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  • 1
    Online Resource
    Online Resource
    Baton Rouge :Taylor & Francis Group,
    Keywords: Lectins. ; Electronic books.
    Description / Table of Contents: Introduces Groundbreaking Approaches for Assessing Lectin Function Lectins and their ligands are under quite a heavy microscope due to their potential applications to pharmacology, immunology, cancer therapy, and agriculture. With growing interest in the glycobiology field, the body of research related to lectin roles has grown at an explosive rate, particularly in the past 20 years. Animal Lectins: A Functional View presents the most up-to-date analysis of these carbohydrate-binding, and potentially lifesaving, proteins in one comprehensive volume. This standard-setting resource presents new insights into the biological roles of most animal lectins, including their function in infection prevention through innate immunity. It also discusses such lectin behaviors as: Glycoprotein folding Sorting and targeting Cell adhesion Embryogenesis Cell-cell interactions and signaling Describes the Structural Basis of Protein-Carbohydrate Interactions Under the editorial guidance of two leading protein chemistry experts and with contributions from well-recognized field authorities, this book logically and systematically discusses both intracellular and extracellular lectin functions. It is an essential springboard for future field research and a clear and concise knowledge base that glycobiology, biochemistry, and immunology researchers cannot afford to be without.
    Type of Medium: Online Resource
    Pages: 1 online resource (598 pages)
    Edition: 1st ed.
    ISBN: 9781420006971
    DDC: 572/.69
    Language: English
    Note: Front cover -- Contents -- Foreword -- Preface -- Editors -- Contributors -- Part I: Introduction -- Chapter 1. Introduction to Animal Lectins -- Part II: Modern Approaches for Assessing Lectin Function -- Chapter 2. Structural Aspects of Lectin-Ligand Interactions -- Chapter 3. Thermodynamic Approaches to the Study of Affinity of Clustered Carbohydrate Epitopes in Galectin- Glycoconjugate Interactions -- Chapter 4. Deciphering Lectin Ligands through Glycan Arrays -- Chapter 5. Chromatography and Related Approaches for Qualitative and Quantitative Analyses of Lectin Specificity -- Chapter 6. Analysis of Whole-Genome and Other Data Resources to Characterize the Molecular, Structural, and Evolutionary Diversity of C-Type Lectins and Discover New Genes -- Chapter 7. Animal Models for Assessing the Biological Roles of Lectins -- Part III: Glycoprotein Folding, Sorting and Secretion, Targeting, Degradation, and Clearance -- Chapter 8. Calreticulin and Calnexin as Chaperones in Glycoprotein Folding -- Chapter 9. Role of L-Type Lectins in Glycoprotein Sorting and Trafficking -- Chapter 10. P-Type Lectins and Lysosomal Enzyme Targeting -- Chapter 11. M-Type Lectins as Novel Components of Secretory Pathways -- Chapter 12. Functional Aspects of the Hyaluronan and Chondroitin Sulfate Receptors -- Part IV: Cell Adhesion and Cell Surface Lattice Formation -- Chapter 13. Galectin-3 and Cancer -- Chapter 14. Myelin-Associated Glycoprotein (Siglec-4): A Nervous System Lectin That Regulates Axon-Myelin Stability and Axon Regeneration -- Chapter 15. Hyaluronan-Binding Proteoglycans -- Chapter 16. Roles of Coral Lectins in Morphological Change of Zooxanthellae -- Part V: Cell-Cell Interactions, Signaling, and Transport -- Chapter 17. Siglecs: Roles in Cell-Cell Interactions and Signaling -- Chapter 18. Signaling through the Fungal -Glucan Receptor Dectin-1. , Chapter 19. CD22: A Regulator of B Cell Survival and Signal Transduction -- Chapter 20. Galectins and Integrins in Pre-B Cell Development -- Chapter 21. Golgi N-Glycan Processing and Galectin Functions -- Part VI: Recognition and Effector Functions in Innate Immunity -- Chapter 22. Mannan-Binding Lectin Polymorphisms and Infectious Diseases -- Chapter 23. Immunoregulatory Roles of Lung Surfactant Proteins A and D -- Chapter 24. C-Type Lectin Receptors on Dendritic Cells -- Chapter 25. Structural and Functional Roles of C-Type Lectin Receptors on Natural Killer Cells -- Chapter 26. Activation of Lepidopteran Insect Innate Immune Responses by C-Type Immulectins -- Chapter 27. Galectins as Novel Regulators of Immune