Lipopolysaccharide epitope specificity and binding cross reactivity of the human IgM anti-lipid a monoclonal antibody SdJ5-1.17.15

Kazemi, Mohammad; Huntenburg, Carolyn C.; Rubbers, J.Eric

doi:10.1016/0161-5890(93)90013-2

Cited by 3 publications

(2 citation statements)

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“…It was of interest, then, to determine whether an anti-lipid A MAb could, by virtue of its capacity to inhibit LPS-induced cytokine production, produce the same effects as reagents which block cytokine activity. The human IgM MAb SdJ5 was generated against a heat-killed S. minnesota R595 whole-organism vaccine and has previously been reported to recognize an epitope expressed on the lipid A moiety of LPS (17). The present study was designed to determine whether the anti-lipid A specificity of SdJ5 conferred upon this antibody the ability to neutralize LPS-induced cytokine production in vitro and whether this activity correlated with the ability of SdJ5 to protect rats from lethal endotoxin challenge.…”

Section: Discussionmentioning

confidence: 99%

“…In order to address these sources of variability, a novel human immunoglobulin M (IgM) MAb, SdJ5-1.17.15 (SdJ5), was developed against lipid A (8). Subsequent studies demonstrated that SdJ5 binds to an epitope on lipid A associated with its biologic activity (17). The present study evaluated the therapeutic potential of SdJ5 and characterized the in vitro inhibitory effects of this MAb on LPS-induced TNF-a and IL-lp production by human peripheral blood mononuclear cells (hPBMC).…”

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Inhibition of lipopolysaccharide-associated endotoxin activities in vitro and in vivo by the human anti-lipid A monoclonal antibody SdJ5-1.17.15

et al. 1993

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The present study evaluated the effect of a novel anti-lipid A monoclonal antibody, termed SdJ5, on the in vitro production of tumor necrosis factor alpha (TNF-a) and interleukin-1f% by endotoxinor lipopolysaccharide (LPS)-challenged human peripheral blood mononuclear cells (hPBMC). In addition, the present study determined whether SdJ5 could neutralize the in vivo toxicity of LPS. SdJ5, at a concentration equal to or greater than 3 iLg/ml, specifically inhibited TNF-a and interleukin-lj production by hPBMC stimulated with every type of LPS and lipid A assessed. SdJ5 also showed a significantly greater inhibition of cytokine production than a nonrelevant human immunoglobulin M myeloma control. The SdJ5-mediated inhibition of TNF-a production was rapid, as the simultaneous addition of the SdJ5 and LPS still resulted in a marked decrease in hPBMC cytokine synthesis. The ability of SdJ5 to neutralize in vivo toxicity was also determined by using LPS from four different strains of gram-negative bacteria. LPS, when preincubated with SdJ5, resulted in a significant decrease in the 24-h mortality rate compared with that for the control. These studies show that the anti-lipid A monoclonal antibody SdJ5 can modulate LPS-induced cytokine production in vitro and increase the survival rate of rats challenged with lethal doses of LPS.

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Inhibition of lipopolysaccharide-associated endotoxin activities in vitro and in vivo by the human anti-lipid A monoclonal antibody SdJ5-1.17.15

et al. 1993

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Rollenhagen

Czaniera

Albert

et al. 2001

Journal of Neurocytology

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The HNK-1 carbohydrate, an unusual 3'-sulfated glucuronic acid epitope characteristic of many neural recognition molecules, serves as a ligand in neural cell interactions and is differentially expressed in the quadriceps and saphenous branches of the femoral nerve in the PNS of adult mice. Based on these observations, we investigated the possibility that the HNK-1 carbohydrate may be differentially distributed in neurons and fiber tracts also in the CNS thereby contributing to different targeting and guidance mechanisms. We have used antibodies with different HNK-1 epitope specificities to probe for subtle differences in expression patterns. In the adult mouse cerebellum the HNK-1 carbohydrate is detectable in stripe-like compartments in the molecular and Purkinje cell layers, whereas N-CAM and its associated alpha2,8 polysialic acid does not show this compartmentation. In the adult hippocampus, the HNK-1 carbohydrate localizes to perineuronal nets of inhibitory interneurons and marks the inner third of the molecular layer of the dentate gyrus. In the adult spinal cord, HNK-1 labeling is most pronounced in gray matter areas. White matter enriched regions show differential labeling with regard to fiber tracts and antibody specificity. Whereas the different antibodies do not show differences in staining in the cerebellum and the hippocampus, they show differences in staining pattern of fiber tracts and motoneurons in the spinal cord. The HNK-1 expression pattern also differed in the adult spinal cord from that observed at embryonic day 14 and postnatal day 14. Our observations suggest a functional role in the specification of functionally discrete compartments in different areas of the CNS and during development.

