Cloning and structure-function analysis of the Leishmania donovani kinetoplastid membrane protein-11

A. Jardim, S. Hanson, B. Ullman, W. D. McCubbin, C. M. Kay, R. W. Olafson

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

This report describes the complete translated gene sequence, predicted secondary structure and lipid bilayer association of a novel kinetoplastid membrane protein (KMP-11) from Leishmania donovani promastigotes. KMP-11 was previously referred to as the lipophosphoglycan-associated protein (LPGAP). The isolation, species distribution and chemical characterization, including a partial protein sequence analysis and post-translational modifications, of this major membrane component have been described. C.d. measurements of KMP-11 indicated a very high helical content estimated to be approximately 86 % in trifluoroethanol. This was in agreement with computer-based secondary-structure analyses which predicted KMP-11 to be almost exclusively α-helical, with the protein adopting a helix-loop-helix motif. Arrangement of the residues located in the putative helical regions on an Edmundson helical wheel showed that this molecule could have a strongly amphipathic conformation and provided an explanation for how such a highly charged protein might be inserted into the plasma membrane. Evidence in support of KMP-11 association with lipid bilayers was provided by showing that KMP-11 could mediate carboxyfluorescein release from liposomes. These findings suggested that KMP-11 may function in part to increase bilayer pressure, stabilizing molecules such as lipophosphoglycan within the parasite pellicular membrane.

Original languageEnglish (US)
Pages (from-to)315-320
Number of pages6
JournalBiochemical Journal
Volume305
Issue number1
DOIs
StatePublished - 1995

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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