Cell Homeostasis and Inflammation -- Chapter 28. Interactions of Galectins with Leukocytes -- Chapter 29. Regulation of Immune Responses by Galectin-3 -- Chapter 30. X-Lectins: A New Family with Homology to the Homology to the Xenopus leavis Oocyte Lectin XL35 -- Chapter 31. F-Type Lectins: A New Family of Recognition Factors -- Chapter 32. Biology of FREPs: Diversified Lectins with Fibrinogen-Related Domains from the Freshwater Snail Biomphalaria glabrata -- Chapter 33. Lectins in Sand Fly-Leishmania Interactions -- Chapter 34. Ficolins: The Structural Basis for Recognition Plasticity -- Chapter 35. Hemolytic Lectin in Marine Invertebrates -- Chapter 36. Structure-Function Relationship in Mammalian Chitinase-Like Lectins -- Index -- Back cover.
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 42 (1995), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . The oyster parasite Perkinsus marinus replicates in our medium consisting of Dulbecco modified Eagle's medium: Ham's F12 nutrient mixture (1:1) supplemented with 1–5% fetal bovine serum, with a doubling time of 24 hours during the exponential phase of the culture. Fetal bovine serum concentrations above 5% dramatically reduced parasite proliferation in a dose-dependent manner. We tested the individual effects of the three major protein components of fetal bovine serum (fetuin, transferrin and albumin) on the replication of the parasite in a serum-free medium. At the concentrations tested, fetuin enhanced parasite growth, whereas albumin had a modest positive effect and transferrin was inhibitory. Proteolytic digestion of fetuin, strongly diminished its growth-enhancing properties, indicating that the overall glycoprotein architecture may be required for activity. On the contrary, desialylation of fetuin slightly enhanced its growth-promoting activity. The addition of fetuin at 1.7 mg/ml to the serum-free DME: Ham's F12 medium yielded growth rates that are comparable to those obtained with our standard culture methodology. This has resulted in a fully defined culture medium that will allow for a rigorous characterization of excretory/secretory products involved in modulating or blocking the host's humoral and cellular defense mechanisms.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Perkinsus atlanticus cultures were established either with trophozoites isolated from fresh gills, with hypnospores isolated from tissues incubated in fluid thioglycollate medium, or directly from infected hemocytes of carpet shell clams Tapes decussatus from Algarve (Southern Portugal), using a culture medium and conditions optimized for Perkinsus marinus. Perkinsus atlanticus isolates were cloned by limiting dilution, and their identity unequivocally established by PCR-based species-specific diagnostic assays, and by sequencing the complete rRNA gene cluster. The rRNA gene cluster is 7.5-kb in length including 5S, IGS, SSU, ITS1, 5.8S, IS2, LSU, and an inter-cluster spacer. rDNA sequences of the P. atlanticus clone were between 98.3–100% identical to P. atlanticus sequences previously obtained from clam tissue (non-clonal) isolates. Based on the IGS sequences available from Perkinsus species, a set of primers was designed to amplify P. atlanticus and the two clonally cultured Perkinsus species (P. marinus and P. andrewsi) currently available from a recognized repository. This Perkinsus“genus-specific” PCR-based assay complements the species-specific assays developed earlier and strengthen the detection of Perkinsus species for which specific detection assays are not yet available.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 51 (2004), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . Perkinsus species are parasitic protozoa of mollusks, currently classified within the Perkinsozoa, a recently established phylum that is basal to the Apicomplexa and Dinozoa. Ribosomal RNA (rRNA) genes and their intergenic spacers have been used to support the taxonomy of Perkinsus species, the description of new species, and to develop molecular probes for their detection and identification. We previously described ultrastructure, behavior in culture, and partial sequence of the rRNA locus of a Perkinsus species isolated from the baltic clam Macoma balthica. The rRNA genes and intergenic spacers of this Perkinsus isolate differed from those described in the currently accepted species to a degree that led to its designation as a new species, Perkinsus andrewsi. In this study, we identify an additional rRNA gene unit (rRNA-B) in the P. andrewsi holotype, and report the complete sequences of both rRNA gene units. Except for the 5. 