scholarly journals Select gp120 V2 domain specific antibodies derived from HIV and SIV infection and vaccination inhibit gp120 binding to α4β7

2018 ◽  
Vol 14 (8) ◽  
pp. e1007278 ◽  
Author(s):  
Sakaorat Lertjuthaporn ◽  
Claudia Cicala ◽  
Donald Van Ryk ◽  
Matthew Liu ◽  
Jason Yolitz ◽  
...  
Keyword(s):  
Specific Antibodies ◽  
Domain Specific ◽  
Gp120 Binding ◽  
Siv Infection

Domain-specific antibodies reveal multiple-site topology of Nup153 within the nuclear pore complex

2002 ◽  
Vol 140 (1-3) ◽  
pp. 254-267 ◽  
Author(s):  
Birthe Fahrenkrog ◽  
Bohumil Maco ◽  
Ammon M. Fager ◽  
Joachim Köser ◽  
Ursula Sauder ◽  
...  
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Multiple Site ◽  
Specific Antibodies ◽  
Domain Specific

scholarly journals Escape of HIV-1 is associated with lack of V3 domain-specific antibodies in vivo

1997 ◽  
Vol 107 (1) ◽  
pp. 15-20 ◽  
Author(s):  
M. SCHREIBER ◽  
H. MULLER ◽  
C. WACHSMUTH ◽  
T. LAUE ◽  
F. T. HUFERT ◽  
...  
Keyword(s):  
Specific Antibodies ◽  
Domain Specific ◽  
Hiv 1

Platelet integrin α2 I-domain specific antibodies produced via domain specific DNA vaccination combined with variable gene phage display

2005 ◽  
Vol 94 (12) ◽  
pp. 1318-1326 ◽  
Author(s):  
Darren L. Hughes ◽  
Prachi Stafford ◽  
Samir W. Hamaia ◽  
Anne Schoolmeester ◽  
Hans Deckmyn ◽  
...  
Keyword(s):  
Phage Display ◽  
Recombinant Antibody ◽  
Dna Vaccination ◽  
Gene Repertoire ◽  
Single Chain ◽  
Specific Antibodies ◽  
Domain Specific ◽  
Variable Gene ◽  
V Gene ◽  
Α2β1 Integrin

SummaryAntibodies are a powerful tool for structure/function studies of platelet proteins. However, classic immunisation frequently elicits antibody responses against domains of minor functional interest. Robust strategies to generate antibodies against defined domains would be of significant interest in post-genome research. In this study, we report a new strategy using a combination of DNA vaccination and V gene phage display that allows the rapid generation of domain specific single-chain Fv antibodies (scFvs).This system was validated using the I-domain of α2 integrin as a model. The α2β1 integrin, which is expressed on many cell types, is the dominant collagen attachment receptor on platelets, functioning in close interplay with the collagen signalling receptor glycoproteinVI. A novel set of I-domain specific antibodies was obtained by a DNA vaccination/V gene repertoire cloning approach. Mice were first immunized with a DNA vaccine in which the α2 I-domain is expressed as a fusion protein with fragment C of tetanus toxoid (FrC-TT).Then the heavy and kappa light chain variable gene repertoires were rescued from immune splenocytes using antibody phage display. A total of four α2 I-domain specific scFvs were isolated by selection on recombinant I-domain or native platelet α2β1 integrin. Characterisation of the scFvs indicated that they recognised distinct epitopes that had profound differences in accessibility between native and recombinant I-domain. Our data suggest DNA immunisation and phage display represent versatile alternatives to protein immunisation and hybridoma-fusion techniques for the isolation of recombinant antibody reagents. This approach will be particularly useful for the generation of domain or splicevariant specific antibodies that recognise native protein.

