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Glycobiology of Innate Immunology 2022 ed. [Hardback]

  • Formāts: Hardback, 656 pages, height x width: 235x155 mm, weight: 1172 g, 1 Illustrations, black and white; XIX, 656 p. 1 illus., 1 Hardback
  • Izdošanas datums: 01-Apr-2022
  • Izdevniecība: Springer Verlag, Singapore
  • ISBN-10: 9811690804
  • ISBN-13: 9789811690808
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  • Formāts: Hardback, 656 pages, height x width: 235x155 mm, weight: 1172 g, 1 Illustrations, black and white; XIX, 656 p. 1 illus., 1 Hardback
  • Izdošanas datums: 01-Apr-2022
  • Izdevniecība: Springer Verlag, Singapore
  • ISBN-10: 9811690804
  • ISBN-13: 9789811690808
Citas grāmatas par šo tēmu:

This book presents the latest knowledge and the most recent research results on glycobiology of innate immunology. Innate immunity is the crucial part of the immunological defense system that exerts their distinct functions through binding to certain functional glycoproteins. They play a role in various human diseases and also function against microbial invaders and self-associated molecular patterns. Co-regulated expression of glycan-binding is associated with many biological components such as cellular oncotransformation, phenotype change, neuronal or embryonic development, regulation of cell division, cell–cell interaction, cell attachment, adhesion, and motility, and intracellular signaling via protein–carbohydrate or carbohydrate–carbohydrate interactions.

This book opens by providing the key background on glycans in innate immunity and its mechanisms behind the Dendritic cell interactions during infection and inflammation are examined in depth, and the concluding chapter is devoted to signaling tumor immunotherapy. Up-to-date information is then presented on all aspects of glycan structure-recognizing signaling. The book should assist in the further development of new strategies against emerging infectious agents and intractable diseases.


1 Repertoire in Innate Immunity
1(36)
1.1 Historical Expansion of Defense System
1(2)
1.2 Columbus Era to Modern Revolution in Immunological Defense System
3(2)
1.3 Historical Profile of Defense Constituents and Progress in Innate Immune Repertoire
5(19)
1.3.1 Phagocytosis
5(1)
1.3.2 Leukocytes
5(3)
1.3.3 Neutrophils
8(1)
1.3.4 Granulocytes
8(1)
1.3.5 Monocytes and Macrophages
9(2)
1.3.6 Dendritic Cells
11(2)
1.3.7 Complement System
13(5)
1.3.8 Opsonization
18(1)
1.3.9 Lysozyme and Salvarsan
19(2)
1.3.10 Progress in Innate Immune Response Since Historic Spanish Flu
21(3)
1.4 The Outline of Innate Immunity
24(6)
1.4.1 Concept of Immune Receptors
25(3)
1.4.2 Host Protection from Microbial Invaders of Innate Immunity
28(2)
1.5 Autophagy from Microbial Invaders and Self-Associated Molecular Patterns (SAMPs) of Innate Immune Cells
30(1)
References
31(6)
2 Dendritic Cells (DCs) in Innate Immunity
37(16)
2.1 General Biology of DCs
37(3)
2.2 Classification and Different Function of DCs
40(9)
2.2.1 pDC, Lymphoid Organ CD8α+ DC, and Tissue CD 103+DC Interaction with Tregs
43(1)
2.2.2 DCs Induce Tolerance State
44(1)
2.2.3 DC co-Stimulatory Receptors
45(3)
2.2.4 Application of DCs to Human Diseases
48(1)
References
49(4)
3 Glycan Biosynthesis in Eukaryotes
