Affordable Access

Publisher Website

Conformational co-dependence betweenPlasmodium bergheiLCCL proteins promotes complex formation and stability

Authors
Journal
Molecular and Biochemical Parasitology
0166-6851
Publisher
Elsevier
Volume
185
Issue
2
Identifiers
DOI: 10.1016/j.molbiopara.2012.07.007
Keywords
  • Plasmodium Berghei
  • Crystalloid
  • Gfp
  • Protein Folding
  • Lccl Domain
Disciplines
  • Biology

Abstract

Abstract Malaria parasites express a conserved family of LCCL-lectin adhesive-like domain proteins (LAPs) that have essential functions in sporozoite transmission. In Plasmodium falciparum all six family members are expressed in gametocytes and form a multi-protein complex. Intriguingly, knockout of P. falciparum LCCL proteins adversely affects expression of other family members at protein, but not at mRNA level, a phenomenon termed co-dependent expression. Here, we investigate this in Plasmodium berghei by crossing a PbLAP1 null mutant parasite with a parasite line expressing GFP-tagged PbLAP3 that displays strong fluorescence in gametocytes. Selected and validated double mutants show normal synthesis and subcellular localization of PbLAP3::GFP. However, GFP-based fluorescence is dramatically reduced without PbLAP1 present, indicating that PbLAP1 and PbLAP3 interact. Moreover, absence of PbLAP1 markedly reduces the half-life of PbLAP3, consistent with a scenario of misfolding. These findings unveil a potential mechanism of conformational interdependence that facilitates assembly and stability of the functional LCCL protein complex.

There are no comments yet on this publication. Be the first to share your thoughts.