A naturally occurring NAR variable domain binds the Kgp protease from Porphyromonas gingivalis

FEBS Letters

Nuttall, Stewart D²  Ally, Nafisa¹  Doughty, Larissa²  Nathanielsz, Anne²  Krishnan, Usha V²  Hudson, Peter J²  Irving, Robert A²  Kortt, Alexander A²  Pike, Robert N¹ 

[1]Department of Biochemistry and Molecular Biology, Monash University, Clayton, Vic. 3800, Australia

[2]CSIRO Health Sciences and Nutrition, 343 Royal Parade, Parkville, Vic. 3052, Australia

关键词: Scaffold;    Peptide display;    VH;    Variable domain;    New antigen receptor;    Lysine-specific gingipain protease from Porphyromonas gingivalis;    wNAR;    new antigen receptor from wobbegong sharks;    nNAR;    new antigen receptor from nurse sharks;    Kgp;    lysine-specific gingipain protease from Porphyromonas gingivalis;    HRgpA;    high molecular weight arginine-specific gingipain protease from Porphyromonas gingivalis;   

DOI  :  10.1016/S0014-5793(02)02506-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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±0.26×10⁻⁷ 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.

【 授权许可】

Unknown