We used ELISA and immunoblotting to investigate antigenic cross-reactivity in mice between third-stage larvae of Anisakis simplex and five other nematodes: the ascaridoids Ascaris suum, Toxocara canis and Hysterothylacium aduncum, and the nonascaridoids Trichinella spiralis and Trichuris muris. Two sera were raised against each species (including A. simplex, but excluding A. suum), by infection or by immunization with somatic antigens. Serum against A. suum was raised by immunization only. The reactivities of each serum with A. simplex somatic antigens (SA), excretion-secretion antigens (ES), pseudocoelomic fluid antigens (PF) and cuticular antigens (CA) were investigated. The results of ELISA indicated high antigenic cross-reactivity between A. simplex and the remaining ascaridoid nematodes, confirming that there is extensive antigenic similarity within this group of nematode parasites. Immunoblotting again confirmed the high degree of cross-reactivity between the SA of A. simplex and SAs of the other ascaridoids, although several A. simplex SA components in the 11-18 kDA range were only recognized by sera from mice infected with A. simplex. In addition, two A. simplex PF components of 22 and 27 kDA, were recognized only by sera from mice infected with, or immunized with the SA of, A. simplex. Finally, the anti-phosphorylcholine monoclonal antibody BH8 recognized only a small number of A. simplex antigens, indicating that phosphorylcholine epitopes are not significant contributors to the observed cross-reactivity with the other nematodes.
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http://dx.doi.org/10.1007/s004360050131 | DOI Listing |
Introduction: Varicella-Zoster virus (VZV) is a highly contagious alpha-herpes virus. The diagnosis of chickenpox remains a difficult task especially in cases of breakthrough chickenpox, so the development of reliable laboratory tests is necessary. The simplest and most sensitive serological test for detecting antibodies in human and animal sera is the passive hemagglutination reaction (PHAR).
View Article and Find Full Text PDFProtein Sci
February 2025
Department of Biotechnology and Bioengineering, Sandia National Laboratories, Livermore, California, USA.
Engineered monoclonal antibodies have proven to be highly effective therapeutics in recent viral outbreaks. However, despite technical advancements, an ability to rapidly adapt or increase antibody affinity and by extension, therapeutic efficacy, has yet to be fully realized. We endeavored to stand-up such a pipeline using molecular modeling combined with experimental library screening to increase the affinity of F5, a monoclonal antibody with potent neutralizing activity against Venezuelan Equine Encephalitis Virus (VEEV), to recombinant VEEV (IAB) E1E2 antigen.
View Article and Find Full Text PDFFood Chem
January 2025
College of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China. Electronic address:
Peanuts are highly nutritious but pose a significant risk of triggering food allergies. While heat treatment can reduce the allergenicity of many foods, it may also alter their structure, potentially impacting detection results. This study employed double antibody sandwich enzyme-linked immunosorbent assay (DAS-ELISA) and lateral flow immunochromatography (LFIA) to evaluate the allergen Ara h 3 following heat-moisture treatment.
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January 2025
Division of Hematology-Oncology, Department of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
Acquired aplastic anaemia (AA) is an autoimmune bone marrow failure disease resulting from a cytotoxic T-cell-mediated attack on haematopoietic stem and progenitor cells (HSPCs). Despite significant progress in understanding the T-cell repertoire alterations in AA, identifying specific pathogenic T cells in AA patients has remained elusive, primarily due to the unknown antigenic targets of the autoimmune attack. In this review, we will synthesize findings from several decades of research to critically evaluate the current knowledge on T-cell repertoires in AA.
View Article and Find Full Text PDFNat Commun
January 2025
Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, USA.
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