Both the promastigote and amastigote forms of the intracellular parasite, Leishmania donovani bind the basement membrane glycoprotein laminin with high affinity (K(d) = 3.56 x 10-9 M and 3.98 x 10-9 M respectively) with ~ 9000 and ~ 800 sites per cell. Bound laminin was identified by direct autoradiography and the binding protein through analysis of the parasite extract by SDS-PAGE and immunoblotting. A major component of 67 kDa was detected. The same protein was obtained when parasite outer membrane proteins were adsorbed to laminin-sepharose affinity matrix and subsequently eluted with SDS. The binding affinity of the isolated receptor was similar to that of the whole cells. Such a receptor isolated in Leishmania for the first time, may function as one of the bridging molecules for extracellular matrix recognition.
|Original language||English (US)|
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Sep 4 1996|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology