1992
DOI: 10.1016/0092-8674(92)90642-p
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A reticulocyte-binding protein complex of plasmodium vivax merozoites

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Cited by 337 publications
(327 citation statements)
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“…Based on these observations, it is likely that the new members of these gene families, as well as 133 ring-and 156 schizont-specific, nonsyntenic, hypothetical genes expressed during the IDC (Fig. 1B), represent important factors associated with the P. vivax selectivity for young erythrocytes (21) and/or immune evasion. Pearson correlation comparisons between the P. vivax and P. falciparum IDC transcriptomes (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Based on these observations, it is likely that the new members of these gene families, as well as 133 ring-and 156 schizont-specific, nonsyntenic, hypothetical genes expressed during the IDC (Fig. 1B), represent important factors associated with the P. vivax selectivity for young erythrocytes (21) and/or immune evasion. Pearson correlation comparisons between the P. vivax and P. falciparum IDC transcriptomes (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…In vitro studies showing that P. knowlesi invades Duffy-negative erythrocytes treated with trypsin and neuraminidase (33) suggest that P. knowlesi possess additional erythrocyte invasion ligands enabling Duffy-independent bloodstage infection. Whether our results signal local evolution of a new P. vivax erythrocyte invasion pathway, or indicate the existence of yet-uncharacterized erythrocyte invasion mechanisms involving DBPs and/or reticulocyte binding proteins (34,35), remains to be clarified.…”
Section: Discussionmentioning
confidence: 99%
“…The PfRh (P. falciparum reticulocyte-binding-like proteins) family of proteins is homologous to Py235 and PvRBP (P. vivax reticulocyte-binding proteins) in P. yoelii and P. vivax, respectively. In P. vivax, two proteins have been identified (PvRBP1 and 2) that bind to reticulocytes; these proteins have been hypothesized to play a role in the preference of P. vivax for invasion of these specific host cells [58]. PvRBP1 and 2 are located at the apical end of 45 and GAP50 to the parasite cytoskeleton comprising the inner membrane particles (IMP), the subpellicular filaments (IMC network) subtending the IMC, and the microtubules.…”
Section: Reorientation and Initiation Of A Junctional Contactmentioning
confidence: 99%