scholarly journals Comparison of 5 monoclonal antibodies for immunopurification of human butyrylcholinesterase on Dynabeads: KD values, binding pairs, and amino acid sequences

2015 ◽  
Vol 240 ◽  
pp. 336-345 ◽  
Author(s):  
Hong Peng ◽  
Stephen Brimijoin ◽  
Anna Hrabovska ◽  
Katarina Targosova ◽  
Eric Krejci ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Amino Acid Sequences ◽  
Kd Values ◽  
Human Butyrylcholinesterase

scholarly journals Comparative Analysis of Two Meningococcal Immunotyping Monoclonal Antibodies by Resonant Mirror Biosensor and Antibody Gene Sequencing

1999 ◽  
Vol 6 (6) ◽  
pp. 838-843 ◽  
Author(s):  
Bambos M. Charalambous ◽  
Janet Evans ◽  
Ian M. Feavers ◽  
Martin C. J. Maiden
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Antigenic Variation ◽  
Gene Sequencing ◽  
Amino Acid Sequences ◽  
Heavy Chains ◽  
Sequence Identity ◽  
Differential Binding ◽  
Major Surface ◽  
Antibody Gene

ABSTRACT Lipooligosaccharide (LOS) is a major surface component of the cell walls of Neisseria meningitidis, which is important for its roles in pathogenesis and antigenic variation, as a target for immunological typing, and as a possible vaccine component. Although the structures of many antigenic variants have been determined, routine immunological typing of these molecules remains problematic. Resonant mirror analysis was combined with gene sequencing to characterize two monoclonal antibodies (MAbs) used in typing panels that were raised against the same LOS immunotype, L3,7,9. The two MAbs (MAb 4A8-B2 and MAb 9-2-L379) were of the same immunoglobulin subtype, but while MAb 9-2-L379 was more than a 1,000-fold more sensitive in immunotyping assays of both whole meningococcal cells and purified LOS, MAb 4A8-B2 was more specific for immunotype L3,7,9. The differences in sensitivity were a consequence of MAb 9-2-L379 having a 44-fold-faster association constant than MAb 4A8-B2. Comparison of the amino acid sequences of the variable chains of the MAbs revealed that they had very similar heavy chains (81% amino acid sequence identity) but diverse light chains (54% sequence identity). The differential binding kinetics and specificities observed with these MAbs were probably due to differences in the epitopes recognized, and these were probably a consequence of the different immunization protocols used in their production.

Highland games: A benchmarking exercise in predicting biophysical and drug properties of monoclonal antibodies from amino acid sequences

2020 ◽  
Vol 117 (7) ◽  
pp. 2100-2115 ◽  
Author(s):  
Jonathan Coffman ◽  
Bruno Marques ◽  
Raquel Orozco ◽  
Minni Aswath ◽  
Hasan Mohammad ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Amino Acid Sequences

scholarly journals Sequence Conservation and Antigenic Variation of the Structural Proteins of Equine Rhinitis A Virus

2001 ◽  
Vol 75 (21) ◽  
pp. 10550-10556 ◽  
Author(s):  
Annalisa Varrasso ◽  
Heidi E. Drummer ◽  
Jin-an Huang ◽  
Rachel A. Stevenson ◽  
Nino Ficorilli ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Antigenic Variation ◽  
Amino Acid Sequences ◽  
Sequence Conservation ◽  
Structural Proteins ◽  
Serum Neutralization ◽  
Prototype Virus

ABSTRACT The nucleotide and deduced amino acid sequences of the P1 region of the genomes of 10 independent equine rhinitis A virus (ERAV) isolates were determined and found to be very closely related. A panel of seven monoclonal antibodies to the prototype virus ERAV.393/76 that bound to nonneutralization epitopes conserved among all 10 isolates was raised. In serum neutralization assays, rabbit polyclonal sera and sera from naturally and experimentally infected horses reacted in a consistent and discriminating manner with the 10 isolates, which indicated the existence of variation in the neutralization epitopes of these viruses.

scholarly journals Cloning and Sequence Analysis of Genes Encoding Staphylococcus hyicus Exfoliative Toxin Types A, B, C, and D

2004 ◽  
Vol 186 (6) ◽  
pp. 1833-1837 ◽  
Author(s):  
Peter Ahrens ◽  
Lars Ole Andresen
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Serine Proteases ◽  
Amino Acid Sequences ◽  
Coding Sequence ◽  
Exfoliative Toxin ◽  
Genes Encoding

