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1. Full Text Gastrointestinal Immune Response to the Shrimp Allergen Tropomyosin: Histological and Immunological Analysis in an Animal Model of Shrimp Tropomyosin Hypersensitivity
by Lam, Yin Fan and Tong, Ka Kui and Kwan, Kin Ming and Tsuneyama, Koichi and Shu, Shang-An and Leung, Patrick S.C and Chu, Ka Hou
International Archives of Allergy and Immunology, ISSN 1018-2438, 07/2015, Volume 167, Issue 1, pp. 29 - 40
Background: Shellfish hypersensitivity is among the most common food allergies. A murine model of IgE-mediated shrimp allergy has been established in our... 
Original Paper | Seafood allergy | Cytokines | Tropomyosin | Mucosal immunology | MUCOSAL IMMUNITY | REPORTED FOOD ALLERGY | MAST-CELLS | INTESTINE | IMMUNOLOGY | BALB/C MICE | MURINE MODEL | SYSTEMIC-ANAPHYLAXIS | ALLERGY | INFLAMMATION | ORAL TOLERANCE | EXPRESSION | Cell Proliferation | Shellfish | Ileum - immunology | CD4-Positive T-Lymphocytes - immunology | Cell Movement - immunology | Gastrointestinal Tract - immunology | RNA, Messenger - biosynthesis | Food Hypersensitivity - immunology | Immunoglobulin E - immunology | Female | Cytokines - genetics | Disease Models, Animal | Duodenum - immunology | Tropomyosin - immunology | Inflammation - immunology | Jejunum - immunology | Proteins - immunology | Animals | Apoptosis - immunology | Epithelial Cells - immunology | Mast Cells - cytology | Mice | Mice, Inbred BALB C | Eosinophils - cytology | Goblet Cells - cytology | Penaeidae - immunology | Seafoods | Food allergies | Immunology
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2. Full Text β-Arrestins negatively regulate the toll pathway in shrimp by preventing dorsal translocation and inhibiting dorsal transcriptional activity
by Sun, Jie-Jie and Lan, Jiang-Feng and Shi, Xiu-Zhen and Yang, Ming-Chong and Niu, Guo-Juan and Ding, Ding and Zhao, Xiao-Fan and Yu, Xiao-Qiang and Wang, Jin-Xing
Journal of Biological Chemistry, ISSN 0021-9258, 04/2016, Volume 291, Issue 14, pp. 7488 - 7504
The Toll signaling pathway plays an important role in the innate immunity of Drosophila melanogaster and mammals. The activation and termination of Toll... 
DEFENSE | FENNEROPENAEUS-CHINENSIS | SYNDROME VIRUS-INFECTION | SIGNALING PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENE-EXPRESSION | RECEPTOR | ANTIMICROBIAL PEPTIDES | CHINESE SHRIMP | DROSOPHILA | INNATE IMMUNITY | Cell Nucleus - immunology | DNA-Binding Proteins - immunology | Toll-Like Receptors - immunology | Arrestins - immunology | Arthropod Proteins - immunology | Extracellular Signal-Regulated MAP Kinases - immunology | Signal Transduction - immunology | Animals | beta-Arrestins | Staphylococcus aureus - immunology | Active Transport, Cell Nucleus - immunology | Phosphorylation - immunology | Penaeidae - immunology | extracellular-signal-regulated kinase (ERK) | Immunology | toll-like receptor (TLR) | innate immunity | arrestin | Staphylococcus aureus (S. aureus)
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3. Full Text Molecular cloning and functional characterization of a homolog of the transcriptional regulator CSL in Litopenaeus vannamei
by Zhao, Weiling and Yu, Zhixue and Aweya, Jude Juventus and Wang, Fan and Yao, Defu and Ma, Hongyu and Lun, Jingsheng and Zhang, Yueling
Developmental and Comparative Immunology, ISSN 0145-305X, 11/2018, Volume 88, pp. 152 - 160
The Notch signaling pathway transcriptional regulator, CSL (also called as CBF1, Suppressor of Hairless or Lag-1 in different species, generally designated as... 