53(62)
3.1 General Glycosylation Events
54(2)
3.2 Sugar Nucleotide Transporters Deliver Donor Saccharides to ER-Golgi Network
56(2)
3.3 Golgi Traffic
58(2)
3.4 N-glycan Synthesis
60(1)
3.5 O-glycosylation and Multiple O-Glycan Structures
61(3)
3.5.1 7 Core O-glycan Structures
61(2)
3.5.2 Modification of 7 Core O-Glycan Structures
63(1)
3.6 O-GlcNAcylation, O-Mannosylation, O-β-Glucosylation, O-α-Fucosylation, O-β-Glucosylation, O-β-Galactosylation, C-Glycosylation, and C-Mannosylation
64(4)
3.6.1 O-GlcNAcylation
64(1)
3.6.2 O-Mannosylation
64(1)
3.6.3 O-β-Glucosylation
65(1)
3.6.4 O-α-Fucosylation
65(1)
3.6.5 OvGlucosylation
66(1)
3.6.6 O-β-Galactosylation
67(1)
3.6.7 C-Mannosylation and C-Glycosylation
67(1)
3.7 Function of O-Glycosylation and O-Glycans
68(1)
3.8 Glycosaminoglycans (GAGs)
69(20)
3.8.1 Classification and Biosynthesis of GAGs
70(1)
3.8.2 Chondroitin Sulfate (CS)
71(10)
3.8.3 Dermatan Sulfate (DS)
81(3)
3.8.4 Keratan Sulfate (KS)
84(1)
3.8.5 Heparin and Heparan Sulfate
85(1)
3.8.6 Hyaluronic Acid (HA) or Hyaluronan
86(1)
3.8.7 Proteoglycans (PGs)
86(2)
3.8.8 Extracellular PGs
88(1)
3.9 Glycosylphosphatidylinositols (GPIs) Anchor Glycosylation
89(14)
3.9.1 General Structure of GPI Anchors
89(2)
3.9.2 Function of GPI-Anchored Protein
91(4)
3.9.3 Biosynthesis, Structural Assembly, and Transportation of GPI-Anchored Protein
95(2)
3.9.4 GPIs in Parasites
97(2)
3.9.5 GPI Interaction with TLRs in Malaria P. falciparum
99(4)
3.9.6 GPI-Defected Disorders of Paroxysmal Nocturnal Hemoglobinuria (PNH) and Prion Disease
103(1)
References
103(12)
4 Glycans in Glycoimmunology
115(84)
4.1 Glycans in Cell Recognition and Evolutionary Adaptation in Organisms
115(1)
4.2 Changes in Glycan Structure Involved in Coregulated Expression of Glycan-Binding Lectin Counterparts
116(1)
4.3 Evolution of Lectin: Alternative Splicing Contributes to Variation for Glycan-Binding Receptors
117(1)
4.4 E-Selectin-Binding Ligand sLex (CD15s) on Neutrophil CD44 N-glycan and Alternatively Spliced Exon 6 Contains Core 2 O-Glycan sLea (CD44v6) Epitope
118(1)
4.5 Glycans Regulate T Cells
119(17)
4.5.1 Glycans Regulate Development and Differentiation in T Cells
121(3)
4.5.2 Glycosylation of Notch Receptor Signaling for Thymocyte β Selection and T Cell Function Regulation
124(1)
4.5.3 Alternatively Spliced Variants Produce Different Glycan Structures of CD43 and CD45 Isoforms in T Cells
125(3)
4.5.4 T Cells CD43 and CD45 Interaction with Their Counter-Receptor or Lectins to Determine T Cell Fates
128(2)
4.5.5 TCR Glycosylation Governs Hyper-response and Autoimmune Responses in T Cells and Tregs
130(2)
4.5.6 SAMP and N-Glycan-Dependent Modulation of Inhibitory T Cell Receptors to Suppress T Cell Functions
132(2)
4.5.7 Galectins in Suppression of T Cell Functions
134(1)
4.5.8 Glycans Regulate T Cell-Mediated Immune Suppression and Tolerance in Tumor Progression
135(1)
4.6 Abnormal N-Glycosylation in Autoimmunity
136(1)
4.7 Glycan Regulation of NK Cell Receptors
137(8)
4.7.1 NCRs on NK Cells
138(1)
4.7.2 NCRLigands
139(2)
4.7.3 Interaction of NCRs Ligands with Pathogens
141(1)
4.7.4 Interaction of NCRs Ligands with Self-Ligands
142(1)
4.7.5 NK Cells MHC-I-Independent Inhibitory Receptors Siglec-7 and Siglec-9
143(2)
