Reactions of human antibodies with CR1 immobilised by mouse monoclonal antibody E11 Red cell phenotype Murine MAb Human anti- Absorbance Ratio Kn(a+) ] Kn(a-) E11 Kna 0.755 0.195 4:1 McC(a+) 0.538 McC(a-) E11 McC 0.136 4:1 Yk(a+) 0.315 Yk(a-) E11 Yka 0.120 26:1 Sl(a+) 0.342 Sl(a-) E11 Sla 0.074 4.6:1 Cs(a+) 0.139 Cs(a-) E11 Cs 0.108 Mapping relative positions of antigens on a specific protein When several murine monoclonal antibodies to different epitopes on the same protein are available, MAIEA can be used to study the relative position of antigens on that protein. This application of MAIEA depends on mutual inhibition of murine monoclonal antibodies and human antibodies. A negative result is obtained when human and monoclonal antibodies compete for the same epitope, or bind to very closely located epitopes, so no tri-molecular complex is produced. Several monoclonal antibodies to the Kell protein have been used in MAIEA to study the relationships of the Kell system antigens [10]. The decay accelerating factor DAF, CD55, is detected by several monoclonal antibodies. Three antibodies BRIC 230, BRIC 110 and BRIC 216 were known from competitive binding assays to bind to different short consensus repeats (SCR) [11]. So three of the four SCRs of the DAF molecule were positively identified (Table II). Strong positive reactions were observed with all three BRIC antibodies and anti-Cr3, anti-WES8, and anti-WESb showing that MAIEA is a useful techique for studying this system [12]. The results showed that Cr8, WESa, and WESb are not on the first three SCRs and must

1995 ◽  
pp. 190-190
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Molecular Complex ◽  
Specific Protein ◽  
Cell Phenotype ◽  
Binding Assays ◽  
Human Antibodies ◽  
Short Consensus Repeats ◽  
Murine Monoclonal Antibodies ◽  
Competitive Binding Assays

Production and characterization of murine monoclonal antibodies against staphylococcal enterotoxins A and E

1991 ◽  
Vol 37 (8) ◽  
pp. 581-585 ◽  
Author(s):  
Kunihiro Shinagawa ◽  
Emiko Nishimura ◽  
Makoto Mitsumori ◽  
Naonori Matsusaka ◽  
Shunji Sugii
Keyword(s):  
Staphylococcus Aureus ◽  
Monoclonal Antibodies ◽  
The Other ◽  
Staphylococcal Enterotoxin A ◽  
Binding Assays ◽  
Spleen Cells ◽  
Myeloma Cells ◽  
Murine Monoclonal Antibodies ◽  
Competitive Binding Assays

Six murine monoclonal antibodies (MAbs) against staphylococcal enterotoxin A (SEA) and enterotoxin E (SEE) were prepared by fusion of myeloma cells with mouse spleen cells immunized with SEA and SEE. Of five MAbs to SEA tested, two MAbs were reactive with only SEA, whereas three were specific for both SEA and SEE. On the other hand, one MAb to SEE was found to be specific for only SEE. To study specificities of the combining sites of these MAbs, competitive binding assays with either SEA or SEE and horseradish peroxidase conjugated MAbs were performed using unconjugated MAbs as inhibitors. The results obtained in the assays suggest that different epitopes may be located on SEA and that some of them may be cross-reacting epitopes between SEA and SEE. Key words: enterotoxins, monoclonal antibodies, Staphylococcus aureus.

scholarly journals Circumsporozoite proteins of malaria parasites contain a single immunodominant region with two or more identical epitopes.

