14

INTRODUCTION

[3]

[3] A p p l i c a t i o n s o f A v i d i n - B i o t i n T e c h n o l o g y : Literature Survey

By MEIR WILCHEK and EDWARD A. BAYER Because of the extensive literature on avidin-biotin technology, we are presenting a survey of reference material to date in tabular form (see Ref. 1 in list at the end of this article). The tables are divided more or less according to the sections in this volume. In order to assist readers in understanding the details therein, a list of pertinent abbreviations is given in Table I. Table II presents the experimental details from studies which have used avidin columns for the isolation of target material. Native biotincontaining systems (e.g., biotin-requiring enzymes) could be isolated directly on such columns. The isolation of other materials, such as membrane proteins and glycoconjugates, is dependent on the mediation of a biotinylated binder, e.g., antibody or lectin. One of the problems in the use of avidin-biotin technology for isolation purposes is the difficulty encountered in eluting the bound material from the column. Therefore, elution conditions used in a given study are also listed in Table II. In some cases, avidin columns have been used for the selective elimination of a given protein or cell type, such that elution from the column was not required. Tables III, IV, and V provide information relating to cytochemical localization studies. These types of studies usually involve the microscopic visualization of membrane-based sites mediated through the avidin-biotin interaction. In some cases, target sites have been directly biotinylated using group-specific biotinylating reagents. In others, biotinylated lectins, hormones, antibodies, and other binders were employed to mediate between the target molecule and the avidin-probe conjugate or complex. In order to give readers an overall view of the various approaches used by different groups, we summarize in Tables III-V details of the biotinylated binder as well as the avidin-probe system. The use of protein blotting for identification and analysis of target molecules in complex mixtures of biological material centers on two basic approaches: (1) direct labeling of blotted material using biotinylating reagents and (2) indirect labeling using biotinylated binders. The staining methodologies developed have been used for blot transfers of material separated by SDS-PAGE or isoelectric focusing, as well as for direct METHODS IN ENZYMOLOGY. VOL. 184

Copyright .~ 1990 by Academic Press, Inc. AII rights of reproduction in any form reserved.

[3]

LITERATURESURVEY

15

detection of target material on dot blots. The biotinylation step may be carried out either in solution (before transfer to nitrocellulose) or directly on the blotted material. Details regarding the reagents, binders, and probes that have been used are listed in Tables VI and VII. One of the most prevalent uses of avidin-biotin technology in recent years has been for immunoassays. In many cases, the signal is enhanced 10-fold or more, owing to the four biotin-binding sites of avidin and the multiple biotinyl groups on the derivatized antibody. The approach is suitable for both monoclonal and polyclonal antibody preparations; any immunoglobulin class may be employed; the biotinylation step can be carried out either on the primary antibody or on a biotinylated secondary antibody system; both avidin-probe conjugates and complexes have been used; and sequential as well as homogeneous assays have been reported. Details of such immunoassay systems are given in Table VIII. Finally, one of the major reasons that avidin-biotin technology has gained prominence in the 1980s is its application to gene probing. Using a suitable probe, an individual nucleic acid segment can be detected from a large heterogeneous population. Today, most of the work in gene probe development deals with probe design and labeling procedures, and biotin can be introduced into the growing DNA chain through the use of a biotinylated nucleotide triphosphate in conjunction with nick-translation techniques. Alternatively, some of the reactive biotin-containing derivatives can be used for direct introduction of the biotin moiety into DNA. Synthetic oligonucleotides (20 to 30 bases in length), to which biotin residues have been introduced either on the 3' or 5' terminus, have also been successfully applied. Details of the various approaches for biotinylation of DNA and their application for hybridization are summarized in Table IX. It is clear that we could not include all of the "avidin-biotin" literature in Tables II-IX (even with the availability of computerized literature surveys, etc.), owing to (1)the many contributions in which the terms avidin or biotin are not included in the title or key words and (2) the unavailability of certain journals and books in the libraries at our disposal. Even if we could have compiled all of the pertinent literature, one would probably question the worth in the end, since the important aspects or relationships among the various entries would have been masked as a consequence of the volume of material presented. These tables thus serve as a starting point for the interested researcher.

