Bacterial Immunoglobulin-Binding Proteins (eBook)

Applications in Immunotechnology

Michael D. P. Boyle (Herausgeber)

eBook Download: PDF

2014 | 1. Auflage
494 Seiten
Elsevier Science (Verlag)
978-1-4832-1653-9 (ISBN)

Infos

Bacterial Immunoglobulin-Binding Proteins: Applications in Immunotechnology, Volume 2 covers the state of knowledge of bacterial immunoglobulin-binding proteins. The book focuses on practical approaches to isolation, characterization, and use of bacterial immunoglobulin-binding proteins. The majority of these studies involve the type I Fc-binding protein (staphylococcal protein A) and the type III Fc-binding protein (streptococcal protein G). Physiological chemists, pediatricians, and microbiologists will find the book invaluable.

Inhalt

Front Cover 1
Bacterial Immunoglobulin-Binding Proteins: Applications in Immunotechnology 4
Copyright Page 5
Table of Contents 6
Contributors 16
Preface 18
Chapter 1. Introduction to bacterial immunoglobulin-binding proteins 20
I. Introduction 20
II. The Distribution and Functional Reactivity of Bacterial IgG Fc-Binding Proteins 22
III. Bacterial IgG-Binding Proteins 23
IV. Second Generation Immunoglobulin-Binding Proteins 34
V. Summary 37
References 37
Chapter 2. Detection and enhancement of expression of bacterial cell surface immunoglobulin-binding proteins 42
I. Introduction 42
II. Preparation of Bacteria 43
III. Standardization of Bacteria 44
IV. Assays for the Detection of Immunoglobulin-Binding Proteins 45
V. Direct Binding of Immunoglobulins to Bacteria 48
VI. Direct Binding Assay 49
VII. Absorption of IgG by Bacteria 50
VIII. Dot Blot Procedure 53
IX. Methods to Enhance Immunoglobulin-Binding Proteins 56
X. Mouse Passage 56
XI. Colony Blot Selection 58
XII. Storage of Strains 64
XIII. Conclusions 65
References 66
Chapter 3. Extraction and monitoring of soluble immunoglobulin-binding proteins 68
I. Introduction 68
II. Extraction Procedures 69
III. Secreted IgG-Binding Proteins 74
IV. Summary 87
Acknowledgment 88
References 88
Chapter 4. Isolation and functional characterization of bacterial immunoglobulin-binding proteins 90
I. Introduction 90
II. Selection of Immunoglobulin Source to Prepare Affinity Columns 91
III. Nature of the Sample to Be Purified 92
IV. Selection of Eluting Agent 93
V. Affinity Purification of a Type III Fc-Binding Protein Solubilized by Bacteriophage Lysis of the Group C Streptococcus 26RP66 94
VI. Characterization of Affinity-Purified Immunoglobulin-Binding Proteins 96
VII. Comparison of Functional Activities of Fc-Binding Proteins 101
VIII. Summary 106
References 107
Chapter 5. Determination of protein-binding affinities among bacterial cell surface proteins 110
I. Introduction 110
II. Binding of Mammalian Proteins to Bacterial Surfaces: Screening Procedures 111
III. Solubilization of Immunoglobulin-Binding Bacterial Surface Proteins 112
IV. Determination of Immunoglobulin-Binding Protein in Low Concentrations 115
V. Analysis of the Binding Immunoglobulins and Other Host Proteins to Purified, Bacterial Surface Proteins 116
VI. Determination of the Affinity Constant for Binding between a Bacterial Cell Wall Protein and Its Ligand 119
Acknowledgments 123
References 123
Chapter 6. Production of polyclonal antibodies to immunoglobulin-binding proteins 124
I. Introduction 124
II. Selection of the Species of Animal to Immunize 124
III. Preparation of Immunogen and Immunization 126
IV. Kinetics of Antibody Production 127
V. Detection of Antibody to Immunoglobulin-Binding Proteins 129
VI. Conclusion 142
References 142
Chapter 7. Use of radiolabeled bacterial Fc-binding proteins as tracers for soluble antigens 144
I. Introduction 144
II. Competitive Inhibition Radioimmunoassay 146
III. Summary 161
References 161
Chapter 8. Application of enzyme-labeled IgG-binding proteins in immunoassay 164
I. Introduction 164
II. Types of Assays 166