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Monoclonal antibodies that distinguish inner core, outer core, and lipid A regions of Pseudomonas aeruginosa lipopolysaccharide

Kievit

Lam

1994

J Bacteriol

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In order to examine the immunochemistry of the core-lipid A region of Pseudomonas aeruginosa lipopolysaccharide (LPS), monoclonal antibodies (MAbs) specific for this region were produced in mice. Immunogen was prepared by coating a rough mutant of P. aeruginosa with column-purified core oligosaccharide fractions in order to enhance the immune response to the LPS core-lipid A region. Fourteen hybridoma clones were isolated, characterized, and further divided into three groups on the basis of their reactivities to rough LPS antigens in both enzyme-linked immunosorbent assays and Western immunoblots. In addition, another MAb, 18-19, designated group 1, was included in this study for defining core-lipid A epitopes. MAb 18-19 recognizes the LPS core-plus-one 0-repeat unit of the serologically cross-reactive P. aeruginosa 02, 05, and 016. Group 2 MAbs are specific for the LPS outer core region and reacted with P. aeruginosa 02, 05, 07, 08, 010, 016, 018, 019, and 020, suggesting that these serotypes share a common outer core type. Group 3 MAbs recognize the inner core region and reacted with all 20 P. aeruginosa serotypes as well as with other Pseudomonas species, revealing the conserved nature of this region. Group 4 MAbs are specific for lipid A and reacted with all gram-negative organisms tested. Immunoassays using these MAbs and well-defined rough mutants, in addition to the recently determined P. aeruginosa core structures, have allowed us to precisely define immunodominant epitopes within the LPS core region.Pseudomonas aeruginosa is an opportunistic pathogen that is among the most frequently isolated bacteria in nosocomial infections (16); it also poses a major threat to compromised individuals such as patients with cancer, burn wounds, and cystic fibrosis (52). It is highly adaptable for survival in a wide range of environments and is known to have intrinsic resistance to antibiotics. These characteristics have led to an interest in active or passive immunization for treatment of infections. P. aeruginosa possesses lipopolysaccharide (LPS) as one of its major virulence factors (8), and LPS has been reported to be the most immunogenic of the various cell surface antigens (30).The structural organization of P. aeruginosa LPS is similar to that of the LPS of members of the family Enterobacteriaceae, consisting of three regions including 0-polysaccharide, core oligosaccharide, and lipid A, covalently linked to one another. Recent studies (45, 47) have indicated that P. aeruginosa produces two antigenically and chemically distinct LPS molecules, namely, A-band and B-band LPS. A-band LPS is a predominantly neutral polysaccharide composed of a D-rhamnan (2) and is antigenically conserved, while B-band is the 0-antigen-containing LPS. Differences in the chemical structure of the B-band 0-polysaccharide form the basis of the 0-serotyping classification of this organism. The most complete serotyping system for P. aeruginosa, the International Antigenic Typing Scheme (IATS), consists of 17 standard 0 serotypes (32); howe...

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Lipopolysaccharide epitope specificity and binding cross reactivity of the human IgM anti-lipid a monoclonal antibody SdJ5-1.17.15

Cited by 3 publications

References 27 publications

Inhibition of lipopolysaccharide-associated endotoxin activities in vitro and in vivo by the human anti-lipid A monoclonal antibody SdJ5-1.17.15

Inhibition of lipopolysaccharide-associated endotoxin activities in vitro and in vivo by the human anti-lipid A monoclonal antibody SdJ5-1.17.15

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Monoclonal antibodies that distinguish inner core, outer core, and lipid A regions of Pseudomonas aeruginosa lipopolysaccharide

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