Functional properties of isotype-switched immunoglobulin M (IgM) and IgG monoclonal antibodies to Pseudomonas aeruginosa lipopolysaccharide

Pollack, Matthew; Koles, Nancy L.; Preston, M J; Brown, Brenda; Pier, Gerald B.

doi:10.1128/iai.63.11.4481-4488.1995

Cited by 25 publications

(18 citation statements)

References 26 publications

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“…Complement plays an essential role in modulating pseudomonal infection and is thus likely vital in host defense from the closely related Burkholderia genus as well. Complement component 3 (C3) promotes phagocytosis and killing of P. aeruginosa (15, 16). Additionally, C3‐ and C5‐derived components promote neutrophil recruitment and activation that are necessary for effective phagocytosis.…”

Section: Discussionmentioning

confidence: 99%

Disseminated Burkholderia gladioli infection in a lung transplant recipient with underlying hypocomplementemic urticarial vasculitis

Thompson

Wickes

Herrera

et al. 2011

Transplant Infectious Dis

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Burkholderia gladioli is difficult to definitively identify within the laboratory using phenotypic testing alone. We describe a case of recurrent B. gladioli infection in a lung transplant recipient with underlying hypocomplementemic urticarial vasculitis syndrome, discuss the difficulties encountered with laboratory identification, provide a review of the methodology required for definitive identification, and discuss potential pathophysiologic mechanisms in this patient responsible for the difficulty in treatment.

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Section: Discussionmentioning

confidence: 99%

Disseminated Burkholderia gladioli infection in a lung transplant recipient with underlying hypocomplementemic urticarial vasculitis

Thompson

Wickes

Herrera

et al. 2011

Transplant Infectious Dis

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“…All other sequences have been collected from sequence databases and literature. [28][29][30][31][32] An anti-lipopolysaccharide (LPS) mouse monoclonal 1F6 33 and an anti-meningococcal serogroup C polysaccharide (MCPS) mouse monoclonal 78Á2 34 were used as representatives of antibodies against T-independent antigens, which usually do not undergo antigen-driven affinity maturation process. The existing method of sequence analysis is utilized widely in studies related to abnormal B cell development.…”

Section: Methodsmentioning

confidence: 99%

Problems in using statistical analysis of replacement and silent mutations in antibody genes for determining antigen‐driven affinity selection

Bose

Sinha

2005

Immunology

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Summary The analysis of molecular signatures of antigen‐driven affinity selection of B cells is of immense use in studies on normal and abnormal B cell development. Most of the published literature compares the expected and observed frequencies of replacement (R) and silent (S) mutations in the complementarity‐determining regions (CDRs) and the framework regions (FRs) of antibody genes to identify the signature of antigenic selection. The basic assumption of this statistical method is that antigenic selection creates a bias for R mutations in the CDRs and for S mutations in the FRs. However, it has been argued that the differences in intrinsic mutability among different regions of an antibody gene can generate a statistically significant bias even in the absence of any antigenic selection. We have modified the existing statistical method to include the effects of intrinsic mutability of different regions of an antibody gene. We used this method to analyse sequences of several B cell‐derived monoclonals against T‐dependent antigens, T‐independent antigens, clones derived from lymphoma and amyloidogenic clones. Our sequence analysis indicates that even after correcting for the intrinsic mutability of antibody genes, statistical parameters fail to reflect the role of antigen‐driven affinity selection in maturation of many clones. We suggest that, contrary to the basic assumption of such statistical methods, selection can act both for and against R mutations in the CDR as well as in the FR regions. In addition we have identified different methodological difficulties in the current uses of such statistical analysis of antibody genes.

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“…This suggests an important structural role for the L chain in forming the Ag-binding site for O6 LPS. In a recent report by Pollack and coworkers, the sequences from the H and L chain variable regions from another anti-O6 LPS-specific MAb were reported (40). However, our anti-O6 LPS V H and V L chain genes showed little homology (60%) to these Ig genes, indicative of a diversified immune response to the complex O polysaccharide.…”

Section: Discussionmentioning

confidence: 55%

“…The protective nature of these recombinant Abs will be closely monitored as the Fab portions of our anti-LPS Abs are fused to human constant regions of varying isotypes. Previous studies on another LPS-specific Ab suggested using a cautious approach when choosing a particular Ig class and subclass for immunotherapeutics where isotype-related differences in levels of the efficiency of various effector functions did not correspond to differences in in vivo function (40). In conclusion, results from this study have helped to shed some light on the technology of construction of a functional Fab.…”

Section: Discussionmentioning

confidence: 67%

Phage display and bacterial expression of a recombinant Fab specific for Pseudomonas aeruginosa serotype O6 lipopolysaccharide

Tout

Lam

1997

Clin Diagn Lab Immunol

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Immunotherapy with antibodies (Abs) against the lipopolysaccharide (LPS) of Pseudomonas aeruginosa remains an alternative to serotype-specific LPS-based vaccines due to their limited use and to antibiotics due to the intrinsic resistance to antimicrobials observed in P. aeruginosa. We have chosen a monoclonal Ab (MAb), MF23-1, that binds to the O antigen of the most clinically relevant serotype, IATS O6, for producing a recombinant antibody. Heavy (H) and light (L) chain genes were isolated from MF23-1 to form a functional Fab molecule in the periplasm of Escherichia coli and on the surface of phage by using phagemid vector pComb3. The entire L chain gene was used, but the H chain gene was amplified to 2 amino acids past cysteine 128 which is involved in interchain disulfide bond formation with the L chain. The truncated H chain associated with the L chain in the periplasm of E. coli to form a functional Fab molecule that bound in both enzyme-linked immunosorbent assay (ELISA) and immunofluorescence assay to O6 LPS. Therefore, the remainder of the C H 1 past cysteine 128 is not essential for stable formation of the Fab portion of MF23-1. This recombinant Fab (r-Fab) was shown to be specific for the LPS of the most predominant clinical isolate, serotype O6, while no cross-reactivity was detected to the LPS of the other 19 remaining serotypes. This r-Fab was also expressed on the surface of filamentous phage upon addition of helper phage to recombinant E. coli containing phagemid. Recombinant phage from clones MT13 and MT24 bound specifically to O6 LPS in ELISA. These results represent an important step toward the design of therapeutic Abs to be used against P. aeruginosa infections.

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Functional properties of isotype-switched immunoglobulin M (IgM) and IgG monoclonal antibodies to Pseudomonas aeruginosa lipopolysaccharide

Cited by 25 publications

References 26 publications

Disseminated Burkholderia gladioli infection in a lung transplant recipient with underlying hypocomplementemic urticarial vasculitis

Disseminated Burkholderia gladioli infection in a lung transplant recipient with underlying hypocomplementemic urticarial vasculitis

Problems in using statistical analysis of replacement and silent mutations in antibody genes for determining antigen‐driven affinity selection

Phage display and bacterial expression of a recombinant Fab specific for Pseudomonas aeruginosa serotype O6 lipopolysaccharide

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