14
August 2003
Immunoglobulins: Small but potent antibodies
Monomeric immunoglobulins in vertebrates consist of two heavy and two light chain polypeptides — except in camelids (camels and llamas), where most antibodies are dimers of heavy chains only. Their small size makes them attractive as possible therapeutic agents, as they may enter tissues and cells that other antibodies cannot. New work reported this week looks at antibodies relevant to protein deposition diseases. A mutant of human lysozyme, D67H, causes a systemic amyloidosis, which can be fatal. A single-domain camel antibody raised against normal human lysozyme is shown to inhibit in vitro formation of amyloid fibrils by D67H lysozyme, by restoring the defective enzyme's structural cooperativity. This suggests that reducing the ability of amyloidogneic proteins to form partly unfolded species — with an antibody or some other agent — may be one way of preventing aggregate formation.
A camelid antibody fragment inhibits the formation of
amyloid fibrils by human lysozyme
MIREILLE DUMOULIN,
ALEXANDER M. LAST, ALINE DESMYTER, KLAAS DECANNIERE, DENIS CANET, G�RAN LARSSON,
ANDREW SPENCER, DAVID B. ARCHER, JURGEN SASSE, SERGE MUYLDERMANS, LODE WYNS, CHRISTINA
REDFIELD, ANDR� MATAGNE, CAROL V. ROBINSON & CHRISTOPHER M. DOBSON
Nature
424, 783–788 (2003); doi:10.1038/nature01870
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