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1.
Dis Aquat Organ ; 158: 143-155, 2024 May 30.
Article in English | MEDLINE | ID: mdl-38813855

ABSTRACT

Perkinsus olseni and P. marinus are classified as notifiable pathogens by the World Organisation for Animal Health and are known to cause perkinsosis in a variety of molluscs globally. Mass mortalities due to these parasites in farms and in the wild have been a recurrent issue. Diagnosis for these protozoans is currently done using Ray's fluid thioglycollate medium method followed by optical microscopy or molecular assays. Both require a high level of skill and are time-consuming. An immunoassay method would make the diagnosis of perkinsosis quicker and cheaper. The present study used mass spectrometry-based proteomics to investigate common hypothetical surface peptides between different geographical isolates of P. olseni, which could be used to develop immunoassays in the future. Two peptides were identified: POLS_08089, which is a 42.7 kDa peptide corresponding to the 60S ribosomal subunit protein L4; and POLS_15916, which is a conserved hypothetical protein of 55.6 kDa. The identification of peptides may allow the development of immunoassays through a more targeted approach.


Subject(s)
Alveolata , Animals , Protozoan Proteins/genetics , Protozoan Proteins/metabolism , Peptides/chemistry
2.
NPJ Precis Oncol ; 4: 24, 2020.
Article in English | MEDLINE | ID: mdl-32923684

ABSTRACT

Despite decades of study, the molecular mechanisms and selectivity of the biomolecular components of honeybee (Apis mellifera) venom as anticancer agents remain largely unknown. Here, we demonstrate that honeybee venom and its major component melittin potently induce cell death, particularly in the aggressive triple-negative and HER2-enriched breast cancer subtypes. Honeybee venom and melittin suppress the activation of EGFR and HER2 by interfering with the phosphorylation of these receptors in the plasma membrane of breast carcinoma cells. Mutational studies reveal that a positively charged C-terminal melittin sequence mediates plasma membrane interaction and anticancer activity. Engineering of an RGD motif further enhances targeting of melittin to malignant cells with minimal toxicity to normal cells. Lastly, administration of melittin enhances the effect of docetaxel in suppressing breast tumor growth in an allograft model. Our work unveils a molecular mechanism underpinning the anticancer selectivity of melittin, and outlines treatment strategies to target aggressive breast cancers.

3.
Nat Chem Biol ; 14(5): 516-524, 2018 05.
Article in English | MEDLINE | ID: mdl-29632412

ABSTRACT

Immunoglobulin G (IgG) glycosylation is essential for function of the immune system, but the genetic and environmental factors that underlie its inter-individual variability are not well defined. The Collaborative Cross (CC) genetic resource harnesses over 90% of the common genetic variation of the mouse. By analyzing the IgG glycome composition of 95 CC strains, we made several important observations: (i) glycome variation between mouse strains was higher than between individual humans, despite all mice having the same environmental influences; (ii) five genetic loci were found to be associated with murine IgG glycosylation; (iii) variants outside traditional glycosylation site motifs affected glycome variation; (iv) bisecting N-acetylglucosamine (GlcNAc) was produced by several strains although most previous studies have reported the absence of glycans containing the bisecting GlcNAc on murine IgGs; and (v) common laboratory mouse strains are not optimal animal models for studying effects of glycosylation on IgG function.


Subject(s)
Glycosylation , Immunoglobulin G/chemistry , Immunoglobulin G/genetics , Acetylglucosamine/chemistry , Aging , Animals , Fucose/chemistry , Gene Expression Regulation , Genetic Variation , Glycopeptides/chemistry , Humans , Mice , Mice, Inbred C57BL , Mice, Inbred NOD , Peptides/chemistry , Phenotype , Polysaccharides/chemistry , Quantitative Trait Loci
4.
Vaccine ; 28(3): 798-802, 2010 Jan 08.
Article in English | MEDLINE | ID: mdl-19879227

ABSTRACT

An understanding of the cross-neutralisation of snake venoms by antibodies is important for snake antivenom development. We investigated the cross-neutralisation of brown snake (Pseudonaja textilis) venom, taipan (Oxyuranus scutellatus) venom and death adder (Acanthophis antarcticus) with commercial antivenoms and monovalent anti-snake IgG, using enzyme immunoassays, in vitro clotting and neurotoxicity assays. Each commercial antivenom bound all three venoms, and neutralised clotting activity of brown snake and taipan venoms and neurotoxicity of death adder venom. The 'in-house' monovalent anti-snake venom IgG raised against procoagulant brown snake and taipan venoms, did not neutralise the neurotoxic effects of death adder venom. However, they did cross-neutralise the procoagulant effects of both procoagulant venoms. This supports the idea of developing antivenoms against groups of snake toxins rather than individual snake venoms.


Subject(s)
Antibodies, Neutralizing/immunology , Antivenins/immunology , Cross Reactions , Venoms/immunology , Animals , Australia , Blood Coagulation/drug effects , Elapidae , Enzyme-Linked Immunosorbent Assay , Immunoglobulin G/immunology , Neurons/drug effects , Rabbits
5.
Proc Natl Acad Sci U S A ; 105(3): 961-6, 2008 Jan 22.
Article in English | MEDLINE | ID: mdl-18195351

ABSTRACT

The thymus is essential for a functional immune system, because the thymic stroma uniquely supports T lymphocyte development. We have previously identified the epithelial progenitor population from which the thymus arises and demonstrated its ability to generate an organized functional thymus upon transplantation. These thymic epithelial progenitor cells (TEPC) are defined by surface determinants recognized by the mAbs MTS20 and MTS24, which were also recently shown to identify keratinocyte progenitor cells in the skin. However, the biochemical nature of the MTS20 and MTS24 determinants has remained unknown. Here we show, via expression profiling of fetal mouse TEPC and their differentiated progeny and subsequent analyses, that both MTS20 and MTS24 specifically bind an orphan protein of unknown function, Placenta-expressed transcript (Plet)-1. In the postgastrulation embryo, Plet-1 expression is highly restricted to the developing pharyngeal endoderm and mesonephros until day 11.5 of embryogenesis, consistent with the MTS20 and MTS24 staining pattern; both MTS20 and MTS24 specifically bind cell lines transfected with Plet-1; and antibodies to Plet-1 recapitulate MTS20/24 staining. In adult tissues, we demonstrate expression in a number of sites, including mammary and prostate epithelia and in the pancreas, where Plet-1 is specifically expressed by the major duct epithelium, providing a specific cell surface marker for this putative reservoir of pancreatic progenitor/stem cells. Plet-1 will thus provide an invaluable tool for genetic analysis of the lineage relationships and molecular mechanisms operating in the development, homeostasis, and injury in several organ/tissue systems.


Subject(s)
Epithelial Cells/metabolism , Pregnancy Proteins/metabolism , Stem Cells/immunology , Stem Cells/metabolism , Thymus Gland/embryology , Thymus Gland/metabolism , Animals , Antigens, Surface/genetics , Antigens, Surface/immunology , Biomarkers , Cell Line , Embryo, Mammalian/embryology , Embryo, Mammalian/immunology , Embryo, Mammalian/metabolism , Epithelial Cells/immunology , Epithelium/metabolism , Gene Expression Regulation , Gene Expression Regulation, Developmental , Humans , Membrane Glycoproteins/genetics , Membrane Glycoproteins/immunology , Mice , Pancreatic Ducts/metabolism , Pregnancy Proteins/genetics , Pregnancy Proteins/immunology , RNA, Messenger/genetics , Thymus Gland/immunology , Time Factors
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