1983 ◽  
Vol 157 (6) ◽  
pp. 1947-1957 ◽  
Author(s):  
F Zavala ◽  
A H Cochrane ◽  
E H Nardin ◽  
R S Nussenzweig ◽  
V Nussenzweig
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Specific Binding ◽  
Polyclonal Antibodies ◽  
Binding Assays ◽  
Malaria Parasites ◽  
Immunodominant Region ◽  
Additional Finding ◽  
Single Region ◽  
Competition Binding

We have used panels of monoclonal antibodies to circumsporozoite (CS) proteins of Plasmodium falciparium, P. vivax, and P. knowlesi to determine the number of topographically independent epitopes of these antigens. The results of competition binding assays indicated that single regions of the CS molecules were recognized by the homologous monoclonal antibodies. Competition binding assays were also used to study the specificity of antibodies contained in the sera of humans and monkeys that had developed sterile immunity after immunization with irradiated, intact sporozoites. We found that single monoclonal antibodies inhibited 70-95% of the specific binding of the polyclonal antibodies to crude extracts of sporozoites. It appears, therefore, that CS proteins are among the most immunogenic constituents of sporozoites, and that a single region of these molecules contains most of the immunogenic activity. An additional finding was that the immunodominant region of CS molecules is multivalent with regard to the expression of a single epitope. This was demonstrated by the ability of monomers of CS proteins to bind simultaneously two or more molecules of the same monoclonal antibody.

Generation and Characterization of a Murine Monoclonal Antibody Specific for the Human T1-Cd5 Molecule

1987 ◽  
Vol 2 (3) ◽  
pp. 143-150 ◽  
Author(s):  
Federico Genzano ◽  
Ada Funaro ◽  
Massimo Alessio ◽  
Lucia B. De Monte ◽  
Graziella Bellone ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
T Cell ◽  
T Lymphocytes ◽  
Membrane Glycoprotein ◽  
Functional Features ◽  
Specific Membrane ◽  
Murine Monoclonal Antibodies ◽  
Selection Of

Murine monoclonal antibodies (MoAbs) have found widespread applications in the characterization of the molecular and functional features of lymphocyte differentiation antigens. The present paper summarizes the results of our work dealing with the production and selection of a murine MoAb recognizing a molecule expressed during the whole differentiative life of T lymphocytes. The MoAb CB01 resulted to be specific for an apparently unique epitope of the T-cell specific membrane glycoprotein T1-CD5.

Analysis of liver-specific protein LSP using murine monoclonal antibodies

1987 ◽  
Vol 17 (4) ◽  
pp. 360-367 ◽  
Author(s):  
T. PORALLA ◽  
M. MANNS ◽  
H. P. DIENES ◽  
W. DIPPOLD ◽  
T. H. HÜTTEROTH ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Specific Protein ◽  
Liver Specific Protein ◽  
Murine Monoclonal Antibodies

scholarly journals Identification of Residues within Human Glycoprotein VI Involved in the Binding to Collagen

2004 ◽  
Vol 279 (50) ◽  
pp. 52293-52299 ◽  
Author(s):  
Christelle Lecut ◽  
Véronique Arocas ◽  
Hans Ulrichts ◽  
Anthony Elbaz ◽  
Jean-Luc Villeval ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Molecular Modeling ◽  
Binding Sites ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Binding Assays ◽  
Glycoprotein Vi ◽  
Ligand Binding Sites ◽  
Human Receptor

Glycoprotein VI (GPVI) has a crucial role in platelet responses to collagen. Still, little is known about its interaction with its ligands. In binding assays using soluble or cell-expressed human GPVI, we observed that (i) collagen, and the GPVI-specific ligands collagen-related peptides (CRP) and convulxin, competed with one another for the binding to GPVI and (ii) monoclonal antibodies directed against the extracellular part of the human receptor displayed selective inhibitory properties on GPVI interaction with its ligands. Monoclonal antibody 9E18 strongly reduced the binding of GPVI to collagen/CRP, 3F8 inhibited its interaction with convulxin, whereas 9O12 prevented all three interactions. These observations suggest that ligand-binding sites are distinct, exhibiting specific features but at the same time also sharing some common residues participating in the recognition of these ligands. The epitope of 9O12 was mapped by phage display, along with molecular modeling of human GPVI, which allowed the identification of residues within GPVI potentially involved in ligand recognition. Site-directed mutagenesis revealed that valine 34 and leucine 36 are critical for GPVI interaction with collagen and CRP. The loop might thus be part of a collagen/CRP-binding site.