ABSTRACT Exfoliative toxins produced by certain strains of Staphylococcus hyicus mediate exudative epidermitis in pigs. In this study the genes coding for four different exfoliative toxin from S. hyicus (ExhA, ExhB, ExhC, and ExhD) were cloned and sequenced. The coding sequence of the four toxin genes ranged from 816 to 834 bp. The amino acid sequences of these four toxins were homologous to the earlier described exfoliative toxins SHETB from S. hyicus and ETA, ETB, and ETD from Staphylococcus aureus. The homology between the S. hyicus toxins was at the same level as the homology to the exfoliative toxins from S. aureus. The toxins showed similarity to serine proteases, including preservation of the catalytic tract in ExhA, ExhB, and ExhC. However, in ExhD, Asp in the putative catalytic tract was replaced with Glu. The recombinant toxins could be expressed in Escherichia coli, and three of the four toxins were recognized by monoclonal antibodies raised against native exfoliative toxins.

Factors that contribute to the immmunogenicity of therapeutic recombinant human proteins

2008 ◽  
Vol 99 (11) ◽  
pp. 874-882 ◽  
Author(s):  
Ilya Mukovozov ◽  
Thomas Sabljic ◽  
Gonzalo Hortelano ◽  
Frederick Ofosu
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Dna Sequences ◽  
Cultured Cells ◽  
Therapeutic Proteins ◽  
Peptide Hormone ◽  
Amino Acid Sequences ◽  
Clinical Use ◽  
Human Proteins ◽  
Therapeutic Monoclonal Antibodies

SummaryUse of recombinant human proteins has revolutionized medicine by providing over 200 highly purified hormones and proteins that effectively treat many inherited and acquired peptide hormone and protein deficiencies. With the exception of therapeutic monoclonal antibodies, these biological medicines are synthesized by cultured cells using DNA sequences that would yield proteins with identical amino acid sequences as endogenous human proteins. Therefore, there was the broad expectation that recombinant human biological medicines would be non-immunogenic in patients capable of synthesizing even sub-optimal levels of these therapeutic proteins to which they are innately tolerant. However, the widespread clinical use of recombinant human proteins has demonstrated that nearly all of them are immunogenic. This observation suggests that factors additional to differences in amino acid sequences of endogenous and biotherapeutic proteins contribute to the immunogenicity of therapeutic proteins. The main aim of this review is to summarize some of the factors that are known to contribute to the immunogenicity of recombinant therapeutic proteins.

Establishing a Link Between Amino Acid Sequences and Self-Associating and Viscoelastic Behavior of Two Closely Related Monoclonal Antibodies

2011 ◽  
Vol 28 (7) ◽  
pp. 1750-1764 ◽  
Author(s):  
Sandeep Yadav ◽  
Alavattam Sreedhara ◽  
Sonoko Kanai ◽  
Jun Liu ◽  
Samantha Lien ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Viscoelastic Behavior ◽  
Amino Acid Sequences

Antigenic analysis of testicular cytochromes c using monoclonal antibodies

1986 ◽  
Vol 64 (12) ◽  
pp. 1211-1217 ◽  
Author(s):  
In C. Kim ◽  
Hector Nolla
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Cross Reactivity ◽  
Amino Acid Sequences ◽  
Antigenic Structure ◽  
Enzyme Linked Immunosorbent Assay ◽  
Antigenic Analysis ◽  
Cyt C ◽  
Primary Amino ◽  
Species Specific

Testicular cytochrome c (cyt ct) was isolated from testes of sexually mature, rat, mouse, rabbit, and bull, among which rat testis is highly rich in cyt c1. By fusion of NS-1 myeloma cells and spleen cells of mice immunized with rat cyt ct, 11 stable mouse hybridoma cell lines were established. Using an enzyme-linked immunosorbent assay, it was determined that 4 of the 11 anti-rat cyt ct monoclonal antibodies (McAb) did not bind to somatic cyt c (cyt cs) of vertebrates nor to cyt ct of mouse, rabbit, and bull. Four other McAb showed no binding to cyt cs but showed different patterns of cross-reactivity with these four cyt ct. Therefore, these McAb appear to be very sensitive and useful probes for the discrimination or identification of extremely similar isocytochromes c. Although the primary amino acid sequences between cyt cs of rat and mouse are identical, the antigenic structure of cyt ct of rat and mouse are clearly distinct with regard to cross-reactivity with some anti-rat cyt ct McAb. Furthermore, these McAb also reveal that the primary amino acid sequences of cyt ct, which reflect differences in the surface conformation of the molecule, are probably species specific.

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