Evidence of a laminin binding protein on the surface of Leishmania donovani

Abhijit Ghosh, Labanyamoy Kole, Keya Bandyopadhyay, Kakali Sarkar, Pijush K. Das

Research output: Contribution to journalArticle


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 languageEnglish (US)
Pages (from-to)101-106
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Sep 4 1996

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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