Hemocytes proliferation | Immune resistance | Litopenaeus vannamei | LvCSL | PENAEID SHRIMP | DENDRITIC CELLS | NOTCH | IMMUNOLOGY | ADAPTIVE IMMUNITY | NEURAL STEM-CELLS | FISHERIES | ZOOLOGY | DISEASE | VIBRIO-ALGINOLYTICUS | INFECTION | DIFFERENTIATION | NF-KAPPA-B | Vibrio parahaemolyticus - immunology | Hemocytes - immunology | Arthropod Proteins - isolation & purification | Disease Resistance - immunology | Phylogeny | Vibrio Infections - immunology | Protein Domains - genetics | Gene Knockdown Techniques | Host-Pathogen Interactions - immunology | Cloning, Molecular | Fish Diseases - immunology | Protein Domains - immunology | Immunoglobulin J Recombination Signal Sequence-Binding Protein - genetics | Vibrio Infections - veterinary | Gene Expression Regulation - immunology | Penaeidae - genetics | Penaeidae - microbiology | Arthropod Proteins - genetics | Arthropod Proteins - immunology | Sequence Homology, Nucleic Acid | Vibrio Infections - virology | Sequence Alignment | Animals | Fish Diseases - virology | Immunoglobulin J Recombination Signal Sequence-Binding Protein - immunology | Immunoglobulin J Recombination Signal Sequence-Binding Protein - isolation & purification | Aquaculture | Hepatopancreas - immunology | Penaeidae - immunology | Immune response | Analysis | Cloning | Mortality | Genetic aspects | Genetic transcription | Cell differentiation | Health aspects | Mitogens
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4. Full Text Viral resistance and immune responses of the shrimp Litopenaeus vannamei vaccinated by two WSSV structural proteins
by Yang, Jr-Yun and Chang, Chin-I and Liu, Kuan-Fu and Hseu, Jinn-Rong and Chen, Li-Hao and Tsai, Jyh-Ming
Immunology Letters, ISSN 0165-2478, 2012, Volume 148, Issue 1, pp. 41 - 48
Highlights ► Shrimp were vaccinated using rVP28 or rVP36B and subsequently challenged with WSSV. ► Complete survival was induced from a higher rVP28 dose and a... 
Allergy and Immunology | Vaccine | Invertebrate immunity | White spot syndrome virus (WSSV) | Shrimp | PROCAMBARUS-CLARKII | IMMUNOLOGY | ENVELOPE PROTEINS | SERINE PROTEINASE | PENAEUS-JAPONICUS | SPOT-SYNDROME-VIRUS | CULTURED KURUMA SHRIMP | ORAL VACCINATION | PROTEOMIC ANALYSIS | MARSUPENAEUS-JAPONICUS | PACIFIC WHITE SHRIMP | Hemolymph - cytology | Superoxide Dismutase - genetics | Cell Count | Hemocytes - immunology | Disease Resistance - immunology | Monophenol Monooxygenase - metabolism | White spot syndrome virus 1 - genetics | Vaccination - methods | Gene Expression - immunology | Viral Envelope Proteins - metabolism | Penaeidae - metabolism | Monophenol Monooxygenase - genetics | Adaptive Immunity - immunology | Superoxide Dismutase - metabolism | White spot syndrome virus 1 - immunology | Recombinant Proteins - metabolism | Penaeidae - virology | Viral Envelope Proteins - genetics | Hemolymph - immunology | Electrophoresis, Polyacrylamide Gel | Hemolymph - metabolism | Immunity - immunology | Reverse Transcriptase Polymerase Chain Reaction | Viral Vaccines - administration & dosage | Immunity, Innate - immunology | Superoxide Dismutase - immunology | White spot syndrome virus 1 - metabolism | Animals | Monophenol Monooxygenase - immunology | Recombinant Proteins - immunology | Viral Envelope Proteins - immunology | Viral Vaccines - immunology | Hemocytes - cytology | Penaeidae - immunology | Virus diseases | Immune response | Messenger RNA | Vaccination
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5. Full Text Molecular Diagnosis of Shrimp Allergy: Efficiency of Several Allergens to Predict Clinical Reactivity
by Pascal, Mariona, PhD and Grishina, Galina, MS and Yang, Ariana C., MD, PhD and Sánchez-García, Silvia, MD and Lin, Jing, PhD and Towle, David, PhD and Ibañez, Maria Dolores, MD, PhD and Sastre, Joaquín, MD, PhD and Sampson, Hugh A., MD and Ayuso, Rosalia, MD, PhD
Journal of Allergy and Clinical Immunology: In Practice, ISSN 2213-2198, 2015, Volume 3, Issue 4, pp. 521 - 529.e10
Background The diagnosis of shellfish allergy remains a challenge for clinicians. Several shellfish allergens have been characterized and their IgE epitopes... 
