Phosphorycholine bearing components of some helminthic parasites: Localization to parasite lipoproteins

McWilliam, Andrew S.; Stewart, G.A.; Allen, William V.

doi:10.1016/0305-0491(86)90059-3

Cited by 7 publications

(2 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although some studies suggested that the parasite Pc carrier in N. brasiliensis was analogous to pneumo coccal C-substance [18], recent studies from our la boratory [12] with both N. brasiliensis and A. suum in dicate that lipoproteins may be the major carrier of Pc in helminthic parasites. These studies showed that low, high and very high density lipoproteins of both A. suum and N. brasiliensis with apparent molecular weights ranging from 470,000 to > 1 x 106 daltons contained Pc, with the majority being present in the very high density lipoprotein fraction (470,000-610,000 daltons).…”

Section: Discussionmentioning

confidence: 99%

An Immunochemical Investigation of the Allergens from <i>Ascaris suum </i>Perienteric Fluid

McWilliam¹,

Stewart²,

Turner³

1987

Int Arch Allergy Immunol

Self Cite

View full text Add to dashboard Cite

An extract of Ascaris suum perienteric fluid was fractionated on Sephadex G-200 and the resulting high molecular weight (approx. 600,000 daltons) and low molecular weight (approx. 16,000 daltons) fractions examined for allergenicity using human sera. Radioallergosorbent (RAST) and RAST-inhibition assays showed that the high molecular weight fraction was 15- to 40-fold more potent than the low molecular weight fraction. Crossed radio-immunoelectrophoretic analysis showed that the high molecular weight fraction contained 10 allergens in contrast to the 6 comprising the low molecular weight fraction. Polyacrylamide gel electrophoretic studies in combination with RAST indicated that two high molecular weight glycoprotein-staining components may be major allergens. A. suum cross-reacted allergenically with Toxocara canis and various life cycle stages of Nippostrongylus brasilliensis but not with Strongyloides ratti or Schistosoma mattheei. The cross-reacting allergens were predominantly of high molecular weight and the molecular weight distribution pattern obtained for A. suum, T. canis and N. brasilliensis paralleled that obtained for the distribution of the carrier of the hapten phosphorylcholine (Pc). However, it was shown that the hapten per se was not allergenic. In contrast, analysis of the allergens from N. brasilliensis using sera from rats infected with the same parasite showed that the homologous allergens were predominantly of low molecular weight (approx. 20,000 daltons) and did not contain Pc.

show abstract

Section: Discussionmentioning

confidence: 99%

An Immunochemical Investigation of the Allergens from <i>Ascaris suum </i>Perienteric Fluid

McWilliam¹,

Stewart²,

Turner³

1987

Int Arch Allergy Immunol

Self Cite

View full text Add to dashboard Cite

show abstract

“…The antibody response to phosphocholine (PC) 1 is biologically interesting because of the frequent expression of PC on pathogenic bacteria and nematodes where the haptenic epitope is coupled to a variety of carrier structures, including carbohydrates and proteins (9)(10)(11). The murine response to PC-protein is a well-characterized model system used to study the shift in specificity to include the carrier as the immune response progresses (7,(12)(13)(14)(15).…”

Section: Introductionmentioning

confidence: 99%

The Structural Basis of Repertoire Shift in an Immune Response to Phosphocholine

Brown¹,

Schumacher

Wiens³

et al. 2000

The Journal of Experimental Medicine

View full text Add to dashboard Cite

The immune response to phosphocholine (PC)–protein is characterized by a shift in antibody repertoire as the response progresses. This change in expressed gene combinations is accompanied by a shift in fine specificity toward the carrier, resulting in high affinity to PC–protein. The somatically mutated memory hybridoma, M3C65, possesses high affinity for PC–protein and the phenyl-hapten analogue, p-nitrophenyl phosphocholine (NPPC). Affinity measurements using related PC–phenyl analogues, including peptides of varying lengths, demonstrate that carrier determinants contribute to binding affinity and that somatic mutations alter this recognition. The crystal structure of an M3C65–NPPC complex at 2.35-Å resolution allows evaluation of the three light chain mutations that confer high-affinity binding to NPPC. Only one of the mutations involves a contact residue, whereas the other two have indirect effects on the shape of the combining site. Comparison of the M3C65 structure to that of T15, an antibody dominating the primary response, provides clear structural evidence for the role of carrier determinants in promoting repertoire shift. These two antibodies express unrelated variable region heavy and light chain genes and represent a classic example of the effect of repertoire shift on maturation of the immune response.

show abstract

Trichinella spiralis: Light microscope monoclonal antibody localization and immunochemical characterization of phosphorylcholine and other antigens in the muscle larva

Choy

Lim

1991

Experimental Parasitology

View full text Add to dashboard Cite

Phosphorycholine bearing components of some helminthic parasites: Localization to parasite lipoproteins

Cited by 7 publications

References 21 publications

An Immunochemical Investigation of the Allergens from <i>Ascaris suum </i>Perienteric Fluid

An Immunochemical Investigation of the Allergens from <i>Ascaris suum </i>Perienteric Fluid

The Structural Basis of Repertoire Shift in an Immune Response to Phosphocholine

Trichinella spiralis: Light microscope monoclonal antibody localization and immunochemical characterization of phosphorylcholine and other antigens in the muscle larva

Contact Info

Product

Resources

About