16

INTRODUCTION TABLE I ABBREVIATIONSUSED JN TABLESII-IX

Abbreviation Ab MAb Abl, B-Ab2 MAbl, B-Ab2 ABC ABC (B-AP) ABC (B-HRP) acidP AP Av Av-AP Av-Fer Av-gold Av-HRP BBcapHZ BcapNHS BCHZ BHZ BNHS BNHS (SO3) B-dUTP B- 11-dUTP B-16-dUTP CHAPS Con A DBB ELISA EM FACS Fer FITC-Av FM fiG Gal ox. Glc ox. Gold GSI

Definition Antibody Monoclonal antibody Sequential use of polyclonal primary Ab and biotinylated secondary Ab Sequential use of monoclonal primary Ab and biotinylated secondary Ab Complexes formed by mixing native avidin with biotinylated probe (identified parenthetically) Complexes containing native avidin and biotinylated alkaline phosphatase Complexes containing native avidin and biotinylated peroxidase Acid phosphatase Alkaline phosphatase Avidin Avidin-conjugated alkaline phsophatase Avidin-conjugated ferritin Avidin-conjugated colloidal gold Avidin-conjugated peroxidase Covalently coupled biotin N-Biotinyl-6-aminocaproylhydrazide N-Biotinyl-6-aminocaproyl-N-hydroxysuccinimide ester Biocytin hydrazide (N6-biotinyl-L-lysine hydrazide) Biotin hydrazide Biotin N-hydroxysuccinimide ester Biotin N-hydroxy(sulfo)succinimide ester 5-(N-Biotinyl-3-aminoallyl)deoxyuridine 5'-triphosphate 5'[N-(3-Aminoallyl)-N'-biotinyl-6-aminocaproyl]deoxyuridine 5'-triphosphate 5'[N-(3-Aminoallyl)-N-(N-biotinyl 6-aminocaproyl)4-aminobutyryl]deoxyuridine 5'-triphosphate 3'[(3-Chloramidopropyl)dimethylammonio]-l-propane Concanavalin A p-Diazobenzoylbiocytin Enzyme-linked immunosorbent assay Electron microscopy Fluorescence-activated cell sorting (cell cytometry) Ferritin Fluorescein-derivatized avidin Fluorescence microscopy /3-Galactosidase Galactose oxidase Glucose oxidase Colloidal gold Lectin from Griffonia simplicifolia

[3]

[3]

17

L I T E R A T U R E SURVEY

TABLE I (continued) Abbreviation HRP IL-2 LM MPB PC PE Photobiotin RIA RITC-Av SBA SDS StABC StABC (B-AP) StABC (B-HRP) StAv StAv-AP StAv-Fer StAv-gold StAv-HRP WGA

Definition Peroxidase from horseradish Interleukin 2 Light microscopy 3-(N-Maleimid opropionyl)biocytin Penicillinase Phycoerythrin

N-(4-Azido-2-nitrophenyl)-N'-(N-biotinyl 3-aminopropyl)-N'-methyl1,3-propanediamine Radioimmunoassay Rhodamine-derivatized avidin Soybean agglutinin Sodium dodecyl sulfate Complexes formed by mixing native avidin with biotinylated probe (identified parenthetically) Complexes containing native streptavidin and biotinylated alkaline phosphatase Complexes containing native streptavidin and biotinylated peroxidase Streptavidin Streptavidin-conjugated alkaline phosphatase Streptavidin-conjugated ferritin Streptavidin-conjugated colloidal gold Streptavidin-conjugated peroxidase Wheat germ agglutinin

TABLE II ISOLATIONOF BIOLOGICALLYACTIVEMATERIALSUSINGAVIDIN COLUMNS Material purified Native biotin-containing systems B-transcarboxylase peptides Acetyl-CoA carboxylase aposubunits Apo(acetyl-CoA carboxylase) Transcarboxylase subunits B-polypeptides B-enzymes Propionyl-CoA carboxylase Acetyl-CoA carboxylase Mitochondrial carboxylases Sodium transport enzyme

Binder

None None None None None None None None None None

Elution conditions

Ref."

6 M Guanidine-HCl, pH 1.5 6 M Guanidine-HCl, pH2 Effluent fractions pooled Differential pH SDS-urea Biotin Biotin gradient Biotin Biotin gradient Biotin

2 3,4 5,6 7 8 9,10 11 12 13 14

(continued)

18

INTRODUCTION

[3]

TABLE I1 (continued) Material purified Membrane components and receptors lminobiotin-labeled membrane proteins and glycoproteins Surface glycoproteins Membrane antigens Terminal deoxynucleotidytransferase IgE receptor Estrogen receptor Glucocorticoid receptor Gonadot ropin-releasing hormone receptor Insulin receptor

Binder

Plasmid DNA Spliceosomes

Ref."

