Bla g 3: a novel allergen of German cockroach identified using cockroach-specific avian single-chain variable fragment antibody.
Khurana T1, Collison M1, Chew FT2, Slater JE3.Author information 1Laboratory of Immunobiochemistry, Division of Bacterial, Parasitic, and Allergenic Products, US Food and Drug Administration, Bethesda, Maryland.2Allergy and Molecular Immunology Laboratory, Department of Biological Sciences, National University of Singapore, Singapore.3Laboratory of Immunobiochemistry, Division of Bacterial, Parasitic, and Allergenic Products, US Food and Drug Administration, Bethesda, Maryland. Electronic address: jay.slater@fda.hhs.gov.AbstractBACKGROUND: The IgE response to cockroach allergens is thought to be associated with asthma. German cockroach (GCr) allergen extract is a complex mixture of allergens, and the identification and characterization of immunodominant allergens is important for the effective diagnosis and treatment of GCr-induced asthma.
Annals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology.Ann Allergy Asthma Immunol.2014 Feb;112(2):140-145.e1. doi: 10.1016/j.anai.2013.11.007. Epub 2013 Dec 5.
BACKGROUND: The IgE response to cockroach allergens is thought to be associated with asthma. German cockroach (GCr) allergen extract is a complex mixture of allergens, and the identification and characterization of immunodominant allergens is important for the effective diagnosis and treatment of GC
Pozzesi N1, Fierabracci A2, Liberati AM3, Martelli MP4, Ayroldi E1, Riccardi C1, Delfino DV1.Author information 1Section of Pharmacology, Toxicology and Chemotherapy, Department of Clinical and Experimental Medicine, University of Perugia, Perugia, Italy.2Research Laboratories, Ospedale Pediatrico Bambino Gesù, Research Institute (IRCCS), Rome, Italy.3Section of Onco-Hematology, Department of Clinical and Experimental Medicine, University of Perugia, Perugia, Italy.4Section of Hematology, Department of Clinical and Experimental Medicine, University of Perugia, Perugia, Italy.AbstractThe thymus is the primary organ responsible for de novo generation of immunocompetent T cells that have a diverse repertoire of antigen recognition. During the developmental process, 98% of thymocytes die by apoptosis. Thus apoptosis is a dominant process in the thymus and occurs through either death by neglect or negative selection or through induction by stress/aging. Caspase activation is an essential part of the general apoptosis mechanism, and data suggest that caspases may have a role in negative selection; however, it seems more probable that caspase-8 activation is involved in death by neglect, particularly in glucocorticoid-induced thymocyte apoptosis. Caspase-8 is active in double-positive (DP) thymocytes in vivo and can be activated in vitro in DP thymocytes by T-cell receptor (TCR) crosslinking to induce apoptosis. Caspase-8 is a proapoptotic member of the caspase family and is considered an initiator caspase, which is activated upon stimulation of a death receptor (e.g., Fas), recruitment of the adaptor molecule FADD, and recruitment and subsequent processing of procaspase-8. The main role of caspase-8 seems to be pro-apoptotic and, in this review, we will discuss about the involvement of caspase-8 in (1) TCR-triggered thymic apoptosis; (2) death receptor-mediated thymic apoptosis; and (3) glucocorticoid-induced thymic apoptosis. Regarding TCR triggering, caspase-8 is active in medullary, semi-mature heat-stable antigen(hi) (HAS(hi) SP) thymocytes as a consequence of strong TCR stimulation. The death receptors Fas, FADD, and FLIP are involved upstream of caspase-8 activation in apoptosis; whereas, Bid and HDAC7 are involved downstream of caspase-8. Finally, caspase-8 is involved in glucocortocoid-induced thymocyte apoptosis through an activation loop with the protein GILZ. GILZ activates caspase-8, promoting GILZ sumoylation and its protection from proteasomal degradation.
Cell death and differentiation.Cell Death Differ.2014 Feb;21(2):226-33. doi: 10.1038/cdd.2013.166. Epub 2013 Nov 22.
The thymus is the primary organ responsible for de novo generation of immunocompetent T cells that have a diverse repertoire of antigen recognition. During the developmental process, 98% of thymocytes die by apoptosis. Thus apoptosis is a dominant process in the thymus and occurs through either deat
Antimicrobial function of the GAPDH-related antimicrobial peptide in the skin of skipjack tuna, Katsuwonus pelamis.
Seo JK1, Lee MJ2, Go HJ2, Kim YJ3, Park NG4.Author information 1Department of Food Science and Biotechnology, Kunsan National University, Kunsan 573-701, Republic of Korea.2Department of Biotechnology, Pukyong National University, Busan 608-737, Republic of Korea.3West Vancouver Secondary School, 1750 Mathers Ave., West Vancouver, BC V7V 2G7, Canada.4Department of Biotechnology, Pukyong National University, Busan 608-737, Republic of Korea. Electronic address: ngpark@pknu.ac.kr.AbstractA 3.4 kDa of antimicrobial peptide was purified from an acidified skin extract of skipjack tuna, Katsuwonus pelamis, by preparative acid-urea-polyacrylamide gel electrophoresis and C18 reversed-phase HPLC. A comparison of the N-terminal amino acid sequence of the purified peptide with that of other known polypeptides revealed high sequence homology with the YFGAP (Yellowfin tuna Glyceraldehyde-3-phosphate dehydrogenase-related Antimicrobial Peptide); thus, this peptide was identified as the skipjack tuna GAPDH-related antimicrobial peptide (SJGAP). SJGAP showed potent antimicrobial activity against Gram-positive bacteria, such as Bacillus subtilis, Micrococcus luteus, Staphylococcus aureus, and Streptococcus iniae (minimal effective concentrations [MECs], 1.2-17.0 μg/mL), Gram-negative bacteria, such as Aeromonas hydrophila, Escherichia coli D31, and Vibrio parahaemolyticus (MECs, 3.1-12.0 μg/mL), and against Candida albicans (MEC, 16.0 μg/mL) without significant hemolytic activity. Antimicrobial activity of this peptide is heat-stable but salt-sensitive. According to the secondary structural prediction and the homology modeling, this peptide consists of three secondary structural motifs, including one α-helix and two parallel β-strands, and forms an amphipathic structure. This peptide showed neither membrane permeabilization ability nor killing ability, but did display a small degree of leakage ability. These results suggest that SJGAP acts through a bacteriostatic process rather than bactericidal one. SJGAP is another GAPDH-related antimicrobial peptide isolated from skipjack tuna and likely plays an important role for GAPDH in the innate immune defense of tuna fish.
Fish & shellfish immunology.Fish Shellfish Immunol.2014 Feb;36(2):571-81. doi: 10.1016/j.fsi.2014.01.003. Epub 2014 Jan 9.
A 3.4 kDa of antimicrobial peptide was purified from an acidified skin extract of skipjack tuna, Katsuwonus pelamis, by preparative acid-urea-polyacrylamide gel electrophoresis and C18 reversed-phase HPLC. A comparison of the N-terminal amino acid sequence of the purified peptide with that of other