TY - JOUR
T1 - Functional Characterization of Plasmodium falciparum Surface-Related Antigen as a Potential Blood-Stage Vaccine Target
AU - Amlabu, Emmanuel
AU - Mensah-Brown, Henrietta
AU - Nyarko, Prince B.
AU - Akuh, Ojo Ajogu
AU - Opoku, Grace
AU - Ilani, Philip
AU - Oyagbenro, Richard
AU - Asiedu, Kwame
AU - Aniweh, Yaw
AU - Awandare, Gordon A.
N1 - Publisher Copyright:
© The Author(s) 2018. Published by Oxford University Press for the Infectious Diseases Society of America.
PY - 2018/7/24
Y1 - 2018/7/24
N2 - Plasmodium falciparum erythrocyte invasion is a multistep process that involves a spectrum of interactions that are not well characterized. We have characterized a 113-kDa immunogenic protein, PF3D7_1431400 (PF14_0293), that possesses coiled-coil structures. The protein is localized on the surfaces of both merozoites and gametocytes, hence the name Plasmodium falciparum surface-related antigen (PfSRA). The processed 32-kDa fragment of PfSRA binds normal human erythrocytes with different sensitivities to enzyme treatments. Temporal imaging from initial attachment to internalization of viable merozoites revealed that a fragment of PfSRA, along with PfMSP119, is internalized after invasion. Moreover, parasite growth inhibition assays showed that PfSRA P1 antibodies potently inhibited erythrocyte invasion of both sialic acid-dependent and -independent parasite strains. Also, immunoepidemio-logical studies show that malaria-infected populations have naturally acquired antibodies against PfSRA. Overall, the results demonstrate that PfSRA has the structural and functional characteristics of a very promising target for vaccine development.
AB - Plasmodium falciparum erythrocyte invasion is a multistep process that involves a spectrum of interactions that are not well characterized. We have characterized a 113-kDa immunogenic protein, PF3D7_1431400 (PF14_0293), that possesses coiled-coil structures. The protein is localized on the surfaces of both merozoites and gametocytes, hence the name Plasmodium falciparum surface-related antigen (PfSRA). The processed 32-kDa fragment of PfSRA binds normal human erythrocytes with different sensitivities to enzyme treatments. Temporal imaging from initial attachment to internalization of viable merozoites revealed that a fragment of PfSRA, along with PfMSP119, is internalized after invasion. Moreover, parasite growth inhibition assays showed that PfSRA P1 antibodies potently inhibited erythrocyte invasion of both sialic acid-dependent and -independent parasite strains. Also, immunoepidemio-logical studies show that malaria-infected populations have naturally acquired antibodies against PfSRA. Overall, the results demonstrate that PfSRA has the structural and functional characteristics of a very promising target for vaccine development.
KW - Erythrocyte invasion
KW - Malaria vaccine
KW - Naturally acquired immunity
KW - Novel antigens
KW - Plasmodium falciparum
UR - http://www.scopus.com/inward/record.url?scp=85055455895&partnerID=8YFLogxK
U2 - 10.1093/infdis/jiy222
DO - 10.1093/infdis/jiy222
M3 - Article
C2 - 29912472
AN - SCOPUS:85055455895
SN - 0022-1899
VL - 218
SP - 778
EP - 790
JO - Journal of Infectious Diseases
JF - Journal of Infectious Diseases
IS - 5
ER -