| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
*
Immunology Group, International Center for Genetic Engineering and Biotechnology, and
National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi, India
The influence of imposing various conformational constraints on immune responses to a model epitope within a synthetic peptide immunogen was examined in mice. Although overall immunogenicity was affected, the model epitope (sequence DPAF) remained the predominant recognition site regardless of the conformation in which it was presented. A comparison of anti-DPAF mAbs obtained in response to two analogue peptides, PS1CT3 and CysCT3, in which the DPAF segment was either unconstrained or held within a cyclic loop, respectively, revealed a significant homology in the paratope composition. At one level a subset of anti-PS1CT3 and anti-CysCT3 mAbs was found to share a common heavy chain variable region. In addition, nucleotide sequence homology comparisons of both heavy and light chain variable regions identified the presence of anti-PS1CT3 and anti-CysCT3 mAbs that collectively appeared to derive from a common progenitor, but with nonidentical somatic mutations. Interestingly, however, no bias toward homologous Ag could be discerned on measurement of relative affinities of the mAbs for the two peptides. In contrast, mAb binding on-rates clearly discriminated between peptides representing the homologous vs the heterologous confomer of the DPAF epitope. Thus, it would appear that the kinetics of Ag recognition dominate over equilibrium binding criteria both in epitope-driven repertoire selection and Ab maturation in a humoral response.
This article has been cited by other articles:
|
|
 |
|
  G. R. McLean, O. A. Olsen, I. N. Watt, P. Rathanaswami, K. B. Leslie, J. S. Babcook, and J. W. Schrader Recognition of Human Cytomegalovirus by Human Primary Immunoglobulins Identifies an Innate Foundation to an Adaptive Immune Response J. Immunol., April 15, 2005; 174(8): 4768 - 4778. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. T. Nair, K. Singh, Z. Siddiqui, B. P. Nayak, K. V. S. Rao, and D. M. Salunke Epitope Recognition by Diverse Antibodies Suggests Conformational Convergence in an Antibody Response J. Immunol., March 1, 2002; 168(5): 2371 - 2382. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. T. Nair, K. Singh, N. Sahu, K. V. S. Rao, and D. M. Salunke Crystal Structure of an Antibody Bound to an Immunodominant Peptide Epitope: Novel Features in Peptide-Antibody Recognition J. Immunol., December 15, 2000; 165(12): 6949 - 6955. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. Nakra, V. Manivel, R. A. Vishwakarma, and K. V. S. Rao B Cell Responses to a Peptide Epitope. X. Epitope Selection in a Primary Response Is Thermodynamically Regulated J. Immunol., June 1, 2000; 164(11): 5615 - 5625. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. P. Nayak, A. Agarwal, P. Nakra, and K. V. S. Rao B Cell Responses to a Peptide Epitope. VIII. Immune Complex-Mediated Regulation of Memory B Cell Generation Within Germinal Centers J. Immunol., August 1, 1999; 163(3): 1371 - 1381. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Agarwal, B. P. Nayak, and K. V. S. Rao B Cell Responses to a Peptide Epitope. VII. Antigen-Dependent Modulation of the Germinal Center Reaction J. Immunol., December 1, 1998; 161(11): 5832 - 5841. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
