title: Evidence of a laminin binding protein on the surface of Leishmania donovani.
abstract: Both the promastigote and amastigote forms of the intracellular parasite, Leishmania donovani bind the basement membrane glycoprotein laminin with high affinity (Kd = 3.56 x 10(-9) M and 3.98 x 10(-9) M respectively) with approximately 9000 and approximately 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.
authors.affiliation: Molecular Cell Biology Division, Indian Institute of Chemical Biology, Calcutta, India.
authors.forename: A
authors.initials: A
authors.lastname: Ghosh
authors.forename: L
authors.initials: L
authors.lastname: Kole
authors.forename: K
authors.initials: K
authors.lastname: Bandyopadhyay
authors.forename: K
authors.initials: K
authors.lastname: Sarkar
authors.forename: P K
authors.initials: PK
authors.lastname: Das
mesh_terms: D000818:Animals; D001485:Basement Membrane / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005109:Extracellular Matrix / Q000378:metabolism; D007893:Leishmania donovani / Q000378:metabolism* / Q000502:physiology; D017474:Receptors, Laminin / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D017474:Receptors, Laminin