra was assessed by investigating the virulence profile of recombinant strains and the inflammation-related parameters in the murine pulmonary model of infection.…”

Section: Discussionmentioning

confidence: 99%

“…administration of wild-type strain M90T in mice induces a strong inflammatory response within the lung parenchyma, characterized by a massive infiltration of PMN within alveoli and bronchi, mimicking the inflammation induced in the intestinal tract with Shigella spp (36). Before testing whether the difference observed in survival was due to limited tissue damage as a result of the control of inflammatory cytokines by IL-10-and IL-1ra-secreting strains, we examined the amount of IL-10 and IL-1ra mRNA produced within infected lung tissues (Fig.…”

Section: Inflammation Is Reduced Upon Infection Of Mice With Shigellamentioning

confidence: 99%

“…36, mice were inoculated intranasally (i.n.) with 2 ϫ 10 8 bacteria in 20 l. Bacterial enumeration was performed in the lungs removed from sacrificed mice and ground in 10 ml sterile PBS.…”

Section: Mice Infection and Bacterial Countsmentioning

confidence: 99%

“…H&E staining was done as previously described (36). Inflammation index, representing the percentage of inflammatory area recorded in a series of sections covering the whole lung, was calculated as previously described (38).…”

Section: Histopathological Analysismentioning

confidence: 99%

See 2 more Smart Citations

Delivery of Biologically Active Anti-Inflammatory Cytokines IL-10 and IL-1ra In Vivo by the Shigella Type III Secretion Apparatus

Chamekh

Phalipon

Quertainmont

et al. 2008

The Journal of Immunology

View full text Add to dashboard Cite

Pathogenicity of many Gram-negative bacteria relies on a type III secretion (T3S) apparatus, which is used for delivery of bacterial effectors into the host cell cytoplasm allowing the bacteria to manipulate host cell cytoskeleton network as well as to interfere with intracellular signaling pathways. In this study, we investigated the potential of the Shigella flexneri T3SA as an in vivo delivery system for biologically active molecules such as cytokines. The anti-inflammatory cytokines IL-10 and IL-1 receptor antagonist (IL-1ra) were genetically fused to the first 30 or 60 residues of the Shigella T3S effector IpaH9.8 or to the first 50 residues of the Yersinia enterocolitica effector YopE and the recombinant fusion proteins were expressed in S. flexneri. YopE50-IL-10, IpaH60-IL-10, and IpaH60-IL-1ra were efficiently secreted via the T3S apparatus of Shigella. Moreover, these recombinant proteins did not impair the invasive ability of the bacteria in vitro. In a murine model, Shigella strains expressing YopE50-IL-10, IpaH60-IL-10, and IpaH60-IL-1ra induced a lower mortality in mice that was associated with reduced inflammation and a restricted localization of bacteria within the lung tissues as compared with wild-type Shigella. Moreover, the level of TNF-α and IL-1β mRNA were reduced in the lungs following infection by IL-10- and IL-1ra-secreting Shigella, respectively. These findings demonstrate that the Shigella T3S apparatus can deliver biologically active cytokines in vivo, thus opening new avenues for the use of attenuated bacteria to deliver proteins for immunomodulation or gene therapy purposes.

show abstract

A synthetic ligand for IgA affinity purification

Palombo¹,

Falco²,

Tortora³

et al. 1998

J. Mol. Recognit.

View full text Add to dashboard Cite

We reported previously that TG19318, a synthetic ligand deduced from the screening of combinatorial libraries, displays specific and selective recognition properties for immunoglobulins of the G class and can be used conveniently for affinity chromatography purification of monoclonal and polyclonal antibodies. In this study we have extended the ligand characterization, examining its ability to bind IgA from cell culture supernatants and from IgG-deprived serum. Affinity columns prepared by immobilizing TG19318 on Sepharose allowed convenient one-step purification of monoclonal IgA directly from crude feedstocks, in high yield and with full recovery of immunoreactivity. Optimal column adsorption occurred with phosphate buffer at neutral pH, while elution of adsorbed IgA could be accomplished by a buffer pH change to acidic or basic conditions. Column capacity was close to 7 mg IgA/ml support.

show abstract

Monoclonal immunoglobulin A antibody directed against serotype-specific epitope of Shigella flexneri lipopolysaccharide protects against murine experimental shigellosis.

Cited by 157 publications

References 40 publications

Glycan:glycan interactions: High affinity biomolecular interactions that can mediate binding of pathogenic bacteria to host cells

Glycan:glycan interactions: High affinity biomolecular interactions that can mediate binding of pathogenic bacteria to host cells

Delivery of Biologically Active Anti-Inflammatory Cytokines IL-10 and IL-1ra In Vivo by the Shigella Type III Secretion Apparatus

A synthetic ligand for IgA affinity purification

Contact Info

Product

Resources

About