scholarly journals Fine Specificity of Serum Antibodies to Plasmodium falciparum Merozoite Surface Protein, PfMSP-119, Predicts Protection from Malaria Infection and High-Density Parasitemia

2004 ◽  
Vol 72 (3) ◽  
pp. 1557-1567 ◽  
Author(s):  
Brenda A. Okech ◽  
Patrick H. Corran ◽  
James Todd ◽  
Amy Joynson-Hicks ◽  
Chairat Uthaipibull ◽  
...  

ABSTRACT Antibodies to the C terminus of the Plasmodium falciparum merozoite surface protein, PfMSP-119, may inhibit merozoite invasion or block the effects of inhibitory antibodies. Here, using a competition enzyme-linked immunosorbent assay and antibody binding to wild-type and mutated recombinant proteins, we show that there are marked variations between individuals in the fine specificity of naturally acquired anti-MSP-119 antibodies. Furthermore, although neither the prevalence nor the concentration of total anti-MSP-119 antibodies was associated with resistance to malaria in African children, significant associations were observed between antibody fine specificity and subsequent risk of infection and high-density parasitemia during a follow-up period. Thus, the fine specificity of naturally acquired human anti-MSP-119 antibodies is crucial in determining their function. Future field studies, including the evaluation of PfMSP-1 vaccine trials, should include assays that explore antibody fine specificity as well as titer.

2005 ◽  
Vol 73 (2) ◽  
pp. 1235-1238 ◽  
Author(s):  
Subhash Singh ◽  
Soe Soe ◽  
Christian Roussilhon ◽  
Giampietro Corradin ◽  
Pierre Druilhe

ABSTRACT Plasmodium falciparum MSP6 is a merozoite surface antigen that shows organization and sequence homologies similar to those of MSP3. Within its C-terminus conserved region, it presents some epitopes that are cross-reactive with MSP3 and others that are not, both being targets of naturally occurring antibodies that block the P. falciparum erythrocytic cycle in cooperation with monocytes.


2010 ◽  
Vol 9 (1) ◽  
pp. 287 ◽  
Author(s):  
Josiane Ngoundou-Landji ◽  
Roseangela I Nwuba ◽  
Chiaka I Anumudu ◽  
Alexander B Odaibo ◽  
Wenceslas D Matondo Maya ◽  
...  

2005 ◽  
Vol 73 (7) ◽  
pp. 3912-3922 ◽  
Author(s):  
Damien R. Drew ◽  
Paul R. Sanders ◽  
Brendan S. Crabb

ABSTRACT To date, the following seven glycosylphosphatidylinositol (GPI)-anchored merozoite antigens have been described in Plasmodium falciparum: merozoite-associated surface protein 1 (MSP-1), MSP-2, MSP-4, MSP-5, MSP-8, MSP-10, and the rhoptry-associated membrane antigen. Of these, MSP-1, MSP-8, and MSP-10 possess a double epidermal growth factor (EGF)-like domain at the C terminus, and these modules are considered potential targets of protective immunity. In this study, we found that surprisingly, P. falciparum MSP-8 is transcribed and translated in the ring stage and is absent from the surface of merozoites. MSP-8 is the only GPI-anchored protein known to be expressed at this time. It is synthesized as a mature 80-kDa protein which is rapidly processed to a C-terminal 17-kDa species that contains the double EGF module. As determined by a combination of immunofluorescence and membrane purification approaches, it appears likely that MSP-8 initially localizes to the parasite plasma membrane in the ring stage. Although the C-terminal 17-kDa fragment is present in more mature stages, at these times it is found in the food vacuole. We successfully disrupted the MSP-8 gene in P. falciparum, a process that validated the specificity of the antibodies used in this study and also demonstrated that MSP-8 does not play a role essential to maintenance of the erythrocyte cycle. This finding, together with the observation that MSP-8 is exclusively intracellular, casts doubt over the viability of this antigen as a vaccine. However, it is still possible that MSP-8 is involved in an early parasitophorous vacuole function that is significant for pathogenesis in the human host.


2009 ◽  
Vol 166 (2) ◽  
pp. 159-171 ◽  
Author(s):  
Christopher G. Adda ◽  
Vince J. Murphy ◽  
Margaret Sunde ◽  
Lynne J. Waddington ◽  
Jesse Schloegel ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document