Quantitative expression of epitopes defined by murine monoclonal antibodies on DR molecules from different HLA haplotypes

1985 ◽  
Vol 5 (10-11) ◽  
pp. 923-931 ◽  
Author(s):  
Michelle Letarte ◽  
Jane Addis ◽  
Sonia Iturbe ◽  
Dieter Petsche
Keyword(s):  
Monoclonal Antibody ◽  
Flow Cytometry ◽  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Class Ii ◽  
Human Class ◽  
Quantitative Expression ◽  
Hla Dr ◽  
Hla Haplotypes ◽  
Murine Monoclonal Antibodies

Monoclonal antibodies 50D6 and 2Ir5, reactive with human class II molecules, were analyzed quantitatively by flow cytometry and cellular radioimmunoassay for their binding to cells of different HLA-DR types. Monoclonal antibody 50D6 bound equally to cells of all DR types tested except DR7, where no reactivity was observed. Monoclonal antibody 2Ir5 was reactive with all cells. However, the percentage of DR molecules at the cell surface expressing 2Ir5 epitope varied with the DR type and increased as follows: DR3 = DR7 < DR2 < DR5 < DR4 < DR1. MAb 50D6 reacted with an epitope spatially related to but distinct from the 2lw4 epitope present on all DR molecules. The 50D6 epitope was shown to be present on isolated DR1 molecules.

scholarly journals Mouse Antibodies with Activity Against the SARS-CoV-2 D614G and B.1.351 Variants

2021 ◽  
Author(s):  
Larisa Troitskaya ◽  
Nelson Lap Shun Chan ◽  
Brendon Frank ◽  
Daniel Capon ◽  
Brian A. Zabel ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Severe Disease ◽  
Human Antibody ◽  
Human Antibodies ◽  
Rapid Spread ◽  
Antibody Repertoires ◽  
Murine Monoclonal Antibodies

With the rapid spread of SARS-CoV-2 variants, including those that are resistant to antibodies authorized for emergency use, it is apparent that new antibodies may be needed to effectively protect patients against more severe disease. Differences between the murine and human antibody repertoires may allow for the isolation of murine monoclonal antibodies that recognize a different or broader range of SARS-CoV-2 variants than the human antibodies that have been characterized so far. We describe mouse antibodies B13 and O24 that demonstrate neutralizing potency against SARS-CoV-2 Wuhan (D614G) and B.1.351 variants. Such murine antibodies may have advantages in protecting against severe symptoms when individuals are exposed to new SARS-CoV-2 variants.

Protection against Lethal Endotoxemia by Anti-Lipid A Murine Monoclonal Antibodies: Comparison of Efficacy with That of Human Anti-Lipid A Monoclonal Antibody HA-1A

1993 ◽  
Vol 167 (4) ◽  
pp. 876-881 ◽  
Author(s):  
J. J. Cornelissen ◽  
I. Makel ◽  
A. Algra ◽  
B. J. Benaissa-Trouw ◽  
J. F. P. ScheUekens ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Lipid A ◽  
Murine Monoclonal Antibodies

scholarly journals Murine Monoclonal Antibodies Specific for Lipopolysaccharide of Escherichia coli O26 and O111

2000 ◽  
Vol 66 (9) ◽  
pp. 4124-4127 ◽  
Author(s):  
Mildred Rivera-Betancourt ◽  
James E. Keen
Keyword(s):  
Escherichia Coli ◽  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Bacterial Strains ◽  
Antigen Specificity ◽  
E Coli ◽  
O Antigen ◽  
Murine Monoclonal Antibodies

ABSTRACT Monoclonal antibody (MAb) 12F5 reacted with 35 Escherichia coli O26 isolates and cross-reacted with 1 of 365 non-E. coli O26 isolates. MAb 15C4 reacted with 30 E. coliO111 strains and 8 Salmonella O35 strains (possessing identical O antigen) but not with 362 other bacterial strains. Lipopolysaccharide immunoblots confirmed MAb O-antigen specificity.

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