Internal Medicine | Allergy and Immunology | Shellfish allergy | Epitope | Tropomyosin | Sarcoplasmic calcium-binding protein | Hemocyanin | Fatty-acid-binding protein | Arginine kinase | Microarray | Component-resolved diagnosis | DBPCFC | Troponin C | Myosin light chain | MACROBRACHIUM-ROSENBERGII | DUST-MITE | FOOD ALLERGY | IMMUNOLOGICAL ANALYSIS | PENAEUS-MONODON | IMMUNOLOGY | ALLERGY | CROSS-REACTIVITY | FRESH-WATER SHRIMP | PEANUT ALLERGY | CALCIUM-BINDING PROTEIN | Skin Tests | Shellfish | Humans | Tropomyosin - immunology | Food Hypersensitivity - blood | Arginine Kinase - immunology | Epitopes | Arthropod Proteins - immunology | Immunoglobulin E - blood | Animals | Food Hypersensitivity - immunology | Immunoglobulin E - immunology | Allergens - immunology | Recombinant Proteins - immunology | Calcium-Binding Proteins - immunology | Immunoglobulin G - immunology | Hemocyanins - immunology | Food Hypersensitivity - diagnosis | Penaeidae - immunology | Proteins | Food allergies | Crustaceans | Lactose | Peptides | Efficiency | Allergies | Binding sites | Cockroaches | Molecular weight
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6. Full Text Pattern recognition protein binds to lipopolysaccharide and β-1,3-glucan and activates shrimp prophenoloxidase system
by Amparyup, Piti and Sutthangkul, Jantiwan and Charoensapsri, Walaiporn and Tassanakajon, Anchalee
Journal of Biological Chemistry, ISSN 0021-9258, 03/2012, Volume 287, Issue 13, pp. 10060 - 10069
The prophenoloxidase (proPO) system is activated upon recognition of pathogens by pattern recognition proteins (PRPs), including a lipopolysaccharide-and... 
BLACK TIGER SHRIMP | MANDUCA-SEXTA | FENNEROPENAEUS-CHINENSIS | GRAM-NEGATIVE BACTERIA | LIPOTEICHOIC ACID | BIOCHEMISTRY & MOLECULAR BIOLOGY | PENAEUS-MONODON | LITOPENAEUS-VANNAMEI | TOBACCO HORNWORM | MOLECULAR-CLONING | INNATE IMMUNITY | Antimicrobial Cationic Peptides - immunology | Catechol Oxidase - immunology | Glucans - immunology | Vibrio - immunology | Enzyme Precursors - genetics | Lipopolysaccharides - metabolism | Antimicrobial Cationic Peptides - metabolism | Lipopolysaccharides - immunology | Vibrio Infections - metabolism | Enzyme Activation - immunology | Vibrio - metabolism | Lectins - metabolism | Vibrio Infections - genetics | Penaeidae - metabolism | Catechol Oxidase - genetics | Glucans - metabolism | Antimicrobial Cationic Peptides - genetics | Lectins - immunology | Vibrio - genetics | Enzyme Precursors - immunology | Penaeidae - microbiology | Glucans - pharmacology | Arthropod Proteins - genetics | Arthropod Proteins - immunology | Enzyme Activation - drug effects | Enzyme Precursors - metabolism | Animals | Catechol Oxidase - metabolism | Lipopolysaccharides - pharmacology | Arthropod Proteins - metabolism | Protein Binding | Lectins - genetics | Enzyme Activation - genetics | Penaeidae - immunology | Pattern Recognition Protein | Phenoloxidase | Carbohydrate-binding Protein | RNA Interference (RNAi) | Pathogen-associated Molecular Pattern (PAMP) | β-Glucan | Enzymology | Shrimp | Lipopolysaccharide (LPS) | Pattern Recognition Receptor
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7. Full Text Protection of Penaeus monodon against White Spot Syndrome Virus by Oral Vaccination
by Jeroen Witteveldt and Carolina C. Cifuentes and Just M. Vlak and Mariëlle C. W. van Hulten
Journal of Virology, ISSN 0022-538X, 02/2004, Volume 78, Issue 4, pp. 2057 - 2061
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
SHRIMP | GENOME SEQUENCE | JAPONICUS | VIROLOGY | MAJOR STRUCTURAL PROTEINS | GENE | WSSV | RESISTANCE | INFECTION | IDENTIFICATION | FABRICIUS | Penaeidae - virology | Viral Envelope Proteins - genetics | Administration, Oral | Vaccination | Viral Vaccines - genetics | Escherichia coli - immunology | DNA Viruses - immunology | Animals | Escherichia coli - genetics | Viral Envelope Proteins - immunology | Genetic Vectors | Viral Vaccines - immunology | Aquaculture | Penaeidae - immunology | Vaccines and Antiviral Agents | infection | shrimp | identification | gene | fabricius | wssv | genome sequence | major structural proteins | japonicus | resistance
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8. Full Text Immunization with hypoallergens of shrimp allergen tropomyosin inhibits shrimp tropomyosin specific IgE reactivity
by Wai, Christine Y. Y and Leung, Nicki Y. H and Ho, Marco H. K and Gershwin, Laurel J and Shu, Shang An and Leung, Patrick S. C and Chu, Ka Hou
PLoS ONE, ISSN 1932-6203, 11/2014, Volume 9, Issue 11, pp. e111649 - e111649
Designer proteins deprived of its IgE-binding reactivity are being sought as a regimen for allergen-specific immunotherapy. Although shrimp tropomyosin (Met e... 
