High affinity binding between laminin and laminin binding protein of Leishmania is stimulated by zinc and may involve laminin zinc-finger like sequences
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High affinity binding between laminin and laminin binding protein
of Leishmania is stimulated by zinc and may involve laminin
zinc-finger like sequences
Das, Pijush K
Infectious Diseases and Immunology
In the course of trying to understand the pathogenesis of
leishmaniasis in relation to extracellular matrix (ECM)
elements, laminin, a major ECM protein, has been found to
bind saturably and with high a�nity to a 67-kDa cell surface
protein of Leishmania donovani. This interaction involves a
single class of binding sites, which are ionic in nature,
conformation-dependent and possibly involves sulfhydryls.
Binding activity was signi®cantly enhanced by Zn2+, an
effect possibly mediated through Cys-rich zinc ®nger-like
sequences on laminin. Inhibition studies with monoclonals
against polypeptide chains and speci®c peptides with adhe-
sive properties revealed that the binding site was localized in
one of the nested zinc ®nger consensus sequences of B1 chain containing the speci®c pentapeptide sequence, YIGSR.
Furthermore, incubation of L. donovani promastigotes with
C(YIGSR)3-NH2 peptide amide or antibody directed
against the 67-kDa laminin-binding protein (LBP) induced
tyrosine phosphorylation of proteins with a molecular mass
ranging from 115 to 130 kDa. These studies suggest a role
for LBP in the interaction of parasites with ECM elements,
which may mediate one or more downstream signalling
events necessary for establishment of infection.
Bandyopadhyay, Keya and Karmakar, Sudipan and Ghosh, Abhijit and Das, Pijush K (2002) High affinity binding between laminin and laminin binding protein of Leishmania is stimulated by zinc and may involve laminin zinc-finger like sequences. European Journal Of Biochemistry, 269 (6). pp. 1622-1629.