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1 activity in which each protein recognizes >1 erythrocyte receptor.
2  of the parasite ligands for binding to this erythrocyte receptor.
3               Each region recognizes its own erythrocyte receptor.
4 encoded by multi-gene families interact with erythrocyte receptors.
5 omains that are postulated to bind different erythrocyte receptors.
6 lex multistep process involving parasite and erythrocyte receptors.
7 NG), it was found that BAEBL bound different erythrocyte receptors.
8  of extracellular recognition events between erythrocyte receptors and ligands on the merozoite, the
9 t on multiple molecular interactions between erythrocyte receptors and parasite ligands.
10    We conclude that the interactions between erythrocyte receptors and their ligands, 2B10 and MSA-1,
11 alaria parasite responds to polymorphisms in erythrocyte receptors and/or evades the immune system.
12 parasite growth and the interaction with its erythrocyte receptor basigin is essential for invasion.
13         In conclusion, PvTRAg38 binds to two erythrocyte receptors basigin and band 3 through P2 and
14 pensable parasite ligand that binds with its erythrocyte receptor, Basigin.
15             Although antibodies against host erythrocyte receptors CD235a and CD35 had no effect, Ag-
16                       Specific engagement of erythrocyte receptors defines target cell tropism, activ
17 co-ligands on its surface to target a single erythrocyte receptor during invasion.
18 ing the glycophorin peptide backbone, is the erythrocyte receptor for adhesion to microgametes.
19                            Like EBA-175, the erythrocyte receptor for BAEBL is destroyed by neuramini
20               The DARC also functions as the erythrocyte receptor for invasion by malarial parasites.
21 re, we have identified basigin as the second erythrocyte receptor for PvTRAg38, which is resistant to
22 ntified band 3 as the chymotrypsin-sensitive erythrocyte receptor for the P4 region, but the other re
23 een identified as the chymotrypsin-sensitive erythrocyte receptor for this parasite protein.
24 lciparum strains vary in their dependence on erythrocyte receptors for invasion and their ability to
25 alciparum merozoites use diverse alternative erythrocyte receptors for invasion and variably express
26 od-stage invasion ligand EBA175 and the host erythrocyte receptor Glycophorin-A (GYPA) has been impli
27                            However, only one erythrocyte receptor, Glycophorin A, has a well-establis
28 ibodies to inhibit binding of EBA-175 to its erythrocyte receptor, glycophorin A, using either native
29                     Multiple parasite ligand-erythrocyte receptor interactions must occur for success
30 uraminidase and trypsin, indicating that the erythrocyte receptor is a sialoglycoprotein.
31  of the Duffy binding protein (DBP) with its erythrocyte receptor is critical for maintaining Plasmod
32 date because adhesion of P. vivax DBP to its erythrocyte receptor is essential for the parasite to co
33                                Further, each erythrocyte receptor is shared by >1 PvTRAg.
34 3 protein are parasite-induced, host-derived erythrocyte receptors mediating parasite sequestration.
35 chimeric antibody (Ab-1) against basigin, an erythrocyte receptor necessary for parasite invasion as
36 eins bind to the same but yet another set of erythrocyte receptor(s).
37 rst identification of likely determinants of erythrocyte receptor specificity for P. falciparum invas
38 re red blood cells through recognition of an erythrocyte receptor that is neuraminidase- and chymotry
39 tical for directing parasites to alternative erythrocyte receptors that define invasion pathways.
40 n erythrocytes involves several parasite and erythrocyte receptors that enable parasite invasion by m
41 wn as invasion ligands that bind to specific erythrocyte receptors to facilitate invasion of human er
42  the GPC receptor, supporting a hierarchy of erythrocyte receptor usage in P. falciparum.
43  an unknown trypsin sensitive factor are all erythrocyte receptors used during invasion by the major
44 FCR3 strain); the binding of both ligands to erythrocyte receptors was totally sialic acid dependent.
45 cated that PvTRAg36 and PvTRAg34 share their erythrocyte receptors with previously described proteins
46 y mediated by an unknown parasite ligand and erythrocyte receptor "X." The neuraminidase-sensitive, t

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