4.8 Carbohydrate Recognition of Target Antigens by DCs During Infection and Inflammation
145(7)
4.8.1 Lewis Ligand Recognition by DCs
146(3)
4.8.2 VIM Ceramide Dodecasaccharide
149(3)
4.9 Glycan-Specific Trafficking Receptors in DC Maturation
152(2)
4.10 Glycan Ligands in Trafficking of DC Migration
154(4)
4.10.1 sLex-PSGL-1 Glycans in DC Trafficking
154(2)
4.10.2 Ganglioside Recognition by DC Receptors in Trafficking
156(2)
4.11 Chemokine Receptors in DC Trafficking
158(6)
4.11.1 Chemokine
158(1)
4.11.2 Chemokine Receptor
159(1)
4.11.3 Chemokine-GAG Interaction as a Type of Protein-Glycan Interactions
159(1)
4.11.4 Molecular Motifs in Chemokine for GAG Recognition
160(2)
4.11.5 C-C Type Chemokine Receptor 4 (CCR4) and Specific Ligand 17 (CCL17) and Specific Ligand 22 (CCL22)
162(2)
4.12 Glycan Structure-Recognizing Selectins in DC-Endothelium Interaction During Infection and Inflammation
164(11)
4.12.1 3 Species of Selectins: E-, L-, and P-selectins
165(3)
4.12.2 Representative Selectin Ligand PSGL-1 and Role of PSGL-1 O-Glycan
168(1)
4.12.3 Glycosyltransferases for Biosynthesis of PSGL-1 O-Glycan
169(2)
4.12.4 Designation of Carbohydrate Glycomimetic Drugs and Natural Inhibitors of Selectins
171(1)
4.12.5 Glycomimetic Drug Candidates
172(2)
4.12.6 GAG-Glycomimetic Drugs
174(1)
References
175(24)
5 Pathogen-Host Infection Via Glycan Recognition and Interaction
199(62)
5.1 Lectin Recognition of Glycans on Cell Surface and Soluble Glycans
199(5)
5.2 Innate Immune-Specific and Host Defensing Lectins of Fungal, Protozoa, Invertebrate, and Lower Vertebrates
204(2)
5.3 How Do Hosts Interact with Pathogens?
206(12)
5.3.1 Lectin-Carbohydrate Interaction
206(3)
5.3.2 Bacterial Glycoconjugates Interact with Host Lectins
209(9)
5.4 Pathogen-Producing Lectins as Receptors to Bind to the Host Carbohydrates
218(18)
5.4.1 Uropathogenic E. coli (UPEC), Enterohemorrhagic E. coli (EHEC), and Enterotoxigenic E. coli (ETEC)
220(8)
5.4.2 Lectins and Glycans of Other Pathogenic Bacteria
228(5)
5.4.3 Viral Lectins or Host Lectin-Binding Glycans
233(3)
5.5 Host Lectin Defense Mechanisms in Lectin-Carbohydrate Interactions
236(2)
5.6 Pathogenic Glycans to Trigger Innate Immune Enhancement
238(5)
5.6.1 Example 1: Polysaccharides with Immune Enhancement of Cyrtomium macrophyllum
240(1)
5.6.2 Example 2: Activation of Macrophage by Polysaccharide from Paecilomyces cicadae
240(1)
5.6.3 Example 3: NK Cell-Mediated Cytotoxicity Increased by Arabinogalactan from Anoectochilus formosanus
241(1)
5.6.4 Example 4: Streptococcus pneumonia Polysaccharides Activate NK Cells, NK-Like T Cells, and Monocytes
242(1)
5.6.5 Example 5: C. macrophyllum Polysaccharides (CMP) Enhance Lymphocyte Proliferation and Macrophage Function
242(1)
5.7 TLR4 Receptor-Activating Glycans Activate NO Production in Macrophage
243(1)
5.8 CBPs or GBPs in Antigen Recognition
244(1)
References
245(16)
6 Innate Immunity Via Glycan-Binding Lectin Receptors
261(50)
6.1 Glycosylation Effect on Autoimmunity and Inflammation
262(4)
6.1.1 Glycosylation in Immunological Recognition and Inflammation
262(1)
6.1.2 Glycosylation Effect on Autoimmunity
263(3)
6.2 Glycosylation Effect on Tumor Immunity of Immune Cells
266(2)
6.3 Immune Tolerance and Defense Mechanisms of Innate Immune DCs During Infection
268(2)
