Involvement of Leishmania donovani major surface glycoprotein gp63 in promastigote multiplication
IR@IICB: CSIR-Indian Institute of Chemical Biology, KolkataView Archive Info
Involvement of Leishmania donovani major surface glycoprotein
gp63 in promastigote multiplication
Molecular & Human Genetics
The major surface glycoprotein gp63 of the kinetoplastid protozoal parasite Leishmania is implicated as a ligand
mediating uptake of the parasite into, and survival within, the host macrophage. By expressing gp63 antisense
RNA from an episomal vector in L. donovani promastigotes, gp63-deficient transfectants were obtained. Reduction
of the gp63 level resulted in increased generation times, altered cell morphology, accumulation of cells in
the G2/M phase of the cell cycle, and increased numbers of binucleate cells with one or two kinetoplasts. Growth
was stimulated, and the number of binucleate cells reduced, by addition to the culture of a bacterially expressed
fusion protein containing the fibronectin-like SRYD motif and the zinc-binding (metalloprotease) domain of
gp63. These observations support an additional role of gp63 in promastigote multiplication; the fibronectin-like
properties of gp63 may be important in this process.
Pandey, Sanjeev and Chakraborti, Phuljhuri and Sharma, Rakhi and Bandyopadhyay, Santu and Sarkar, Dwijen and Adhya, Samit (2004) Involvement of Leishmania donovani major surface glycoprotein gp63 in promastigote multiplication. Journal of Biosciences, 29 (1). pp. 15-22.