Host ICAMs play a role in cell invasion by Mycobacterium tuberculosis and Plasmodium falciparum

Abstract

Intercellular adhesion molecules (ICAMs) belong to the immunoglobulin superfamily and participate in diverse cellular processes including host-pathogen interactions. ICAM-1 is expressed on various cell types including macrophages, whereas ICAM-4 is restricted to red blood cells. Here we report the identification of an 11-kDa synthetic protein, M5, that binds to human ICAM-1 and ICAM-4, as shown by in vitro interaction studies, surface plasmon resonance and immunolocalization. M5 greatly inhibits the invasion of macrophages and erythrocytes by Mycobacterium tuberculosis and Plasmodium falciparum, respectively. Pharmacological and siRNA-mediated inhibition of ICAM-1 expression also results in reduced M. tuberculosis invasion of macrophages. ICAM-4 binds to P. falciparum merozoites, and the addition of recombinant ICAM-4 to parasite cultures blocks invasion of erythrocytes by newly released merozoites. Our results indicate that ICAM-1 and ICAM-4 play roles in host cell invasion by M. tuberculosis and P. falciparum, respectively, either as receptors or as crucial accessory molecules.

Host–parasite interaction: multiple sites in the Plasmodium vivax tryptophan‐rich antigen PvTRAg38 interact with the erythrocyte receptor band 3

“…In each experiment, ligands were coupled either to Fc‐2 or Fc‐4 and Fc‐1 or Fc‐3 served as control flow cells. Experiments were performed either by immobilizing band 3 fragments onto the sensor chip CM5 using amine‐coupling chemistry in accordance with the protocol described previously . Binding was measured at 50 μL·min −1 to avoid the mass transport effect.…”

Red cell receptors as access points for malaria infection

“…CD55 and ICAM-4 are RBC receptors without known parasite ligands identified through forward genetics [46] and parasite inhibition studies [47], respectively (Table 2). Conversely, parasite ligands without known receptors include PfMSPDBL 1 & 2 [49], PfRh2 [50], PfEBA-181 [48], and PfTRAMP (Table 2) [51].…”

Interaction of Plasmodium vivax Tryptophan-rich Antigen PvTRAg38 with Band 3 on Human Erythrocyte Surface Facilitates Parasite Growth

“…Surface Plasmon Resonance Analysis-Real time interactions of PvTRAg38, its fragment M-PvTRAg38, or peptide P-4 with Band 3 or with Band 3 fragments (B3F1, B3F3, and B3F6) were analyzed by surface plasmon resonance studies under flow condition using a Biacore 2000 instrument (Biacore, Uppsala, Sweden) as described by Bhalla et al (24). The carboxymethylateddextran surfaces of Biacore CM5 sensor chips were activated by injection of 1:1 mixture of N-hydroxysuccinimide and 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide hydrochloride for 7 min at a flow rate of 10 l/min.…”