BIRCH POLLEN ALLERGEN | MOLECULAR CHARACTERIZATION | ANTIBODIES | MURINE MODEL | FOOD ALLERGY | MULTIDISCIPLINARY SCIENCES | MOUSE MODEL | ORAL IMMUNOTHERAPY | IDENTIFICATION | CALCIUM-BINDING PROTEIN | EPITOPES | Tropomyosin - genetics | Immunoglobulin G - blood | Humans | Molecular Sequence Data | Epitopes - immunology | Food Hypersensitivity - immunology | Immunoglobulin E - immunology | Allergens - immunology | Antibody Specificity - immunology | Immunoglobulin G - immunology | Allergens - chemistry | Female | Disease Models, Animal | Amino Acid Sequence | Immunization | Tropomyosin - immunology | Allergens - genetics | Epitopes - genetics | Proteins - immunology | Proteins - genetics | Sequence Alignment | Animals | Recombinant Proteins - immunology | Epitopes - chemistry | Mice | Mutation | Proteins - chemistry | Penaeidae - immunology | Allergens | Allergy | Analysis | Immunoglobulin E | Amino acids | Muscle proteins | Allergic reaction | Enzyme-linked immunosorbent assay | Antigenic determinants | Protein binding | Pediatrics | Animal models | Shellfish | Immunoglobulin G | Antibodies | Construction sites | Mollusks | Allergenicity | Proteins | Reduction | Crustaceans | Anaphylaxis | Clonal deletion | Immunotherapy | Deletion | Life sciences | Mathematical models | Binding | Food allergies | Immunoglobulins | Tropomyosin | Hypersensitivity | Rheumatology | Epitopes | Patients | Medicine | Reactivity | Mutagenesis | Site-directed mutagenesis | Computer applications | Degranulation | Passive cutaneous anaphylaxis | Index Medicus
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9. Full Text Prophenoloxidase system and its role in shrimp immune responses against major pathogens
by Amparyup, Piti and Charoensapsri, Walaiporn and Tassanakajon, Anchalee
Fish and Shellfish Immunology, ISSN 1050-4648, 04/2013, Volume 34, Issue 4, pp. 990 - 1001
The global shrimp industry still faces various serious disease-related problems that are mainly caused by pathogenic bacteria and viruses. Understanding the... 
Phenoloxidase | proPO system | Penaeus | Melanization | Shrimp | ProPO system | CRAYFISH PACIFASTACUS-LENIUSCULUS | BLACK TIGER SHRIMP | PATTERN-RECOGNITION RECEPTOR | HOLOTRICHIA-DIOMPHALIA LARVAE | IMMUNOLOGY | FRESH-WATER CRAYFISH | PENAEUS LITOPENAEUS VANNAMEI | FISHERIES | INDUCED MELANIN SYNTHESIS | MARINE & FRESHWATER BIOLOGY | PRO-PHENOL-OXIDASE | VETERINARY SCIENCES | VECTOR ANOPHELES-GAMBIAE | BETA-1,3-GLUCAN BINDING-PROTEIN | Host-Pathogen Interactions | Immunity, Innate - immunology | Catechol Oxidase - immunology | Animals | Receptors, Pattern Recognition - immunology | Enzyme Precursors - immunology | Melanins - immunology | Serine Endopeptidases - immunology | Penaeidae - enzymology | Aquaculture | Penaeidae - immunology | Proteins | Genetic engineering | Pathogenic microorganisms | Immune response | Proteases | Health aspects | Index Medicus
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10. Full Text Two host gut-derived lactic acid bacteria activate the proPO system and increase resistance to an AHPND-causing strain of Vibrio parahaemolyticus in the shrimp Litopenaeus vannamei
by Chomwong, Sudarat and Charoensapsri, Walaiporn and Amparyup, Piti and Tassanakajon, Anchalee
Developmental and Comparative Immunology, ISSN 0145-305X, 12/2018, Volume 89, pp. 54 - 65
Lactic acid bacteria (LAB) are group of beneficial bacteria that have been proposed as relevant probiotics with immunomodulatory functions. In this study, we... 
