AI Article Synopsis
- * Two specific NARs were identified that can bind to a harmful protease (Kgp) from a type of bacteria (Porphyromonas gingivalis) when tested in a lab setting using E. coli.
- * These findings suggest that NARs play a role in the immune response against pathogenic bacteria, supporting the idea that they function like true antibodies.
Article Abstract
The new antigen receptor (NAR) from sharks consists of a single immunoglobulin variable domain attached to five constant domains, and is hypothesised to function as an antibody. Two closely related NARs with affinity for the Kgp (lysine-specific) gingipain protease from Porphyromonas gingivalis were selected by panning an NAR variable domain library. When produced in Escherichia coli, these recombinant NARs were stable, correctly folded, and specifically bound Kgp (K(d)=1.31+/-0.26x10(-7) M). Binding localised to the Kgp adhesin domains, however without inhibiting adhesin activity. These naturally occurring proteins indicate an immune response to pathogenic bacteria and suggest that the NAR is a true antibody-like molecule.
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| http://dx.doi.org/10.1016/s0014-5793(02)02506-1 | DOI Listing |
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