Citations

3636 total record number
147 records this year

To narrow your search, use one or more of the following search menus below.

To search by keyword, you may search by type of cell/animal/assay/protein/research or publication.

Antibodies against a Plasmodium falciparum antigen PfMSPDBL1 inhibit merozoite invasion into human erythrocytes

Sakamoto, H;Takeo, S;Maier, AG;Sattabongkot, J;Cowman, AF;Tsuboi, T;
Product: Tetanolysin from Clostridium tetani

One approach to develop a malaria blood-stage vaccine is to target proteins that play critical roles in the erythrocyte invasion of merozoites. The merozoite surface proteins (MSPs) and the erythrocyte-binding antigens (EBAs) are considered promising vaccine candidates, for they are known to play important roles in erythrocyte invasion and are exposed to host immune system. Here we focused on a Plasmodium falciparum antigen, PfMSPDBL1 (encoded by PF10_0348 gene) that is a member of the MSP3 family and has both Duffy binding-like (DBL) domain and secreted polymorphic antigen associated with merozoites (SPAM) domain. Therefore, we aimed to characterize PfMSPDBL1 as a vaccine candidate. Recombinant full-length protein (rFL) of PfMSPDBL1 was synthesized by a wheat germ cell-free system, and rabbit antiserum was raised against rFL. We show that rabbit anti-PfMSPDBL1 antibodies inhibited erythrocyte invasion of wild type parasites in vitro in a dose dependent manner, and the specificity of inhibitory activity was confirmed using PfMSPDBL1 knockout parasites. Pre-incubation of the anti-PfMSPDBL1 antibodies with the recombinant SPAM domain had no effect on the inhibitory activity suggesting that antibodies to this region were not involved. In addition, antibodies to rFL were elicited by P. falciparum infection in malaria endemic area, suggesting the PfMSLDBL1 is immunogenic to humans. Our results suggest that PfMSPDBL1 is a novel blood-stage malaria vaccine candidate.

PubMed ID: 22248820
244924492017-06-052017-06-0511:03:0311:03:032018-03-262018-03-2616:14:4716:14:47Sakamoto, H;Takeo, S;Maier, AG;Sattabongkot, J;Cowman, AF;Tsuboi, T;Sakamoto, H;Takeo, S;Maier, AG;Sattabongkot, J;Cowman, AF;Tsuboi, T;20122012Antibodies against a Plasmodium falciparum antigen PfMSPDBL1 inhibit merozoite invasion into human erythrocytesAntibodies against a Plasmodium falciparum antigen PfMSPDBL1 inhibit merozoite invasion into human erythrocytesVaccineVaccine1972-801972-80303011112224882022248820

One approach to develop a malaria blood-stage vaccine is to target proteins that play critical roles in the erythrocyte invasion of merozoites. The merozoite surface proteins (MSPs) and the erythrocyte-binding antigens (EBAs) are considered promising vaccine candidates, for they are known to play important roles in erythrocyte invasion and are exposed to host immune system. Here we focused on a Plasmodium falciparum antigen, PfMSPDBL1 (encoded by PF10_0348 gene) that is a member of the MSP3 family and has both Duffy binding-like (DBL) domain and secreted polymorphic antigen associated with merozoites (SPAM) domain. Therefore, we aimed to characterize PfMSPDBL1 as a vaccine candidate. Recombinant full-length protein (rFL) of PfMSPDBL1 was synthesized by a wheat germ cell-free system, and rabbit antiserum was raised against rFL. We show that rabbit anti-PfMSPDBL1 antibodies inhibited erythrocyte invasion of wild type parasites in vitro in a dose dependent manner, and the specificity of inhibitory activity was confirmed using PfMSPDBL1 knockout parasites. Pre-incubation of the anti-PfMSPDBL1 antibodies with the recombinant SPAM domain had no effect on the inhibitory activity suggesting that antibodies to this region were not involved. In addition, antibodies to rFL were elicited by P. falciparum infection in malaria endemic area, suggesting the PfMSLDBL1 is immunogenic to humans. Our results suggest that PfMSPDBL1 is a novel blood-stage malaria vaccine candidate.

One approach to develop a malaria blood-stage vaccine is to target proteins that play critical roles in the erythrocyte invasion of merozoites. The merozoite surface proteins (MSPs) and the erythrocyte-binding antigens (EBAs) are considered promising vaccine candidates, for they are known to play important roles in erythrocyte invasion and are exposed to host immune system. Here we focused on a Plasmodium falciparum antigen, PfMSPDBL1 (encoded by PF10_0348 gene) that is a member of the MSP3 family and has both Duffy binding-like (DBL) domain and secreted polymorphic antigen associated with merozoites (SPAM) domain. Therefore, we aimed to characterize PfMSPDBL1 as a vaccine candidate. Recombinant full-length protein (rFL) of PfMSPDBL1 was synthesized by a wheat germ cell-free system, and rabbit antiserum was raised against rFL. We show that rabbit anti-PfMSPDBL1 antibodies inhibited erythrocyte invasion of wild type parasites in vitro in a dose dependent manner, and the specificity of inhibitory activity was confirmed using PfMSPDBL1 knockout parasites. Pre-incubation of the anti-PfMSPDBL1 antibodies with the recombinant SPAM domain had no effect on the inhibitory activity suggesting that antibodies to this region were not involved. In addition, antibodies to rFL were elicited by P. falciparum infection in malaria endemic area, suggesting the PfMSLDBL1 is immunogenic to humans. Our results suggest that PfMSPDBL1 is a novel blood-stage malaria vaccine candidate.

3.4853.485

... To harvest parasite pellets, mature schizonts were purified using Percoll (GE Healthcare, Camarillo, CA) density gradient centrifugation and further treated with tetanolysin (List Biological Laboratories, Campbell, CA), washed with phosphate buffered saline (PBS) containing ...

... To harvest parasite pellets, mature schizonts were purified using Percoll (GE Healthcare, Camarillo, CA) density gradient centrifugation and further treated with tetanolysin (List Biological Laboratories, Campbell, CA), washed with phosphate buffered saline (PBS) containing ...

http://www.sciencedirect.com/science/article/pii/S0264410X12000138http://www.sciencedirect.com/science/article/pii/S0264410X120001382012-03-022012-03-0210.1016/j.vaccine.2012.01.01010.1016/j.vaccine.2012.01.010Tetanolysin from Clostridium tetaniTetanolysin from Clostridium tetanitsuboi@ccr.ehime-u.ac.jptsuboi@ccr.ehime-u.ac.jpActivity;Anti;Antibodies;Antigen;Antiserum;Binding;Biological;Blood;Cell;Dependent;Domain;Gene;Host;Immune System;Immunogenic;In vitro;Infection;Inhibit;Inhibitory;List;List Biological;Novel;Protein;Purified;Rabbit;Recombinant;Surface;Target;Tetanolysin;Vaccine;Activity;Anti;Antibodies;Antigen;Antiserum;Binding;Biological;Blood;Cell;Dependent;Domain;Gene;Host;Immune System;Immunogenic;In vitro;Infection;Inhibit;Inhibitory;List;List Biological;Novel;Protein;Purified;Rabbit;Recombinant;Surface;Target;Tetanolysin;Vaccine;199199antibodies-against-a-plasmodium-falciparumantibodies-against-a-plasmodium-falciparum