8S, all regions of the rRNA-B gene unit exhibited sequence differences from that initially described (rRNA-A). Each rRNA gene unit is arranged in a “head-to-tail” tandem repeat. This is the first report demonstrating two distinct rRNA units in a Perkinsus species.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 48 (2001), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . We established monoclonal in vitro cultures of a Perkinsus sp. isolated from the baltic clam Macoma balthica and compared morphological features of various life stages by light and transmission electron microscopy to those of the currently accepted Perkinsus species: Perkinsus marinus, Perkinsus olseni, Perkinsus atlanticus, and Perkinsus qugwadi. Except that trophozoites were slightly larger than those of P. marinus, and that they underwent zoosporulation in culture, observation of our isolate under light microscopy did not reveal striking differences from any Perkinsus species. Perkinsus sp. from M. balthica shared fine structural characteristics with other Perkinsus species that clearly place it within this genus. Although zoospores of Perkinsus sp. from M. balthica were slightly smaller than those from other species, the ultrastructural arrangement and appearance of the apical complex and flagella seem to be identical to those of P. marinus and P. atlanticus. Our isolate also appeared, in some sections, to have cortical alveolar expansions of the plasmalemma at regions other than the anterior end and lobulated mitochondria that were reported as unique for P. qugwadi. Little consensus exists among authors in the assignment of taxonomic weight to any particular morphological feature to designate Perkinsus species. The present study of gross morphology and ultrastructure was complemented with molecular studies reported elsewhere, which propose that Perkinsus sp. from Macoma balthica is a distinct species.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . A Perkinsus species was isolated from the baltic clam Macoma balthica and an in vitro culture established under conditions described for P. marinus. As reported previously, morphological features remarkable enough to clearly indicate that this isolate is a distinct Perkinsus species were lacking. In this study, regions of the rRNA locus (NTS, 18S. ITS1, 5.8S. and 1TS2) of this isolate were cloned, sequenccd, and compared by alignment with those available for other Perkinsus species and isolates. Sequence data from the rRNA locus and species-specific PCR assays indicated not only that Perkinsus sp. from M. balthica was not P. marinus, but it was different from P. atlanlicus and P. olseni. The degree of difference was comparable to or greater than differences between accepted Perkinsus species. In particular, NTS sequence and length were dramatically different from that of P. marinus and P. atlanlicus. Therefore, we formally propose to designate the Perkinsus sp. from M. balthica as a separate species, P. andrewsi n. sp. Primers based on P. andrewsi NTS sequence were used to develop a PCR-based diagnostic assay that was validated for species-specificity and sensitivity. PCR-based assays specific for cither P. andrewsi or P. marinus were used to test for their presence in bivalve species sympatric to M. balthica. Although isolated from M. balthica, P. andrewsi was also detected in the oyster Crassostrea virginica and clams Macoma mitchelli and Mercenaria mercenaria, and could coexist with P. marinus in all four bivalve species tested.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature structural biology 9 (2002), S. 628-634 
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Anguilla anguilla agglutinin (AAA), a fucolectin found in the serum of European eel, participates in the recognition of bacterial liposaccharides by the animal innate immunity system. Because AAA specifically recognizes fucosylated terminals of H and Lewis (a) blood groups, it has been used ...
    Type of Medium: Electronic Resource
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