Author： Ghosh A. Kole L. Bandyopadhyay K. Sarkar K. Das P.K.
Publisher： Elsevier
ISSN： 0006-291X
Source： Biochemical and Biophysical Research Communications, Vol.226, Iss.1, 1996-09, pp. : 101-106
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Abstract
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.
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