Domain-specific antibodies against the B2 chain of laminin inhibit neuronal migration in the neonatal rat cerebellum

1995 ◽  
Vol 40 (2) ◽  
pp. 199-206 ◽  
Author(s):  
Päivi Liesi ◽  
G. Hager ◽  
H.-U. Dodt ◽  
I. Seppälä ◽  
W. Zieglgänsberger
Keyword(s):  
Neuronal Migration ◽  
Neonatal Rat ◽  
Specific Antibodies ◽  
Domain Specific ◽  
Rat Cerebellum

Expression of CCN3 protein in human Wilms’ tumors: immunohistochemical detection of CCN3 variants using domain-specific antibodies

2007 ◽  
Vol 452 (1) ◽  
pp. 33-39 ◽  
Author(s):  
Manish Mani Subramaniam ◽  
Noureddine Lazar ◽  
Samuel Navarro ◽  
Bernard Perbal ◽  
Antonio Llombart-Bosch
Keyword(s):  
Immunohistochemical Detection ◽  
Specific Antibodies ◽  
Domain Specific

scholarly journals All four putative ligand-binding domains in megalin contain pathogenic epitopes capable of inducing passive Heymann nephritis.

1998 ◽  
Vol 9 (9) ◽  
pp. 1638-1644
Author(s):  
H Yamazaki ◽  
R Ullrich ◽  
M Exner ◽  
A Saito ◽  
R A Orlando ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Rat Kidney ◽  
Target Antigen ◽  
Specific Antibodies ◽  
Domain Specific ◽  
Binding Domains ◽  
Heymann Nephritis ◽  
Extracellular Region ◽  
Putative Ligand Binding

Megalin (gp330) is the main target antigen involved in the induction of Heymann nephritis (HN), a rat model of human membranous nephropathy. Its large extracellular region contains four putative ligand-binding domains separated by spacer regions. Previously, it was reported that the second ligand-binding domain (LBD II) of megalin is involved in the pathogenesis of passive HN because it is capable of binding antibodies in vivo and initiating formation of immune deposits (ID). This study explores the possibility that pathogenic epitopes might also be present in the other putative ligand-binding domains. Recombinant fragments of ligand-binding domains (LBD) I through IV expressed in a baculovirus system were used to generate polyclonal domain-specific antibodies. Antibodies raised against each of the recombinant megalin fragments reacted preferentially with its respective antigen and with whole megalin by immunoblotting. Each of the antibodies also gave a characteristic brush-border staining for megalin by indirect immunofluorescence on rat kidney. When rats were injected with the domain-specific antibodies to test their ability to produce passive HN, glomerular ID were present in kidneys of all injected animals. The staining pattern in glomeruli of rats injected with LBD I, III, or IV was similar to that obtained with antibodies to LBD II. It is concluded that passive HN can be induced with antibodies against LBD I, III, and IV, as well as LBD II, and that each of the ligand-binding domains contains a pathogenic epitope. These findings provide further evidence for the multiple epitope model of HN.

scholarly journals Mapping the binding domains on decay accelerating factor (DAF) for haemagglutinating enteroviruses: implications for the evolution of a DAF-binding phenotype

1999 ◽  
Vol 80 (12) ◽  
pp. 3145-3152 ◽  
Author(s):  
Robert M. Powell ◽  
Trevor Ward ◽  
Ian Goodfellow ◽  
Jeffrey W. Almond ◽  
David J. Evans
Keyword(s):  
Cell Attachment ◽  
Haemagglutination Inhibition ◽  
Virus Binding ◽  
Decay Accelerating Factor ◽  
Specific Antibodies ◽  
Domain Specific ◽  
Binding Domains ◽  
Short Consensus Repeat ◽  
Wide Range ◽  
A Cell

Decay accelerating factor (DAF) functions as a cell attachment receptor for a wide range of human enteroviruses, the interaction accounting for the haemagglutination phenotype exhibited by many members of this family. Haemagglutination inhibition assays using purified truncated soluble DAF (sDAF) receptors and short consensus repeat (SCR) domain-specific antibodies have been used to determine the domain(s) of DAF to which the viruses bind. Further sDAF-mediated virus neutralization and biosensor analysis have been used to confirm the virus-binding domains of DAF. Of the four distinct clusters of human enteroviruses, three contain representatives that bind DAF. The majority of DAF-binding enteroviruses occupy the ‘CBV-like’ cluster, and require SCR domains 2–4 for DAF binding. In contrast, the DAF-binding representatives of the ‘ENV70-like’ and ‘PV-like’ clusters require SCR1 for DAF interaction. These studies confirm that DAF binding is a widespread characteristic amongst phylogenetically divergent clusters within the enteroviruses and suggest that the ability to bind DAF may have evolved more than once within this group of viruses.

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