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. 2014 Jun 12;10(6):e1004120.
doi: 10.1371/journal.ppat.1004120. eCollection 2014 Jun.

Multimeric assembly of host-pathogen adhesion complexes involved in apicomplexan invasion

May M Paing  1 , Niraj H Tolia  1
Affiliations

Multimeric assembly of host-pathogen adhesion complexes involved in apicomplexan invasion

May M Paing et al. PLoS Pathog. .
No abstract available

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Conflict of interest statement

The authors have declared that no competing interests exist.

Figures

Figure 1
Figure 1. Multimeric assembly, clustered interactions, and molecular complexes between parasite ligands and host-cell receptors for invasion.
(A) PfTRAP engagement with heparan sulphate proteoglycans (HSPGs) on the hepatocyte surface; (B) proteolytic processing and shedding of PfMSP1 exposes the 19 kDa fragment (MSP119) that forms an invasion complex with MSP9 and the band 3 homodimer; (C) assembly of two PfEBA-175 monomers around dimeric glycophorin A of erythrocytes; (D) stepwise multimeric assembly of two PvDBP with two Duffy antigen/receptor for chemokines on reticulocyte surface; (E) monomeric interaction between PfEBA-140 and glycophorin C on erythrocytes; (F) proposed complexes of TgMIC2 and TgM2AP and of TgMIC1, TgMIC4, and TgMIC6 on the parasite surface; (G) variations in oligomeric states of GPI-anchored surface antigens (SAGs) create distinct interaction sites.
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