Mutant/mutation
The mutant lacks expression of HMGB2

Protein (function)
High mobility group box (HMGB) proteins are nuclear proteins originally shown to be loosely associated with DNA and to participate, to at least some extent, in the regulation of gene transcription. Subsequent studies have shown that the human HMGB proteins composed of two HMGB domains, Box A and Box B in tandem and in particular the HMGB1 isoform are actively secreted from activated innate immune cells, namely macrophages and can be released from injured cells as well. In humans, HMGB1 has an role as extracellular soluble protein that signals tissue injury and initiates inflammatory responses.
Plasmodium species have two high mobility group proteins, HMGB1 and HMGB2, which consist of only one HMGB domain also comprising a 20 amino acid peptide potentially bearing pro-inflammatory activity.

See also RMgm-1251 for a P. berghei ANKA mutant (from the same group) lacking expression of HMGB2 (with reduced cerebral complications in C57Bl/6 mice)

See also RMgm-162 for a P. yoelii mutant lacking expression of HMGB2. These parasites showed a slightly reduced growth rate of blood stages and reduced ookinete and oocyst production.

Phenotype
Reduced growth of blood stages and C57Bl/6 are able to clear the infection after day 15 (in contrast to wild type infections where mice die from hyperparasitemia)

Additional information
Evidence is presented that:
Pre-immunization with Δhmgb2PbNK65 parasitized red blood cells can confer long-lasting protection in a murine experimental cerebral malaria model against two  pathogenic homologous and heterologous parasites.

Other mutants
See also RMgm-1251 for a P. berghei ANKA mutant (from the same group) lacking expression of HMGB2 (with reduced cerebral complications in C57Bl/6 mice)

See also RMgm-162 for a P. yoelii mutant lacking expression of HMGB2. These parasites showed a slightly reduced growth rate of blood stages and reduced ookinete and oocyst production.