Mutant/mutation
The mutant lacks expression of HSPJ62 and expresses GFP (see also mutant RMgm-2668 for unsuccessful attempts to select mutants with a disrupted hspj62 gene).

Protein (function)
Te crucial mediators of the heat shock response during elevated temperatures in the host are heat shock proteins (HSPs) that display stress-induced expression. As molecular chaperones, these proteins promote the folding of cellular proteins and prevent their aggregation10. Approximately 2% of the Plasmodium genome codes for molecular chaperones. Chaperones are a family of proteins responsible for proper folding of translated peptide chains into their monomeric or oligomeric forms during stress. Based on their molecular weight, HSPs are categorized into eight main families: HSP110, HSP100, HSP90, HSP70, HSP60, HSP40, HSP10, and  small HSPs (sHSPs). Comparison with other organisms shows that more than 50% of HSP proteins (~43) in the Plasmodium parasite belong to the HSP40 family. Based on their conserved domains, the HSP40 protein family is divided into four distinct classes: Type I HSP40 proteins contain an N-terminal J-domain, zinc-binding  cysteine rich domain, substrate-binding C-terminal, histidine-proline-aspartate (HPD) motif, and glycine/phenylalanine (GP) rich region. Te GP region separates the N-terminal J domain from the rest of the protein. Type II proteins do not have zinc-binding domains, while only DNAJ domains are present in type III and IV HSP40 proteins; however, type IV protein sequences exhibit disparities in the HPD motif. Generally, HSP families are conserved in Plasmodium species, while comparative data analysis of the molecular chaperone families shows that there are some members that are specifc to stage, lineage or species of Plasmodium. RESA is a type IV Hsp40-like protein that is expressed in parasites during early development of the merozoite stage and interacts with the membrane of invaded erythrocytes to prevent further invasion. Out of 43 Hsp40 proteins, 19 proteins show homology with their orthologues from other species of Apicomplexan, indicating that these proteins could have specifc functions in the parasite and could be promising drug targets, while variance was observed in most of the exported proteins 

Phenotype
Normal growth and morphology. evidence is presented for a higher growth rate. Evidence is presented for the lack of gametocyte production and absence of male gamete production (by exflagellation). No oocyst formation.

Additional information
See also mutant RMgm-2668 for unsuccessful attempts to select mutants with a disrupted hspj62 gene).

Other mutants