III. Preparation of Immunoglobulin Fc-Binding Protein-Enzyme Conjugate Tracers 168
IV. Development of an ELIS A to Quantify Human IgA Using a Type III Fc-Binding Protein-Alkaline Phosphatase Conjugate as Tracer 171
V. Summary 178
References 179
Chapter 9. Use of Fc-binding proteins to identify cell surface and secreted antigens associated with group B streptococci 180
I. Introduction 180
II. Group B Streptococcal Typing Nomenclature 181
III. Two-Stage Radioimmunoassay for Detection of Group B Streptococcal Type-Specific Antigens 182
IV. Adaptation of the Two-Stage RIA to a Dot Blot Assay 191
V. Adaptation of the Two-Stage RIA to an ELISA Typing Procedure 194
VI. Summary 196
References 196
Chapter 10. Application of Fc-binding proteins for the detection of specific antibodies 200
I. Introduction 200
II. Development of an Assay for Antibodies to a Soluble Antigen 202
III. Detection of Antibodies to Tumor-Associated Antigens 205
IV. Detection of Rabbit IgM Antibodies to Sheep Erythrocytes 209
V. Summary 213
References 214
Chapter 11. Use of fluorescent-conjugated bacterial immunoglobulin-binding proteins 216
I. Standard Methods 216
II. Conjugation Method Using GMBS 219
III. Comparison of Recombinant Protein G to Wild Type Protein G Isolated from Streptococcus Cell Membranes 220
References 222
Chaper 12. Biotinylated IgG-binding proteins—doubly versatile 224
I. Introduction 224
II. Biotinylation of IgG-Binding Protein 227
III. Immunohistochemical Staining Using Biotinylated IgG-Binding Proteins 228
Acknowledgments 233
References 233
Chapter 13. Use of IgG-binding proteins in immunoelectronmicroscopy 236
I. Introduction 236
II. Preparation of Colloidal Gold 236
III. Coupling of Proteins to Colloidal Gold 240
IV. Use of Gold-Labeling for Localization of Immunoglobulin-Binding Sites and Antigen-Antibody Complexes in Bacteria 244
V. Double Labeling Techniques with Different Sizes of Colloidal Gold to Localize Two Different Antigens on Thin Sections 250
VI. Streptavidin/Avidin-Biotin Labeling for Detection of Immunoglobulin-Binding Proteins 255
VII. Replica Method with Plasma Polymerization Film by Glow Discharge for Three-Dimensional Demonstration of Colloidal Gold Particles 259
VIII. General Applications of Colloidal Gold Labeling 265
References 265
Chapter 14. The use of bacterial Fc-binding proteins as probes for antigen–antibody complexes immobilized on nitrocellulose membranes 268
I. Dot Blot Assay 269
II. Colony and Plaque Blotting of Antigens Expressed by Bacteria 277
III. Western Blot Analysis 282
IV. Summary 288
Acknowledgments 289
References 289
Chapter 15. Application of bacteria expressing immunoglobulin-binding proteins to immunoprecipitation reactions 292
I. Introduction 292
II. General Background 293
III. Preparation of Bacterial Immunosorbent Reagents 294
IV. Practical Applications Using Bacterial Immunosorbents 298
V. Summary 306
Acknowledgments 306
References 306
Chapter 16. Use of bacteria expressing immunoglobulin-binding proteins in coagglutination assays 310
I. Introduction 310
II. Detection of Cell-Bound Antigens 312
III. Detection of Specific Antibody 313
IV. Procedure for Establishing a Coagglutination Assay to Measure a Polyvalent Soluble Antigen 315
V. Summary 317
References 317
Chapter 17. Utilization of whole bacteria expressing IgG-binding proteins to detect cell surface antigens 320
I. Introduction 320
II. Reagents and Equipment 321
III. Preparation of Antibodies 323
IV. Preparation of Anti-Immunoglobulin-Coated Bacteria 323
V. Preparation of Hybridoma Antibody-Coated Bacteria 324
VI. Binding Assay 324
VII. Staining and Quantitation 325
VIII. Variations on the Theme 326
IX. Comments 326
Acknowledgments 327
References 327
Chapter 18. Use of immobilized protein A to purify immunoglobulins 328
I. Introduction 328
II. Overview of Purification Procedure 332
III. Choice of Ligand 339
IV. Choice of Matrix 340
V. Immobilization Procedure 341
VI. Available Binding Capacity 342