6.4 How Are Pathogenic Bacteria Recognized by Receptors of DCs of the Host Immune System?
270(22)
6.4.1 DC Lectins for Glycan Recognition of Invasive Agents
270(3)
6.4.2 Toll-Like Receptors
273(5)
6.4.3 Innate Immune Receptors in Malaria Infection
278(9)
6.4.4 Innate Immunity Receptors in Protozoan Parasite Toxoplasma gondii
287(5)
6.5 Pathogen Recognition and Adaptive Immune Responses in Acquired Immunity
292(3)
6.6 Galactose-Specific C-Type Lectin: Two Major ASGPR and Macrophage Galactose Lectin (MGL) in the Human
295(2)
References
297(14)
7 Sialic Acid-Binding Ig-Like Lectins (Siglecs)
311(186)
7.1 PolySia and Host Sialic Acids Modulate Host Immune Responses as Pathogenic Decoys
313(3)
7.2 Sialic Acid Recognition by Siglecs for Self-or Nonself-Antigens
316(2)
7.3 Classification of Siglecs
318(3)
7.4 Evolution of Siglecs, Sialic Acids, and Sialic Acid O-Acetylation as Host Ligands (Receptors) for Microbes and Innate Immunity
321(1)
7.5 Microbial Sialic Acid-like Molecules Synthesis and Recognition of Microbial Sialic Acids by DCs and Bacteriophages
322(3)
7.6 Hematopoietic System in Siglecs
325(2)
7.7 Structure of Siglecs
327(7)
7.7.1 Cytoplasmic ITIM and IT AM Domains of Siglecs
327(2)
7.7.2 Adaptor Proteins Associated with Siglecs
329(1)
7.7.3 SA-Recognition Tropism of Siglecs
330(4)
7.8 Inhibitory Signaling of DCs
334(4)
7.9 Siglec-1 (CD169, Sialoadhesin/Sn)
338(8)
7.9.1 General SAbinding Specificity of Siglec-1
338(3)
7.9.2 Siglec-1 Is a Pathogen-Binding Receptor
341(2)
7.9.3 Siglec-1 Recognizes HIV and Is a Transinfection Receptor Expressed on mDCs
343(3)
7.10 CD22/Siglec-2
346(20)
7.10.1 General and Structural Aspects of CD22/Siglec-2
346(3)
7.10.2 CD22 I Associated with Development of Autoimmune Diseases
349(2)
7.10.3 CD22 Function in Immune Tolerance Events
351(3)
7.10.4 Role of CD22 (Siglec-2, Mice Siglec-G) in Immune Responses
354(3)
7.10.5 Model Ligands for Recognition of CD22 on B Cells
357(1)
7.10.6 B Cell-Targeted Immunotherapy Through CD22-Positive Targeting of B-Cell Lymphomas
357(2)
7.10.7 Immune Tolerance Capacity of Neu5Ac-α2,6-Gal Ligands in DCs by ST6Gal-l of Tumor Cells for Immunesurveillance
359(1)
7.10.8 CD22 Vs. Pathogens
360(1)
7.10.9 CD22 Application with CAR-T on Acute Lymphoblastic Leukemia (ALL)
361(1)
7.10.10 CD22/Siglec-2 Coreceptor, CD45 on T Cells
362(4)
7.11 Siglec-4/Myelin-Associated Glycoprotein (MAG)
366(4)
7.11.1 General Aspects of MAG/Siglec-4
366(1)
7.11.2 Siglec-4/MAG in the CNS and Brain Development
367(2)
7.11.3 Siglec-4/MAG in Hippocampal Long-Term Potentiation
369(1)
7.12 Siglec-15, Non-CD33-Related Siglecs in Humans
370(3)
7.12.1 The Structure and Expression of Siglec-15, Called Misnomer "CD33L3" in Humans
370(2)
7.12.2 DAP12-Syk Pathway in Siglec-15-Mediated Remodeling of the Tumor Microenvironment
372(1)
7.12.3 Siglec-15 Functions in Osteoclastogenesis
372(1)
7.13 Siglec-3 (CD33)-Related Siglecs on DCs
373(74)
7.13.1 Siglec-3 (CD33)
374(1)
7.13.2 Structure, Natural Ligand, and Cellular Signaling with SHP-1/-2 of Siglec-3/CD33
375(2)
7.13.3 Pathogen Ligand for CD33
377(1)
7.13.4 Siglec-3/CD33 Is Related to SOCS3 and Internalization of CD33
378(1)
