Dee Athwal
3 Papers
181 Citations
Dee Athwal is an academic researcher. The author has contributed to research in topics: Cardiolipin & Beta 2-Glycoprotein I. The author has an hindex of 3, co-authored 3 publications.
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Papers
Molecular cloning and expression of the Fabs of human autoantibodies in Escherichia coli. Determination of the heavy or light chain contribution to the anti-DNA/-cardiolipin activity of the Fab.
Sanjeev Kumar,Jatinderpal Kalsi,C. T. Ravirajan,Anisur Rahman,Dee Athwal,David S. Latchman,David A. Isenberg,Laurence H. Pearl +7 more
TL;DR: The comparative DNA/cardiolipin binding analyses of the nine Fabs revealed that the anti-DNA (light, B3/33H11) or anti-cardiolIPin (heavy, UK4) activity lies predominantly on one of the two chains, however, a compatible partner chain is necessary for optimum antigen binding activity of the antibody.
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Anti-cardiolipin/β-2 glycoprotein activities co-exist on human anti-DNA antibody light chains ☆
Sanjeev Kumar,Sylvia Nagl,Jatinderpal Kalsi,C. T. Ravirajan,Dee Athwal,David S. Latchman,Laurence H. Pearl,David A. Isenberg +7 more
TL;DR: It is demonstrated that hybrid Fabs with constituent light chain, but not the heavy chain, of B3 or 33H11, exhibit anti-cardiolipin activity and the constructs possessing the auto-antibody-derived light chain also exhibited significant reactivity to beta2-GPI.
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Beta-2-glycoprotein specificity of human anti-phospholipid antibody resides on the light chain: a novel mechanism for acquisition of cross-reactivity by an autoantibody.
Sanjeev Kumar,Sylvia Nagl,Jatinderpal Kalsi,C. T. Ravirajan,Dee Athwal,David S. Latchman,Laurence H. Pearl,David A. Isenberg +7 more
TL;DR: The results demonstrate that anti-beta2-GPI activity resides on UK4 light chain and, importantly, this activity could be transferred to a novel antibody construct via the light chain alone and the possible mechanisms that such antibodies may employ to recognise their antigens are discussed.
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