None

Acetate, pH 4

15,16

B-Con A B-MAb B-MAb B-IgE IgE, B - M A b B-estradiol B-dexamethasone B-GnRH

2% SDS SDS (boiling) 2 M MgCIe None SDS (boiling) Estradiol Dexamethasone CHAPS, Tris/glycerol, pH 5.5

17 18 19 20 21 22 23 24

Acetate, pH 5.0 1 M NaCl, biotin 5.0 M MgCl2 or SDS Enkephalin Glycine-HCl, pH 2.2

25 26 27 28 29

30 31 32 33 34 35 36

B-MAb B-MAb B-antigen

None None None None None None (1) Rosette formation, erythrocyte lysis (2) None (rosette formation) (3) Mechanical agitation Selection by FACS

37-39 40 41

B-RNA

None

42

B-RNA None None B-tRNA None None None

1 M NaOH 6 M Guanidine-HCl, pH 2.5 70% formic acid 99% formamide None 6 M Guanidine-HCl, pH 2.5 SS-reduction of cleavable biotin analog 0.1 M NaOH 90° in SDS

43,44 45 46 47 48 49 50,51

B-insulin B-insulin Lactogenic and somatogenic receptors B-growth hormone Opioid receptor B-enkephalin Cytomegalovirus hydrophobic proteins (1) B - M A b or glycoproteins (2) MAbl, B - A b 2 Selective retrieval or elimination of target material B-lectin or antibody None B-thymocytes None B-subunit of transcarboxylase None B-mitogen or inducer None B-enzymes None Daudi lymphoblasts B-MAb Lymphocyte subpopulations B-Ab

Human B lymphocytes (MAb-producing cells) Nucleic acids and associated complexes Drosophila DNA, sea urchin DNA, Leishmania DNA Drosophila DNA B-tRNA B - r R N A fragment (affinity-labeled) R loop structures B-DNA B-RNA B-nucleosomes

Elution conditions

B-DNA B-RNA

52 53

[3]

LITERATURE SURVEY

19

TABLE lI (continued) Material purified

Binder

Transcriptionally active B - D N A

None

Transcription factors Sequence-specific DNA-binding factor Recombinant plasmids

B-DNA B-DNA

Neisseria DNA

B-DNA, B - R N A

B-DNA

Elution conditions

Ref.

SS reduction of cleavable biotin analog Differential salt concentration Differential salt concentration

54

(1) SS reduction of cleavable biotin analog (2) Heat, low ionic strength, phenol extraction EDTA, 1 M NaCI, 0.1% SDS

57

" See reference list at end of article.

TABLE III DIRECT LABELING OF BIOLOGICALLY ACTIVE MATERIALS USING AVIDIN-BIOTIN TECHNOLOGY Target material

Biotin reagent

Probe

Comments

Ref."

(1) BNHS (2) Periodate/BHZ (3) Gal ox./BHZ

Av-Fer

EM

59

Periodate/BHZ

Av-Fer

EM

60-63

Biotin-tagged sites

Acholeplasma laidlawii membranes Erythrocyte ghosts Membrane sialic acids Intact erythrocytes and lymphocytes Thalassemic erythrocytes Membrane proteins

Acholeplasma laidlawii

64 BNHS

Av-Fer

EM

65

membranes

Halobacterium halobium membranes Surface sites Intact yeast cells Membrane galactose residues Intact erythrocytes and lymphocytes

66

Periodate/BHZ

Av-Fer

EM

67

Gal ox./BHZ

Av-Fer

EM

68

" See reference list at end of article.

55 56

58

20

INTRODUCTION

"s

[3]

I

o

MM

~

,,-.]

~

[.,,T.J

< ..0

.~

< 0 ©

o >.m

'-~ ~

E I I I

,~ o -~ z o

Applications of avidin-biotin technology: literature survey.

14 INTRODUCTION [3] [3] A p p l i c a t i o n s o f A v i d i n - B i o t i n T e c h n o l o g y : Literature Survey By MEIR WILCHEK and EDWARD A...
1MB Sizes 0 Downloads 0 Views