Probiotic | Vibrio parahaemolyticus | proPO system | Lactic acid bacteria | Immunity | Shrimp | Catechol Oxidase - immunology | Vibrio parahaemolyticus - immunology | Enzyme Precursors - genetics | Seafood | Lactobacillales - immunology | Phylogeny | Vibrio Infections - immunology | Penaeidae - enzymology | Host-Pathogen Interactions - immunology | Lactobacillus plantarum - immunology | Catechol Oxidase - genetics | Vibrio Infections - veterinary | Enzyme Precursors - immunology | Penaeidae - microbiology | Arthropod Proteins - genetics | Lactobacillus plantarum - genetics | Arthropod Proteins - immunology | Gastrointestinal Microbiome - genetics | Immunity, Innate | Vibrio parahaemolyticus - pathogenicity | Lactobacillales - genetics | Probiotics | Enzyme Precursors - metabolism | Animals | Host-Pathogen Interactions - genetics | Catechol Oxidase - metabolism | Arthropod Proteins - metabolism | Enzyme Activation | Gastrointestinal Microbiome - immunology | Aquaculture | Penaeidae - immunology | Medical research | Drug resistance in microorganisms | RNA | Analysis | Medicine, Experimental | Bacteria | Genetic engineering
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11. Full Text T cell epitope immunotherapy ameliorates allergic responses in a murine model of shrimp allergy
by Wai, C. Y. Y and Leung, N. Y. H and Leung, P. S. C and Chu, K. H
Clinical & Experimental Allergy, ISSN 0954-7894, 03/2016, Volume 46, Issue 3, pp. 491 - 503
BackgroundShellfish allergy is one of the most common food hypersensitivities worldwide but allergen-specific immunotherapy for shellfish allergy is not yet... 
shellfish | T cell epitopes | Met e 1 | peripheral tolerance | peptide immunotherapy | allergen‐specific immunotherapy | Th1/Th2 balance | Peripheral tolerance | Allergen-specific immunotherapy | Shellfish | Peptide immunotherapy | PEPTIDE-IMMUNOTHERAPY | FOOD ALLERGY | MAST-CELLS | IMMUNOLOGY | PEANUT ORAL IMMUNOTHERAPY | B-CELLS | CYTOKINE PRODUCTION | ALLERGY | DNA IMMUNIZATION | MOUSE MODEL | IGE ANTIBODY-FORMATION | IMMUNE TOLERANCE | allergen-specific immunotherapy | Epitope Mapping | Immunoglobulin G - blood | Humans | Th1-Th2 Balance | Immunoglobulin E - blood | Food Hypersensitivity - immunology | Immunoglobulin E - immunology | Allergens - immunology | Antibody Specificity - immunology | Immunoglobulin G - immunology | Epitopes, T-Lymphocyte - immunology | Disease Models, Animal | Amino Acid Sequence | Immunization | Cytokines - metabolism | Peptides - chemistry | Peptides - immunology | Proteins - immunology | Epitopes, T-Lymphocyte - chemistry | Animals | Food Hypersensitivity - therapy | Biomarkers | Mice | Desensitization, Immunologic - methods | Penaeidae - immunology | Food allergy | Allergens | Peptides | Analysis | Immunotherapy | Immunoglobulin E | T cells | Muscle proteins | Antigenic determinants
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12. Full Text Molecular cloning, characterization and expression analysis of the tumor necrosis factor (TNF) superfamily gene, TNF receptor superfamily gene and lipopolysaccharide-induced TNF-α factor (LITAF) gene from Litopenaeus vannamei
by Wang, Pei-Hui and Wan, Ding-Hui and Pang, Li-Ran and