Dynamic association of PfEMP1 and KAHRP in knobs mediates cytoadherence during Plasmodium invasion
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Title |
Dynamic association of PfEMP1 and KAHRP in knobs mediates cytoadherence during Plasmodium invasion
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Creator |
GANGULY, AK
RANJAN, P KUMAR, A BHAVESH, NS |
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Subject |
HISTIDINE-RICH PROTEIN
ERYTHROCYTE-MEMBRANE PROTEIN-1 FALCIPARUM-INFECTED ERYTHROCYTES INTRINSICALLY DISORDERED PROTEINS NMR STRUCTURE DETERMINATION TITRATION CALORIMETRY DATA STRUCTURAL BASIS CHEMICAL-SHIFTS GLOBAL ANALYSIS ALPHA-HELIX |
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Description |
Plasmodium falciparum infected erythrocytes display membrane knobs that are essential for their adherence to vascular endothelia and for prevention of clearance by the spleen. The knob associated histidine rich protein (KAHRP) is indispensable to knob formation and has been implicated in the recruitment and tethering of P. falciparum erythrocyte membrane protein-1 (PfEMP1) by binding to its cytoplasmic domain termed VARC. However, the precise mechanism of interaction between KAHRP and VARC is not very well understood. Here we report that both the proteins co-localize to membrane knobs of P. falciparum infected erythrocytes and have identified four positively charged linear sequence motifs of high intrinsic mobility on KAHRP that interact electrostatically with VARC in solution to form a fuzzy complex. The current study provides molecular insight into interaction between KAHRP and VARC in solution that takes place at membrane knobs.
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Publisher |
NATURE PUBLISHING GROUP
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Date |
2016-01-15T06:37:19Z
2016-01-15T06:37:19Z 2015 |
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Type |
Article
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Identifier |
SCIENTIFIC REPORTS, 5
2045-2322 http://dx.doi.org/10.1038/srep08617 http://dspace.library.iitb.ac.in/jspui/handle/100/17950 |
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Language |
en
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