7.13.5 Putative Functions of Siglec-3/CD33 in Alzheimer's Disease (AD)
379(2)
7.13.6 Siglec-3-/CD33-Based Immunotherapy for AML
381(1)
7.13.7 Siglec-5/CD170 as a CD33-Related Siglec
382(6)
7.13.8 Siglec-6 as a CD33-Related Siglec
388(2)
7.13.9 Siglec-7 (CD328) as a CD33-Related Siglec
390(9)
7.13.10 Siglec-8 as a CD33-Related Siglec and Siglec-F as a Mouse Paralog
399(4)
7.13.11 Siglec-9 as a CD33-Related Siglec and Murine Functional Counterpart, Siglec-E
403(21)
7.13.12 Siglec-10 (Mouse Ortholog Siglec-G) in Humans as a CD33-Related Siglec
424(9)
7.13.13 Human Siglec-11 as a CD33-Related Siglec
433(5)
7.13.14 Siglec-14 in Humans as a CD33-Related Siglec
438(7)
7.13.15 Siglec-16 as a CD33-Related Siglec Is a Paired Receptor with Siglec-11
445(2)
7.14 Mouse CD33-Related Siglecs with ITIM-Like Domains
447(12)
7.14.1 mSiglec-E that Belongs to CD33-Related Siglecs
448(3)
7.14.2 Siglec-F (Human Paralog Siglec-8) as a CD33-Related Siglec
451(3)
7.14.3 Human Siglec-10 and Mouse Ortholog Siglec-G as CD33-Related Siglecs
454(3)
7.14.4 Siglec-H as a CD33-Related Siglec
457(2)
References
459(38)
8 C-Type Lectin (C-Type Lectin Receptor)
497(60)
8.1 Evolutionary Diversity of C-Type Lectins
497(2)
8.2 Ca2+-Dependent Glycan-Binding CTLs
499(3)
8.3 Myeloid CTL-Like Receptor or Myeloid-Suppressive or Inhibitory CLR (MICL), CLEC 12A
502(2)
8.4 Macrophage Inducible CTLR (Mincle, Clec4e, ClecSf9)/Macrophage CTL (MCL, CLEC4d, ClecSfS)
504(6)
8.4.1 Expression and Ligand-Binding Specificity of Mincle, Clec4e, ClecSf9, and MCL
504(1)
8.4.2 Pathogenic PAMPs-Recognition of Mincle and MCL
505(2)
8.4.3 Thl/Thl7 Activation and T Cell Development in Mincle or MCL Interaction with Host
507(3)
8.5 Mannose Receptor (MR) as CLR and Macrophage Mannose Receptor
510(5)
8.5.1 Structural Basis and Functions of MR
510(2)
8.5.2 MR Expression in Immune Systems and Interaction with Helminth Flatworm Trematodes
512(2)
8.5.3 Recognition of Pathogenic Microbes by MR
514(1)
8.6 Mannose (or Mannan)-Binding Protein (MBP) and Mannose-Binding Lectin (MBL)
515(5)
8.6.1 Structural Basis and Glycan Ligand Binding Specificity of MBL
516(1)
8.6.2 Immunoprotective Activity of MBL
517(2)
8.6.3 MBL Function in Diseases
519(1)
8.7 Fucose-Binding Lectin (FBL) and Ficolin
520(6)
8.7.1 Fucose-Binding Lectin (FBL) Diversity of F-Lectin Repertoires
520(1)
8.7.2 Specificity of Ficolins or FBL
521(2)
8.7.3 Ficolin Functions in the Immune Response
523(2)
8.7.4 Ficolin Interaction with Microorganisms
525(1)
8.8 Dectin 1 (CLEC-7A in Human)
526(7)
8.8.1 Basic Function and Structure of Dectin 1
526(1)
8.8.2 Dectin-1 Recognizes β1,3/β1,6-glycans in Fungi, Plants, Bacteria, and House Dust Mite
527(3)
8.8.3 Dectin-1 Cluster Includes CTL-Like Receptor 2 (CLEC-2)
530(1)
8.8.4 CLEC Structures and Ligand Recognition
531(2)
8.9 DC-Associated CTL-2 (Dectin-2) Family or CLEC4n
533(4)
8.9.1 Structural Basis and Function of Dectin-2
533(2)
8.9.2 Langerhans Cell-Specific Expression of Dectin-2 and Interaction with Fungal High-Man Glycans
535(2)
8.10 Dectin-3 (Clec4D, Clecsf8, MCL, Macrophage CTL)
537(3)
References
540(17)
9 Galectins
557(28)
9.1 General and Structural Aspects of Galectins
