The dust mite Lepidoglyphus destructor is the dominating source of allergens giving rise to asthma and rhinitis among farmers. In a previous study of the localization of allergens in L. destructor we demonstrated that the 39 kDa allergen is associated with digestion. Here we describe the localization of the principal 15 kDa allergen and the high molecular weight allergen complex (79 and 93 kDa) in L. destructor with confocal laser scanning microscopy (CLSM). Cryostat-cut sections of mite bodies and faecal pellets were probed with mouse monoclonal antibodies (MoAbs) raised against the allergens. The 15 kDa allergen disclosed labelling of the mite body and most of the faecal pellets but left the exoskeleton unlabelled. The binding was widespread, and most intense in the mouth region. However, some staining was also observed around the gastrointestinal tract. In contrast, the 79 and 93 kDa allergen complex stained the exoskeleton and the front part of the mite. Interestingly, we detected no labelling of the faecal pellets with the MoAb against the 79/93 kDa allergen. The study indicates that the 15 kDa allergen is associated with the digestive tract whereas the function of the 79 and 93 kDa allergen complex remains to be elucidated.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1111/j.1365-2222.1995.tb01091.x | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
A novel immunoinformatic approach for design and evaluation of heptavalent multiepitope foot-and-mouth disease virus vaccine.
BMC Vet Res
March 2025
Department of Chemistry, Faculty of Science, Cairo University, Giza, 12613, Egypt.
Background: Foot-and-mouth disease virus (FMDV) vaccine development can be a laborious task due to the existence of various serotypes and lineages and its quasi-species nature. Immunoinformatics provide effective and promising avenue for the development of multiepitope vaccines against such complex pathogens. In this study, we developed an immunoinformatic pipeline to design a heptavalent multi-epitope vaccine targeting circulating FMDV isolates in Egypt.
View Article and Find Full Text PDFEffects of chemical modifications on allergenicity and functional properties of silkworm pupae proteins.
Food Chem
February 2025
School of Public Health, Health Science Center, Shenzhen University, Shenzhen 518060, Guangdong Province, PR China. Electronic address:
Silkworm pupae proteins (SPP) have been exploited as a new functional protein, but there are still some people who are allergic to it. This study investigated the effects of different chemical modifications (phosphorylation, succinylation, deamidation, glycosylation) on SPP's allergenicity and its structural and functional impact. Spectroscopic analysis showed that all three modifications except glycosylation loosened the three-dimensional structure of SPP.
View Article and Find Full Text PDFEffects of Heat Treatment on Physicochemical Properties of Lam. Leaf Protein.
Int J Mol Sci
February 2025
College of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
leaves represent a novel and nutritious food. Prior research has demonstrated that leaves can elicit allergic responses in BALB/c mice. Based on these findings, further studies were conducted to investigate the effects of heat treatment on the allergenicity, particle size, zeta potential, total sulfhydryl (TSH) content, hydrophilicity and hydrophobicity, ultraviolet spectrum, and intrinsic fluorescence spectrum of leaf protein.
View Article and Find Full Text PDFStructural and Stability Analysis of GRP Family Allergens Pru p 7 and Cry j 7, Which Cause Pollen and Food Allergy Syndrome.
Biomolecules
February 2025
Laboratory of Protein Science, Graduate School of Life Science, Hokkaido University, Sapporo 060-0810, Hokkaido, Japan.
Cry j 7 is a 7 kDa cysteine-rich gibberellin regulatory protein (GRP) with six disulfide bonds. It was isolated from Japanese cedar as the pollen allergen in this study. It exhibits cross-reactivity with food allergens such as Pru p 7 from peach and causes pollen-food allergy syndrome (PFAS).
View Article and Find Full Text PDFPollen Metabolome Insights, Allergenicity, and Dispersal in Response to Climate Change Variables.
Metabolites
February 2025
Plant Biotechnology and Molecular Pharming Lab, Department of Biosciences, COMSATS University Islamabad (CUI), Islamabad 45550, Pakistan.
: is a tree-producing allergenic pollen that grows in varied climatic conditions worldwide and causes pollen allergies in susceptible humans. This study aimed to investigate pollen morphology, pollen metabolome, pollen allergenicity, and climate change's impact on the plant habitat suitability in the future. : Tree pollen was collected in spring from different regions of Pakistan.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!