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Plasmodium vivax
Image by Mae Melvin
Researchers say they have determined the structure of the protein PvRBP2a, which is used by the malaria parasite Plasmodium vivax to infect human red blood cells.
This revealed that PvRBP2a is structurally similar to PfRh5, the essential erythrocyte-binding protein in the parasite P falciparum.
The researchers believe these findings could help scientists generate new tools to prevent infection with malaria parasites.
Wai-Hong Tham, PhD, of The Walter and Eliza Hall Institute of Medical Research in Parkville, Victoria, Australia, and her colleagues conducted this research and reported the results in PNAS.
“We have produced the first 3-dimensional, atomic resolution structure of the protein [PvRBP2a] using the Australian Synchrotron in Melbourne,” Dr Tham said.
She and her colleagues found that PvRBP2a consists of 10 α-helices and 1 short β-hairpin. And although PvRBP2a is structurally similar to PfRh5, the 2 proteins have different surface properties.
“The 3-dimensional map showed us that the proteins are folded in the same way—like having similar origami instructions,” Dr Tham said. “The difference is actually in the electrical charge on the surface of the molecules.”
“Now that we have an atomic-resolution map, we hope to identify a common part of the protein that could be used to design a vaccine not only for Plasmodium vivax but potentially for both vivax and falciparum.”
“These two species of malaria are responsible for the majority of malaria infections worldwide, so a vaccine that targets both would be a critical addition to our arsenal.”
Dr Tham said there is growing evidence that developing better treatments or preventive strategies for P vivax malaria is imperative for malaria eradication.
“Not only is P vivax the most widespread species of malaria, it is also more difficult to treat because it can hide in the liver for long periods of time without symptoms,” she said. “In addition, studies show that effective treatment of falciparum malaria tends to be accompanied by a resurgence of P vivax, so it is critical to continue looking for better ways to manage this species.” 
Plasmodium vivax
Image by Mae Melvin
Researchers say they have determined the structure of the protein PvRBP2a, which is used by the malaria parasite Plasmodium vivax to infect human red blood cells.
This revealed that PvRBP2a is structurally similar to PfRh5, the essential erythrocyte-binding protein in the parasite P falciparum.
The researchers believe these findings could help scientists generate new tools to prevent infection with malaria parasites.
Wai-Hong Tham, PhD, of The Walter and Eliza Hall Institute of Medical Research in Parkville, Victoria, Australia, and her colleagues conducted this research and reported the results in PNAS.
“We have produced the first 3-dimensional, atomic resolution structure of the protein [PvRBP2a] using the Australian Synchrotron in Melbourne,” Dr Tham said.
She and her colleagues found that PvRBP2a consists of 10 α-helices and 1 short β-hairpin. And although PvRBP2a is structurally similar to PfRh5, the 2 proteins have different surface properties.
“The 3-dimensional map showed us that the proteins are folded in the same way—like having similar origami instructions,” Dr Tham said. “The difference is actually in the electrical charge on the surface of the molecules.”
“Now that we have an atomic-resolution map, we hope to identify a common part of the protein that could be used to design a vaccine not only for Plasmodium vivax but potentially for both vivax and falciparum.”
“These two species of malaria are responsible for the majority of malaria infections worldwide, so a vaccine that targets both would be a critical addition to our arsenal.”
Dr Tham said there is growing evidence that developing better treatments or preventive strategies for P vivax malaria is imperative for malaria eradication.
“Not only is P vivax the most widespread species of malaria, it is also more difficult to treat because it can hide in the liver for long periods of time without symptoms,” she said. “In addition, studies show that effective treatment of falciparum malaria tends to be accompanied by a resurgence of P vivax, so it is critical to continue looking for better ways to manage this species.”
Plasmodium vivax
Image by Mae Melvin
Researchers say they have determined the structure of the protein PvRBP2a, which is used by the malaria parasite Plasmodium vivax to infect human red blood cells.
This revealed that PvRBP2a is structurally similar to PfRh5, the essential erythrocyte-binding protein in the parasite P falciparum.
The researchers believe these findings could help scientists generate new tools to prevent infection with malaria parasites.
Wai-Hong Tham, PhD, of The Walter and Eliza Hall Institute of Medical Research in Parkville, Victoria, Australia, and her colleagues conducted this research and reported the results in PNAS.
“We have produced the first 3-dimensional, atomic resolution structure of the protein [PvRBP2a] using the Australian Synchrotron in Melbourne,” Dr Tham said.
She and her colleagues found that PvRBP2a consists of 10 α-helices and 1 short β-hairpin. And although PvRBP2a is structurally similar to PfRh5, the 2 proteins have different surface properties.
“The 3-dimensional map showed us that the proteins are folded in the same way—like having similar origami instructions,” Dr Tham said. “The difference is actually in the electrical charge on the surface of the molecules.”
“Now that we have an atomic-resolution map, we hope to identify a common part of the protein that could be used to design a vaccine not only for Plasmodium vivax but potentially for both vivax and falciparum.”
“These two species of malaria are responsible for the majority of malaria infections worldwide, so a vaccine that targets both would be a critical addition to our arsenal.”
Dr Tham said there is growing evidence that developing better treatments or preventive strategies for P vivax malaria is imperative for malaria eradication.
“Not only is P vivax the most widespread species of malaria, it is also more difficult to treat because it can hide in the liver for long periods of time without symptoms,” she said. “In addition, studies show that effective treatment of falciparum malaria tends to be accompanied by a resurgence of P vivax, so it is critical to continue looking for better ways to manage this species.”