To be present in a common GDC-0941 complex with KAHRP and PfEMP3 further supporting its association with knobs. This indicated that chromosomal cluster of KAHRP, KAHsp40 and PfEMP3 is also a functional cluster. Interaction of KAHsp40 with the components of the PEXEL translocon as well suggests that it may be involved in shuttling proteins from PVM to erythrocyte membrane thereby facilitating knob assembly. It is important to mention here that knock out of the KAHsp40 gene in CS2 strain of the parasite does not show an obvious defect in knob formation on the erythrocyte surface. This may be due to the presence of several Hsp40s with redundant functions within the erythrocyte cytosol. In addition, knockouts of several molecular chaperones do not result in a direct readable phenotype under normal conditions but often result in phenotypes that can be uncovered only during stressful conditions such as high temperatures or nutrient deprivation or in combination with knockouts of other genes. Although the knockout of KAHsp40 is not essential under normal circumstances, it may be involved in finetuning the export and assembly of knob components or recruitment of Hsp70, along with other exported Hsp40. A recent study has elegantly demonstrated that two exported PfHsp40s are present in cholesterol containing mobile structures in the erythrocyte cytosol referred to as J-dots. This study addresses the organization of parasite-encoded Hsp40s in the erythrocyte cytosol for the first time, by examining the fractionation of Hsp40-GFP chimeras into detergent solubilized cells. They found that these Hsp40s are released into the soluble fraction upon treatment of cells with saponin/methyl-b-cyclodextrin, indicating their association with cholesterol-containing structures. The authors have postulated that these structures could be instrumental in protein trafficking within the infected erythrocyte. J-dots are distinct from Maurer’s clefts and do not co-localize with KAHRP and PfEMP1. Our results reveal nonoverlapping distribution of KAHsp40 with J-dots suggesting that these Hsp40s may have different functions. Considering the fact that these Hsp40s cluster together in a phylogram of all 44 PfHsp40s, it cannot be ruled out that these Hsp40s could have complementary functions. In all, our study implicates a parasite encoded Hsp40 that possibly acts in the biogenesis or assembly of cytoadherent knobs. The remodeling of the erythrocyte upon infection by the parasite is crucial for parasite virulence and it is no surprise that the parasite has evolved customized chaperones to facilitate this process. This is also supported by the fact that Plasmodium vivax which does not involve host cell remodeling and knob formation in its life cycle lacks the homologs of exported Hsp40s present in Plasmodium falciparum. Undoubtedly, implication of additional exported chaperones and understanding the assembly of this fascinating supramolecular complex will be an area of intense research focus in parasitology in the years to come. The 7q deletion may play an important role in the pathogenesis of SMZL. To investigate this, we searched for evidence of any potential tumour suppressor genes in the MDR. The classic tumour suppressor genes are often inactivated on both alleles by multiple mechanisms including homozygous deletion, heterozygous deletion and mutation. To ascertain the gene or genes targeted by the 7q deletion in SMZL, we sought evidence of homozygous deletion by gene resolution array CGH of chromosome 7.