Specificity and structure-function analysis of lupus-derived monoclonal anti-DNA autoantibodies

Specificity and structure-function relationships of the monoclonal anti-DNA autoantibodies, BV 04-01 and BV 17-45, derived from the NZB/NZW F1 lupus-prone murine strain were examined. A single-chain Fv derivative of BV 04-01 was constructed and a series of site-specific mutants were engineered. A sensitive fluorescence-based tryptophan quenching assay was developed for analysis of the binding properties of the wild-type and mutant single-chain Fv proteins. Results of these binding assays revealed the importance of a tryptophan-thymidine-tyrosine complex in conveying ligand specificity in the cleft-like anti-DNA active site of BV 04-01. Basic residues within the active site enhanced the affinity of the interaction through energetically important but relatively non-specific contributions.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Rumbley, Catherine Ann

Contributors dc:contributor

• Voss, Edward W., Jr.

• Health Sciences, Pathology
• Health Sciences, Immunology

Statement dc:rights

• Copyright 1995 Rumbley, Catherine Ann

Language dc:language

eng

Identifier

AAI9624476
(UMI)AAI9624476

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/20008