Title:
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A novel Plasmodium falciparum rhoptry associated adhesin
mediates erythrocyte invasion through the sialic-acid dependent
pathway
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Author:
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Anand, Gaurav; Reddy, K. Sony; Pandey, Alok Kumar; Mian, Syed Yusuf; Singh, Hina; Mittal, Shivani Arora; Amlabu, Emmanuel; Bassat Orellana, Quique; Mayor Aparicio, Alfredo Gabriel; Chauhan, Virander Singh; Gaur, Deepak
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Abstract:
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Erythrocyte invasion by Plasmodium falciparum merozoites is
central to blood-stage infection and malaria pathogenesis. This
intricate process is coordinated by multiple parasite adhesins
that bind erythrocyte receptors and mediate invasion through
several alternate pathways. P. falciparum expresses 2700 genes
during the blood-stages, of which the identity and function of
many remains unknown. Here, we have identified and characterized
a novel P. falciparum rhoptry associated adhesin (PfRA) that
mediates erythrocyte invasion through the sialic-acid dependent
pathway. PfRA appears to play a significant functional role as
it is conserved across different Plasmodium species. It is
localized in the rhoptries and further translocated to the
merozoite surface. Both native and recombinant PfRA specifically
bound erythrocytes in a sialic-acid dependent, chymotrypsin and
trypsin resistant manner, which was abrogated by PfRA antibodies
confirming a role in erythrocyte invasion. PfRA antibodies
inhibited erythrocyte invasion and in combination with
antibodies against other parasite ligands produced an additive
inhibitory effect, thus validating its important role in
erythrocyte invasion. We have thus identified a novel P.
falciparum adhesin that binds with a sialic acid containing
erythrocyte receptor. Our observations substantiate the strategy
to block P. falciparum erythrocyte invasion by simultaneously
targeting multiple conserved merozoite antigens involved in
alternate invasion pathways. |
Subject(s):
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-Plasmodium falciparum -Malària -Plasmodium falciparum -Malaria |
Rights:
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cc by (c) Anand et al., 2016
http://creativecommons.org/licenses/by/3.0/es/ |
Document type:
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Article Article - Published version |
Published by:
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Nature
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