Functional characterization of an LCCL-lectin domain containing protein family in Plasmodium berghei

Holly E. Trueman, J. Dale Raine, Laurence Florens, Johannes T. Dessens, Jacqui Mendoza, Jeffrey Johnson, Cecilia C. Waller, Isabelle Delrieu, Anthony A. Holder, Jean Langhorne, Daniel J. Carucci, John R. Yates, Robert E. Sinden

Research output: Contribution to journalArticlepeer-review

37 Scopus citations


Using bioinformatic, proteomic, immunofluorescence, and genetic cross methods, we have functionally characterized a family of putative parasite ligands as potential mediators of cell-cell interactions. We name these proteins the Limulus clotting factor C, Coch-5b2, and Lgl1 (LCCL)-lectin adhesive-like protein (LAP) family. We demonstrate that this family is conserved amongst Plasmodium spp. It possesses a unique arrangement of adhesive protein domains normally associated with extracellular proteins. The proteins are expressed predominantly, though not exclusively, in the mosquito stages of the life cycle. We test the hypothesis that these proteins are surface proteins with 1 member of this gene family, lap1, and provide evidence that it is expressed on the surface of Plasmodium berghei sporozoites. Finally, through genetic crosses of wild-type Pblap1+ and transgenic Pblap1- parasites, we show that the null phenotype previously reported for sporozoite development in a Pblap1- mutant can be rescued within a heterokaryotic oocyst and that infectious Pblap1- sporozoites can be formed. The mutant is not rescued by coparasitization of mosquitoes with a mixture Pblap1+ and Pblap1- homokaryotic oocysts.

Original languageEnglish
Pages (from-to)1062-1071
Number of pages10
JournalJournal of Parasitology
Issue number5
StatePublished - Oct 2004
Externally publishedYes


Dive into the research topics of 'Functional characterization of an LCCL-lectin domain containing protein family in Plasmodium berghei'. Together they form a unique fingerprint.

Cite this