557(9)
9.1.1 Biological Roles of Galectins
558(1)
9.1.2 Immunological Roles of Galectins
559(2)
9.1.3 Classification of Galectins
561(3)
9.1.4 Galectin Ligands in Proteins and Gangliosides
564(1)
9.1.5 Galectins in Lower Organisms such as Zebrafish or Marine Oyster
565(1)
9.2 Galectin-2
566(1)
9.3 Galectin-3 and - 8 Recognize GM3, But Not Galectin-4
567(3)
9.3.1 Galectin-3
567(3)
9.3.2 Galectin-8
570(1)
9.4 Galectin-1 and - 4 Bind to GM1, But Not GM3
570(6)
9.4.1 Galectin-4
570(1)
9.4.2 Galectin-1
571(5)
9.5 Galactine-9 and Galelctin-10
576(1)
References
576(9)
10 DC-SIGNs
585(22)
10.1 DC-Specific ICAM-3-Grabbing Non-integrin, DC-SIGNB (CD209)
585(8)
10.1.1 Molecular Characteristics of DC-SIGN
585(1)
10.1.2 General Signaling of DC-SIGN
586(3)
10.1.3 α2,6 Sialyl IgG Fc Function by DC-SIGN Receptor
589(1)
10.1.4 DC-SIGN Binds to Pathogens, Antigen, and Glycans
590(1)
10.1.5 DC-SIGN Role in DC-Mediated Viral Transmission by HIV-1
591(1)
10.1.6 DC-Mediated Immunosuppression by Mycobacteria
592(1)
10.1.7 DC-SIGN Recognizes Lewis Antigens Expressed in PMN
593(1)
10.2 Other DCs-Derived Receptors
593(9)
10.2.1 Dendritic Cell NK Lectin Group Receptor (DNGR-1; CLEC9A)
593(2)
10.2.2 CTL-Like Receptor-1 (CLEC-1)
595(2)
10.2.3 CTL-Like Receptor, CLEC12A, Known as Myeloid Inhibitory CTL-Like Receptor (MICL), CTL-Like Molecule-1 (CLL-1), DC-Associated CTL 2 (DCAL-2), and CD371
597(3)
10.2.4 CD161 (NKR-P1A)
600(2)
References
602(5)
11 Toll-Like Receptors (TLRs)
607(24)
11.1 TLR Molecular Structure, Subtypes, and Recognition Ligand
609(3)
11.2 Signal Initiation and Transduction of TLRs
612(2)
11.3 Glycosylation of TLRs
614(1)
11.4 General TLR Functions as Pathogen and Antigen Receptors on DCs
614(2)
11.5 TLR-9 as a CpG DNA Receptor
616(1)
11.6 TLR-3 as a dsRNA Receptor
617(1)
11.7 TLR-4 as the LPS Receptor
618(4)
11.7.1 Ligands of TRL4 Recognition
619(2)
11.7.2 MyD88-Dependent Pathway of TLR4
621(1)
11.7.3 MyD88-Independent Pathway of TLR4
621(1)
11.8 TLR11
622(3)
11.8.1 Three Major Domains and Binding Ligand of TLRll
623(1)
11.8.2 TLR 11 Intracellular Signal Transduction
624(1)
11.9 Inhibition of TLRs by Gangliosides
625(1)
References
626(5)
12 CD33 and CD33-Related Siglecs in Pathogen Recognition and Endocytosis of DC in the Innate Immune System
631
12.1 CD33 (Siglec-3)
631(5)
12.1.1 General Biology of CD33
631(4)
12.1.2 CD33 (Siglec-3)-Targeting of Acute Myeloid Leukemia (AML)
635(1)
12.1.3 CD33 (Siglec-3)-Targeting Treatment of Alzheimer's Disease (AD)
636(1)
12.2 CD33-Related Siglecs (CD33rSiglecs)
636(3)
12.2.1 Inhibitory CD33rSiglecs in Escape from Tumor and Bacterial Immunosurveillance
637(1)
12.2.2 Activating CD33rSiglecs
638(1)
12.3 Pathogenic Suppression of the Pathogen-Specific Host Immune Response
639(9)
12.3.1 Inhibitory Receptor CD200R and CD200: CD200R1 Signaling
640(2)
12.3.2 Pathogenic Decoy Ligands Neutralize Host Immunity Through Eliciting Host CD200-CD200R1 Inhibitory Signaling
642(6)
12.4 DCs Tumor Immunotherapy Through Sialyl Binding of DCsto T Cells
648(2)
References
650
Prof. Cheorl-Ho KimMolecular and Cellular Glycobiology Unit, Department of Biological Sciences, Sungkyunkwan University