VII. Column Preparation 343
VIII. Sample Preparation 345
IX. Sample Application 346
X. Elution Procedures 347
XI. Collection and Detection Methods 348
XII. Column Reequilibration, Reuse, and Storage 348
XIII. Limitations of Method 349
XIV. General Methods Using Protein A Sepharose CL-4B and Protein A Sepharose 4 Fast Flow for Mouse and Human IgG Purification 351
References 356
Chapter 19. Purification and quantitation of monoclonal antibodies by affinity chromatography with immobilized protein A 360
I. Purification of IgG1 Monoclonal Antibodies 360
II. Purification of IgM Monoclonal Antibodies 362
III. Quantitation of Monoclonal Antibodies 364
IV. Purification of Injectable-Grade Monoclonal Antibodies 365
V. Conclusions 371
Acknowledgments 372
References 372
Chapter 20. Use of immobilized protein G to isolate IgG 374
I. Introduction 374
II. Determination of Optimal Conditions for Protein G Affinity Chromatography 376
III. Examples of Affinity Chromatography Using Protein G Agarose 378
IV. Use of Protein G Agarose to Make an Antigen-Binding Column 382
V. Summary 385
Acknowledgments 386
References 386
Chapter 21. Bacterial immunoglobulin-binding proteins and complement 388
I. Introduction 388
II. Measurement of Functional Complement Activity 390
III. Detection of Classical Pathway Complement Activity 391
IV. Measurement of the Functional Activity of the Alternate Complement Pathway 397
V. Application of Functional Complement Titrations to Measurement of Activity of Immunoglobulin-Binding Proteins 398
VI. Measurement of the Generation of Complement Split Products 399
VII. Measurement of Complement Split Products Generated as a Consequence of Complement Activation Mediated by Bacterial Immunoglobulin-Binding Proteins 405
VIII. Studies of Binding of the First Component of Complement 406
IX. Antigenic Determination of Complement Activation 407
X. Analysis of Complexes Formed between Bacterial Immunoglobulin-Binding Proteins and IgG 407
XI. Summary 408
Acknowledgment 409
References 409
Chapter 22. Activation and differentiation of human lymphocytes by bacterial Fc-binding proteins 412
I. Introduction 412
II. Lymphocyte Isolation and Purification 413
III. Assays for Lymphocyte Proliferation 415
IV. Assays of Lymphocyte Differentiation 417
V. Conclusion 422
References 422
Chapter 23. Measurement of in vivo leucocyte chemotaxis mediated by Fc-binding proteins 424
I. Introduction 424
II. Air Sac Procedure 425
III. Use of Fc-Binding Proteins in the Air Sac Procedure 429
IV. Advantages and Limitations of the Air Sac Procedure 432
References 433
Chapter 24. The cloning of streptococcal protein G genes 436
I. Colony Immunoassay 436
II. Streptococcal Clinical Isolates 438
III. Preparation of Streptococcal DNA 438
IV. Initial Gene Cloning 439
V. Cloning of Protein G Genes from Other Isolates 442
References 443
Chapter 25. Bacterial immunoglobulin-binding proteins— future trends 444
I. Introduction 444
II. Role of Bacterial Immunoglobulin-Binding Proteins in Pathogenicity 448
III. Structure–Function Relationships of Bacterial Fc-Binding Proteins 449
IV. Applications Involving Immunoglobulin-Binding Proteins—Future Trends 461
V. Summary 466
References 467
Appendix 472
I. General Buffers 472
II. lodination Buffers and Related Solutions 474
III. ELISA Buffers and Related Solutions 475
IV. Electrophoresis Buffers 475
V. Buffers for Use in Applications Involving Nitrocellulose 477
VI. General Buffers and Reagents 478
Index 480

Produkt-Details

• Erscheint lt. Verlag: 10.5.2014
• Sprache: englisch
• Themenwelt: Sachbuch/Ratgeber ► Gesundheit / Leben / Psychologie ► Krankheiten / Heilverfahren
• Themenwelt: Medizin / Pharmazie ► Allgemeines / Lexika
• Themenwelt: Medizin / Pharmazie ► Medizinische Fachgebiete ► Allgemeinmedizin
• Themenwelt: Studium ► Querschnittsbereiche ► Infektiologie / Immunologie
• ISBN-10: 1-4832-1653-5 / 1483216535
• ISBN-13: 978-1-4832-1653-9 / 9781483216539